@article {pmid113918,
year = {1979},
author = {Pinevich, AV and Desnitskiĭ, AG},
title = {[Evolutionary origin of cell organelles].},
journal = {Tsitologiia},
volume = {21},
number = {7},
pages = {755-767},
pmid = {113918},
issn = {0041-3771},
mesh = {Aerobiosis ; Anaerobiosis ; *Biological Evolution ; Cell Compartmentation ; Chloroplasts/metabolism ; Clone Cells/ultrastructure ; Cyanobacteria/metabolism ; Cytogenetics ; Energy Metabolism ; Eukaryotic Cells/ultrastructure ; Mitochondria/metabolism ; Organoids/physiology/*ultrastructure ; Oxygen Consumption ; Phenotype ; Photosynthesis ; Phylogeny ; Symbiosis ; },
abstract = {A review on the evolutionary origin of the energy-yielding eukaryotic organelles is presented. Current autogenetic (endogenous compartmentalization) schemes, as well as different variants of symbiogenesis, are critically envisaged. A new symbiogenetic scheme is put forth, according to which mitochondria and chloroplasts originated divergently from a primordial photosynthetic organelle; the latter was acquired by endosymbiosis of ancient cyanobacteria in the cells of protoeukaryotes.},
}

Aerobiosis
Anaerobiosis
*Biological Evolution
Cell Compartmentation
Chloroplasts/metabolism
Clone Cells/ultrastructure
Cyanobacteria/metabolism
Cytogenetics
Energy Metabolism
Eukaryotic Cells/ultrastructure
Mitochondria/metabolism
Organoids/physiology/*ultrastructure
Oxygen Consumption
Phenotype
Photosynthesis
Phylogeny
Symbiosis

@article {pmid125189,
year = {1975},
author = {Lipmann, F},
title = {The roots of bioenergetics.},
journal = {Ciba Foundation symposium},
volume = {},
number = {31},
pages = {3-22},
doi = {10.1002/9780470720134.ch2},
pmid = {125189},
issn = {0300-5208},
mesh = {Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Biochemistry/*history ; Biological Evolution ; Creatine/metabolism ; Cytochromes/metabolism ; *Energy Metabolism ; Fermentation ; Flavoproteins/metabolism ; Fructosephosphates/metabolism ; Glyceric Acids/metabolism ; Glycolysis ; History, 20th Century ; Membrane Potentials ; Microscopy, Electron ; Mitochondria/ultrastructure ; Muscle Contraction ; Myosin Subfragments/metabolism ; Nucleotides/metabolism ; Oxidative Phosphorylation ; Phosphates/metabolism ; Photophosphorylation ; Pyridines/metabolism ; Pyruvates/metabolism ; Thermodynamics ; },
abstract = {Understanding metabolic energy transformation began with the realization of an 'intrusion' of phosphate into the mechanism of alcoholic fermentation. The discovery of an analogous participation of phosphate in muscle glycolysis connected the metabolic generation of energy-rich phosphate bonds fed into a common transmitter, adenosine triphosphate (ATP), with the production of mechanical energy through the finding that the phosphoryl group of creatine phosphate transferred to ATP could supply the energy for muscle contraction. In this way, a functional applicability of the energy of the phosphate bond was first shown. This observation was soon followed by the recognition that the phosphoanhydride bond of ATP provided the driving force in biosynthetic reactions; in this type of bond, metabolic energy apparently collects before it is transmitted for functional and biosynthetic use. The storage of energy in ATP was first detected in anaerobic energy-yielding reactions but soon was also found in respiratory and photosynthetic energy production. However, the mechanism by which energy derived from metabolites was converted into phosphate-bond energy in the latter processes appeared to differ from that of anaerobic energy transmission. Whereas phosphorylated compounds mediate the latter in homogeneous solutions, aerobic phosphorylation and photophosphorylation in prokaryotes seem to require special submembranous structures; and in eukaryotes, energy conversion is a function of special organelles, the mitochondria and chloroplasts. The evolutionary aspects of the transition from prokaryotes to eukaryotes are of considerable interest. In conclusion, the relevance of an apparent prokaryotic origin of the energy-transforming organelles in the eukaryotes will be commented on.},
}

Adenosine Triphosphatases/metabolism
Adenosine Triphosphate/metabolism
Biochemistry/*history
Biological Evolution
Creatine/metabolism
Cytochromes/metabolism
*Energy Metabolism
Fermentation
Flavoproteins/metabolism
Fructosephosphates/metabolism
Glyceric Acids/metabolism
Glycolysis
History, 20th Century
Membrane Potentials
Microscopy, Electron
Mitochondria/ultrastructure
Muscle Contraction
Myosin Subfragments/metabolism
Nucleotides/metabolism
Oxidative Phosphorylation
Phosphates/metabolism
Photophosphorylation
Pyridines/metabolism
Pyruvates/metabolism
Thermodynamics

@article {pmid274302,
year = {1978},
author = {Cannon, B and Nedergaard, J},
title = {Energy dissipation in brown fat.},
journal = {Experientia. Supplementum},
volume = {32},
number = {},
pages = {107-111},
doi = {10.1007/978-3-0348-5559-4_12},
pmid = {274302},
issn = {0071-335X},
mesh = {Adenosine Triphosphate/biosynthesis ; Adipose Tissue, Brown/drug effects/*metabolism/ultrastructure ; Amino Acids/biosynthesis ; Animals ; Carbon Dioxide/pharmacology ; Citric Acid Cycle ; Cricetinae ; *Energy Metabolism/drug effects ; Fatty Acids/metabolism ; In Vitro Techniques ; Mitochondria/metabolism ; Norepinephrine/pharmacology ; Oxygen Consumption/drug effects ; },
abstract = {Heat evolution in isolated brown fat cells has been measured by microcalorimetry. Thermogenesis (= oxygen consumption) is enhanced in the presence of CO2. This effect is probably due to pyruvate carboxylase activity which will increase the mitochondrial concentration of oxaloacetate. Oxaloacetate serves as condensing partner for acetyl-CoA coming from fatty acid oxidation. The high rate of oxygen consumption is impossible in cells when mitochondrial respiration is coupled to ATP synthesis, due to low amounts of ATP synthetase enzyme. A loosening of coupling is therefore required. This is possibly facilitated by acyl-CoA.},
}

Adenosine Triphosphate/biosynthesis
Adipose Tissue, Brown/drug effects/*metabolism/ultrastructure
Amino Acids/biosynthesis
Animals
Carbon Dioxide/pharmacology
Citric Acid Cycle
Cricetinae
*Energy Metabolism/drug effects
Fatty Acids/metabolism
In Vitro Techniques
Mitochondria/metabolism
Norepinephrine/pharmacology
Oxygen Consumption/drug effects

@article {pmid1041247,
year = {1975},
author = {},
title = {Mitochondria, chloroplasts, and energy transfer: a discussion.},
journal = {Ciba Foundation symposium},
volume = {},
number = {31},
pages = {63-68},
pmid = {1041247},
issn = {0300-5208},
mesh = {Adenosine Triphosphate/metabolism ; Bacteria/metabolism ; Biological Evolution ; Biological Transport, Active ; Chloroplasts/*metabolism ; Cytosol/metabolism ; Energy Metabolism ; Energy Transfer ; Enzyme Induction ; Ions/metabolism ; Membranes/metabolism ; Mitochondria/*metabolism ; Oxidative Phosphorylation ; Oxygen/pharmacology ; Photosynthesis ; },
}

Adenosine Triphosphate/metabolism
Bacteria/metabolism
Biological Evolution
Biological Transport, Active
Chloroplasts/*metabolism
Cytosol/metabolism
Energy Metabolism
Energy Transfer
Enzyme Induction
Ions/metabolism
Membranes/metabolism
Mitochondria/*metabolism
Oxidative Phosphorylation
Oxygen/pharmacology
Photosynthesis

@article {pmid1292665,
year = {1992},
author = {Müller, M},
title = {Energy metabolism of ancestral eukaryotes: a hypothesis based on the biochemistry of amitochondriate parasitic protists.},
journal = {Bio Systems},
volume = {28},
number = {1-3},
pages = {33-40},
doi = {10.1016/0303-2647(92)90005-j},
pmid = {1292665},
issn = {0303-2647},
support = {AI 11942/AI/NIAID NIH HHS/United States ; RR 07065/RR/NCRR NIH HHS/United States ; },
mesh = {Animals ; Biological Evolution ; Energy Metabolism ; Entamoeba histolytica/metabolism ; Eukaryotic Cells/*metabolism ; Giardia lamblia/metabolism ; Mitochondria/metabolism ; Models, Biological ; Trichomonas vaginalis/metabolism ; },
abstract = {Parasitic amitochondriate protists, representatives of early branches of eukaryote evolution, differ considerably in their central, energy metabolism from mitochondrion-bearing cells. These differences are: significant metabolic functions of inorganic pyrophosphate, major role of iron-sulfur proteins in key metabolic steps and in hydrogenosome-bearing organisms the disposal of electrons by H2 formation. Cytochrome-mediated electron transport and electron transport-linked phosphorylation are absent. All proteins which have been sequenced so far were found to be homologous to isofunctional proteins from other organisms. A few reactions, however, are catabolized by proteins which are not homologous to enzymes performing similar reactions in other eukaryotes. Two significantly different types of metabolism of amitochondriate protists can be distinguished: (a) without compartmentation and (b) with cytosol/hydrogenosome compartmentation. It is likely that these metabolic types have conserved certain traits present in ancestral eukaryotes before mitochondria became established.},
}

Animals
Biological Evolution
Energy Metabolism
Entamoeba histolytica/metabolism
Eukaryotic Cells/*metabolism
Giardia lamblia/metabolism
Mitochondria/metabolism
Models, Biological
Trichomonas vaginalis/metabolism

@article {pmid1390679,
year = {1992},
author = {Lewandowski, ED},
title = {Metabolic heterogeneity of carbon substrate utilization in mammalian heart: NMR determinations of mitochondrial versus cytosolic compartmentation.},
journal = {Biochemistry},
volume = {31},
number = {37},
pages = {8916-8923},
doi = {10.1021/bi00152a031},
pmid = {1390679},
issn = {0006-2960},
mesh = {Alanine/metabolism ; Animals ; Carbon/*metabolism ; Cell Compartmentation ; Cytosol/metabolism ; Energy Metabolism ; Glutamates/metabolism ; Lactates/metabolism ; Magnetic Resonance Spectroscopy ; Mitochondria, Heart/*metabolism ; Myocardial Contraction ; Myocardium/*metabolism ; Pyruvates/metabolism ; Rabbits ; },
abstract = {Carbon-13 (13C) nuclear magnetic resonance (NMR) spectroscopy can be used to target specific pathways of intermediary metabolism within intact tissues and was employed in this study to evaluate the compartmentation of pyruvate metabolism between the cytosol and mitochondrial matrix. The distribution of 13C into the tissue alanine, lactate, and glutamate pools was evaluated during metabolism of [3-13C]-pyruvate in intact, isolated perfused rabbit hearts with and without activation of pyruvate dehydrogenase activity by dichloroacetate (5 mM). Equilibrium between the intracellular alanine and pyruvate pools was in evidence from the rapid evolution of the steady-state 13C signal arising from the 3-carbon of alanine in intact hearts perfused with 2.5 mM 99.4% [3-13C]pyruvate. Augmented pyruvate oxidation, in response to perfusion with dichloroacetate, was evident within 13C NMR spectra of intact hearts as a relative increase in signal intensity of 53-62% (p less than 0.05) from the 4-carbon resonance of 13C-enriched glutamate when compared to the unaffected alanine signal. The increased bulk flow of [3-13C]pyruvate into the tricarboxylic acid cycle in response to dichloroacetate resulted in elevated fractional enrichment of glutamate from 68% in controls to 83% in the treated group (p less than 0.04), via interconversion with alpha-ketoglutarate, without changes in the actual tissue content of glutamate. Evidence of metabolic heterogeneity of cytosolic and mitochondrial pyruvate pools was also obtained from analysis of tissue extracts with in vitro NMR spectroscopy.(ABSTRACT TRUNCATED AT 250 WORDS)},
}

Alanine/metabolism
Animals
Carbon/*metabolism
Cell Compartmentation
Cytosol/metabolism
Energy Metabolism
Glutamates/metabolism
Lactates/metabolism
Magnetic Resonance Spectroscopy
Mitochondria, Heart/*metabolism
Myocardial Contraction
Myocardium/*metabolism
Pyruvates/metabolism
Rabbits

@article {pmid1462374,
year = {1992},
author = {Makhmudov, ES and Alimukhamedov, AA and Akhmerov, RI and Babaeva, RN and Baratova, GKh},
title = {[Effect of hyperglycemia and hyperthermia on liver mitochondrial respiration and blood glucose content of rats during postnatal ontogenesis].},
journal = {Ukrainskii biokhimicheskii zhurnal (1978)},
volume = {64},
number = {5},
pages = {77-82},
pmid = {1462374},
issn = {0201-8470},
mesh = {Animals ; Animals, Newborn/growth & development/*metabolism ; Blood Glucose/*metabolism ; Body Temperature/*physiology ; Caprylates/metabolism ; Hyperglycemia/blood/*metabolism ; Malates/metabolism ; Mitochondria, Liver/*metabolism ; Oxygen Consumption/*physiology ; Pyruvates/metabolism ; Pyruvic Acid ; Rats ; Rats, Wistar ; Succinates/metabolism ; Succinic Acid ; },
abstract = {Correlation between glucose level in blood and liver mitochondrial energetics of 1, 10, 20-days rats under hyperglycemia and high environmental temperature (38 degrees C) has been studied. Glucose feeding led to a significant increase of glucose content in blood, this increase being less at hyperthermia. Glucose feeding strengthened the oxidation of such intermediates as succinate (Krebs cycle), pyruvate and malate (hydrocarbonates) and caprylate (lipid). High environmental temperature with hyperglycemia suppresses the liver mitochondria breathing, hydrocarbon and lipid intermediates being used; the suppression is less in the presence of succinate. It is found that liver mitochondria of growing rats at different experimental conditions oxidize different intermediates with various rates. These data can be explained in the light of ontogenetic evolution of the energetic apparatus. It is supposed that exogenic glucose is the factor which activates growing processes of animals and to certain extent diminishes the negative influence of hyperthermia on the organism.},
}

Animals
Animals, Newborn/growth & development/*metabolism
Blood Glucose/*metabolism
Body Temperature/*physiology
Caprylates/metabolism
Hyperglycemia/blood/*metabolism
Malates/metabolism
Mitochondria, Liver/*metabolism
Oxygen Consumption/*physiology
Pyruvates/metabolism
Pyruvic Acid
Rats
Rats, Wistar
Succinates/metabolism
Succinic Acid

@article {pmid1794596,
year = {1991},
author = {Bolgiano, B and Davies, HC and Poole, RK},
title = {Using the bacterium, Paracoccus denitrificans and other 'runaway mitochondria' as classroom models for respiratory electron transport studies.},
journal = {Biochemical Society transactions},
volume = {19},
number = {4},
pages = {976-981},
doi = {10.1042/bst0190976a},
pmid = {1794596},
issn = {0300-5127},
mesh = {Biological Evolution ; Biology/*education ; *Electron Transport ; Energy Metabolism ; Escherichia coli/metabolism ; Mitochondria/metabolism ; Paracoccus denitrificans/*metabolism ; },
abstract = {Our suggestions for experiments demonstrating electron-transport-chain composition and reactions all exploit bacteria which can be prepared quickly, easily and cheaply from cells grown in Erlenmeyer flasks. While they have been designed from a cytochrome oxidase point of view using organisms of our own prejudice, strains containing mutations in other sites could be just as educational. Most bacteria that can grow aerobically have features in common with the mitochondrial respiratory chain. Because of the vital importance of oxygen utilization throughout most of evolution, and consequent conservation of electron-transport complexes and carriers, the teaching of bioenergetics, whether in the laboratory or lecture room, could benefit from the inclusion of micro-organisms in the curriculum.},
}

Biological Evolution
Biology/*education
*Electron Transport
Energy Metabolism
Escherichia coli/metabolism
Mitochondria/metabolism
Paracoccus denitrificans/*metabolism

@article {pmid1823597,
year = {1991},
author = {Henderson, PJ},
title = {Studies of translocation catalysis.},
journal = {Bioscience reports},
volume = {11},
number = {6},
pages = {477-53; discussion 534-8},
doi = {10.1007/BF01130216},
pmid = {1823597},
issn = {0144-8463},
support = {//Wellcome Trust/United Kingdom ; },
mesh = {Amino Acid Sequence ; Biological Transport, Active ; *Catalysis ; Energy Metabolism ; Molecular Sequence Data ; Osmosis ; Sequence Homology, Nucleic Acid ; },
abstract = {There is a symbiotic relationship between the evolution of fundamental theory and the winning of experimentally-based knowledge. The impact of the General Chemiosmotic Theory on our understanding of the nature of membrane transport processes is described and discussed. The history of experimental studies on transport catalysed by ionophore antibiotics and the membrane proteins of mitochondria and bacteria are used to illustrate the evolution of knowledge and theory. Recent experimental approaches to understanding the lactose-H+ symport protein of Escherichia coli and other sugar porters are described to show that the lack of experimental knowledge of the three-dimensional structures of the proteins currently limits the development of theories about their molecular mechanism of translocation catalysis.},
}

Amino Acid Sequence
Biological Transport, Active
*Catalysis
Energy Metabolism
Molecular Sequence Data
Osmosis
Sequence Homology, Nucleic Acid

@article {pmid1850242,
year = {1991},
author = {Brand, MD and Couture, P and Else, PL and Withers, KW and Hulbert, AJ},
title = {Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile.},
journal = {The Biochemical journal},
volume = {275 (Pt 1)},
number = {Pt 1},
pages = {81-86},
pmid = {1850242},
issn = {0264-6021},
mesh = {Adenosine Triphosphate/biosynthesis ; Animals ; *Biological Evolution ; *Energy Metabolism ; Fatty Acids/analysis ; Intracellular Membranes/chemistry/metabolism ; Kinetics ; Lizards/*metabolism ; Membrane Lipids/analysis ; Membrane Potentials ; Mitochondria, Liver/*metabolism/ultrastructure ; Permeability ; *Protons ; Rats ; },
abstract = {Standard metabolic rate is 7-fold greater in the rat (a typical mammal) than in the bearded dragon, Amphibolurus vitticeps (a reptile with the same body mass and temperature). Rat hepatocytes respire 4-fold faster than do hepatocytes from the lizard. The inner membrane of isolated rat liver mitochondrial has a proton permeability that is 4-5-fold greater than the proton permeability of the lizard liver mitochondrial membrane per mg of mitochondrial protein. The greater permeability of rat mitochondria is not caused by differences in the surface area of the mitochondrial inner membrane, but differences in the fatty acid composition of the mitochondrial phospholipids may be involved in the permeability differences. Greater proton permeability of the mitochondrial inner membrane may contribute to the greater standard metabolic rate of mammals.},
}

Adenosine Triphosphate/biosynthesis
Animals
*Biological Evolution
*Energy Metabolism
Fatty Acids/analysis
Intracellular Membranes/chemistry/metabolism
Kinetics
Lizards/*metabolism
Membrane Lipids/analysis
Membrane Potentials
Mitochondria, Liver/*metabolism/ultrastructure
Permeability
*Protons
Rats

@article {pmid2508761,
year = {1989},
author = {},
title = {Bioenergetic systems, structure control and evolution. Autumn congress. (Sept. 28-30, 1988, Bombannes, France). Proceedings.},
journal = {Biochimie},
volume = {71},
number = {8},
pages = {877-979},
pmid = {2508761},
issn = {0300-9084},
mesh = {Animals ; Biological Transport ; *Energy Metabolism ; Mitochondria/*metabolism ; Yeasts/*metabolism ; },
}

Animals
Biological Transport
*Energy Metabolism
Mitochondria/*metabolism
Yeasts/*metabolism

@article {pmid2554073,
year = {1989},
author = {Villa, RF and Gorini, A and Geroldi, D and Lo Faro, A and Dell'Orbo, C},
title = {Enzyme activities in perikaryal and synaptic mitochondrial fractions from rat hippocampus during development.},
journal = {Mechanisms of ageing and development},
volume = {49},
number = {3},
pages = {211-225},
doi = {10.1016/0047-6374(89)90072-9},
pmid = {2554073},
issn = {0047-6374},
mesh = {Age Factors ; Animals ; Citrate (si)-Synthase/metabolism ; Electron Transport Complex IV/metabolism ; Energy Metabolism ; Female ; Glutamate Dehydrogenase/metabolism ; Hippocampus/*enzymology/growth & development ; In Vitro Techniques ; Malate Dehydrogenase/metabolism ; Mitochondria/*enzymology ; NADH Dehydrogenase/metabolism ; Rats ; Rats, Inbred Strains ; Synapses/enzymology ; },
abstract = {When pharmacological or basic neurochemical systematic characterization of mitochondrial enzymatic systems correlated to energy transduction processes is attempted, studies must be based on subcellular fractions with a high degree of purity from specific brain areas and from individual animals. Distinct populations of mitochondria heterogenous with respect to biochemical enzyme characteristics from rat brain hippocampus are described. Two mitochondrial populations were derived from synaptosomes by lysis and a third consists of free non-synaptic mitochondria. The maximum rate of some cerebral enzyme activities which are part of energy transduction (citrate synthase, malate dehydrogenase; total NADH-cytochrome c reductase, cytochrome oxidase) and amino acid metabolism (glutamate dehydrogenase) were tested on these mitochondrial populations of 8- and 16-week-old rats. A comprehensive analysis of the data suggests that extensive but highly diversified catalytic expressions of the enzymes studied occur in the hippocampus. This is true even when a short period of the rat life span is studied. Hence the varying pattern of evolution of the differing cerebral mitochondria, probably a consequence of different metabolic functions, should be taken into account in any pharmacological study on these systems.},
}

Age Factors
Animals
Citrate (si)-Synthase/metabolism
Electron Transport Complex IV/metabolism
Energy Metabolism
Female
Glutamate Dehydrogenase/metabolism
Hippocampus/*enzymology/growth & development
In Vitro Techniques
Malate Dehydrogenase/metabolism
Mitochondria/*enzymology
NADH Dehydrogenase/metabolism
Rats
Rats, Inbred Strains
Synapses/enzymology

@article {pmid2710162,
year = {1989},
author = {Campbell, T and Rubin, N and Komuniecki, R},
title = {Succinate-dependent energy generation in Ascaris suum mitochondria.},
journal = {Molecular and biochemical parasitology},
volume = {33},
number = {1},
pages = {1-12},
doi = {10.1016/0166-6851(89)90036-4},
pmid = {2710162},
issn = {0166-6851},
support = {AI18427/AI/NIAID NIH HHS/United States ; },
mesh = {Adenine Nucleotides/metabolism ; Animals ; Ascaris/*metabolism ; *Energy Metabolism ; Ferricyanides/pharmacology ; Hydrogen Peroxide/pharmacology ; Malates/metabolism ; Mitochondria/*metabolism ; Models, Biological ; Phosphorylation ; Succinates/*metabolism ; Succinic Acid ; },
abstract = {Phosphorylation in isolated Ascaris suum mitochondria was much greater in the presence of malate than succinate, but, in the absence of added adenine nucleotides, incubations in succinate resulted in substantial elevations in intramitochondrial ATP levels. Succinate-dependent phosphorylation was stimulated aerobically and this stimulation was due almost entirely to a site I, rotenone-sensitive, phosphorylation. Increased substrate level phosphorylation, coupled to propionate formation, or additional sites of electron-transport associated ATP synthesis were not significant. Under aerobic conditions, 14CO2 evolution from 1,4-[14C]succinate was stimulated and NADH/NAD+ ratios were elevated, but the formation of [14C]propionate was unchanged. It appears that succinate was metabolized to pyruvate and acetate, and NADH, generated from the decarboxylations of malate and pyruvate, was the primary source of reducing power fueling electron-transport. The terminal oxidase and final electron-acceptor are still not clearly defined. However, ferricyanide, H2O2, and 100% oxygen all stimulated succinate-dependent phosphorylation. A possible role for cytochrome c peroxidase in A. suum mitochondrial metabolism is discussed.},
}

Adenine Nucleotides/metabolism
Animals
Ascaris/*metabolism
*Energy Metabolism
Ferricyanides/pharmacology
Hydrogen Peroxide/pharmacology
Malates/metabolism
Mitochondria/*metabolism
Models, Biological
Phosphorylation
Succinates/*metabolism
Succinic Acid

@article {pmid3059999,
year = {1988},
author = {Müller, M},
title = {Energy metabolism of protozoa without mitochondria.},
journal = {Annual review of microbiology},
volume = {42},
number = {},
pages = {465-488},
doi = {10.1146/annurev.mi.42.100188.002341},
pmid = {3059999},
issn = {0066-4227},
mesh = {Anaerobiosis ; Animals ; Biological Evolution ; Decarboxylation ; Electron Transport ; *Energy Metabolism ; Eukaryota/*metabolism ; Glycolysis ; Mitochondria/metabolism ; Pyruvates/metabolism ; },
}

Anaerobiosis
Animals
Biological Evolution
Decarboxylation
Electron Transport
*Energy Metabolism
Eukaryota/*metabolism
Glycolysis
Mitochondria/metabolism
Pyruvates/metabolism

@article {pmid3555260,
year = {1986},
author = {Coleman, PS},
title = {Membrane cholesterol and tumor bioenergetics.},
journal = {Annals of the New York Academy of Sciences},
volume = {488},
number = {},
pages = {451-467},
doi = {10.1111/j.1749-6632.1986.tb46578.x},
pmid = {3555260},
issn = {0077-8923},
support = {CA28677/CA/NCI NIH HHS/United States ; },
mesh = {Animals ; Cholesterol/*metabolism ; Citrates/metabolism ; Citric Acid ; Citric Acid Cycle ; *Energy Metabolism ; Liver Neoplasms, Experimental/*metabolism ; Membrane Lipids/*metabolism ; Mitochondria, Liver/metabolism ; Rats ; },
abstract = {We have established that a preferential export of pyruvate-generated citrate occurs from cholesterol-rich tumor mitochondria, with both isolated mitochondrial systems as well as with viable tumor tissue slices (i.e., with whole tumors cells). Furthermore, we have demonstrated that the more rapid citrate efflux kinetics (catalyzed by the tricarboxylate exchange carrier) of isolated tumor mitochondria is completely inhibited upon addition of 1,2,3-benzenetricarboxylate (BTC) and have shown that this inhibition is apparently also obtained in viable tumor tissue when the inhibitor is added to the tissue incubation. Upon BTC inhibition of tumor mitochondrial citrate export in viable tumor tissue incubations, the incorporation of [14C]pyruvate into newly synthesized cholesterol is severely inhibited as well. Among the most interesting conclusions drawn from our results, we catalog the following. The preferential export of citrate from isolated tumor mitochondria appears to be coupled, functionally, to a high linear rate of incorporation of 14C from pyruvate to cholesterol in viable tumor tissue slices, simultaneously supporting the postulate of a truncated Krebs cycle and corroborating the well-established deregulated and continuous cholesterogenesis pathway in tumors, especially hepatomas. The extent of [14C]pyruvate flux to newly generated cholesterol in either tumor or normal liver tissue is inversely related to the extent of 14CO2 production. Despite the evolution of some CO2 during cholesterogenesis, the predominant portion presumably arises via metabolic processing of pyruvate-generated citrate during Krebs cycle-linked respiration. Isolated tumor mitochondrial systems, as well as viable tumor tissue incubations, can manifest a reversal in the pattern of enhanced mitochondrial citrate efflux coupled to increased cholesterogenesis, when BTC is added to the system. This implies that BTC, a hydrophobic but negatively charged moiety at pH 7, can indeed penetrate the plasma membrane of cells. Upon entry into the cell, BTC apparently blocks the tricarboxylate carrier of tumor tissue mitochondria, thus forcing the mitochondrial citrate into Krebs cycle-linked respiration rather than permitting it to serve as the predominant provider of an increased supply of cytosolic acetyl CoA precursor required for deregulated cholesterogenesis during the development of the tumor.},
}

Animals
Cholesterol/*metabolism
Citrates/metabolism
Citric Acid
Citric Acid Cycle
*Energy Metabolism
Liver Neoplasms, Experimental/*metabolism
Membrane Lipids/*metabolism
Mitochondria, Liver/metabolism
Rats

@article {pmid3908651,
year = {1985},
author = {Enoki, Y},
title = {[Physiological mechanisms for effective utilization of ambient oxygen--with a special relevance to its phylogenetic aspects and exercise].},
journal = {Nihon seirigaku zasshi. Journal of the Physiological Society of Japan},
volume = {47},
number = {7},
pages = {268-278},
pmid = {3908651},
issn = {0031-9341},
mesh = {Adenosine Triphosphate/biosynthesis ; Animals ; Biological Evolution ; Capillaries/anatomy & histology ; Cats ; Dogs ; Energy Metabolism ; Erythrocytes/metabolism ; Fishes ; Guinea Pigs ; Hemoglobins/metabolism/physiology ; Mice ; Microcirculation ; Mitochondria/metabolism/ultrastructure ; Muscles/blood supply ; Myoglobin/physiology ; Oxygen/blood/*physiology ; Rabbits ; Rats ; Reptiles ; },
}

Adenosine Triphosphate/biosynthesis
Animals
Biological Evolution
Capillaries/anatomy & histology
Cats
Dogs
Energy Metabolism
Erythrocytes/metabolism
Fishes
Guinea Pigs
Hemoglobins/metabolism/physiology
Mice
Microcirculation
Mitochondria/metabolism/ultrastructure
Muscles/blood supply
Myoglobin/physiology
Oxygen/blood/*physiology
Rabbits
Rats
Reptiles

@article {pmid6264827,
year = {1981},
author = {Whatley, FR},
title = {The establishment of mitochondria: Paracoccus and Rhodopseudomonas.},
journal = {Annals of the New York Academy of Sciences},
volume = {361},
number = {},
pages = {330-340},
doi = {10.1111/j.1749-6632.1981.tb46529.x},
pmid = {6264827},
issn = {0077-8923},
mesh = {Biological Evolution ; Cytochrome c Group/metabolism ; Electron Transport ; *Mitochondria/metabolism ; *Paracoccus/metabolism ; *Rhodobacter sphaeroides/metabolism ; *Symbiosis ; },
abstract = {Many aerobic bacteria (both facultative and obligate) possess a number of those biochemical features of mitochondria which are concerned with energy metabolism. However, only restricted number, notably Paracoccus denitrificans and Rhodopseudomonas spheroides, have the majority of these features. The theory of endosymbiosis proposes that a primitive eukaryote took up bacteria to yield mitochondria. The present-day Paracoccus then resembles the ancestral bacterium in many respects the primitive amoeba, Pelomyxa palustris, which lacks mitochondria but contains a permanent population of unique symbiotic bacteria, has many of the characteristics of a present-day transitional form. The evolution of mitochondria from endosymbiotic bacteria would involve their integration with the host cell both biochemically and structurally: a number of the intermediate steps are discussed. Attention is drawn to the existence in some ciliates of hydrogenosomes, which function as anaerobic mitochondria.},
}

Biological Evolution
Cytochrome c Group/metabolism
Electron Transport
*Mitochondria/metabolism
*Paracoccus/metabolism
*Rhodobacter sphaeroides/metabolism
*Symbiosis

@article {pmid6268221,
year = {1981},
author = {Harris, DA},
title = {The coupling ATPase complex: an evolutionary view.},
journal = {Bio Systems},
volume = {14},
number = {1},
pages = {113-121},
doi = {10.1016/0303-2647(81)90026-5},
pmid = {6268221},
issn = {0303-2647},
mesh = {Adenosine Triphosphatases/*metabolism ; Amino Acid Sequence ; Bacteria/metabolism ; *Biological Evolution ; Energy Metabolism ; Ion Channels/metabolism ; Mitochondria/metabolism ; Oxidative Phosphorylation Coupling Factors/*metabolism ; Proton-Translocating ATPases/*metabolism ; Saccharomyces cerevisiae/enzymology ; },
abstract = {Phospholipid micelles and vesicles, present in the primordial soup, formed both primitive (surface) catalyst and primitive replicative life forms. With the adoption of a common energy source, ATP, integrated biochemical systems within these vesicles became possible - cells. Fermentation within these primitive cells was favoured by the evolution, first of ion channels allowing protons to leak out, and then of an active ATP-driven pump. In the prokaryotic/mitochondria/chloroplast line, the proton channel was such as to be blocked by dicyclohexylcarbodiimide and the adenosine 5' triphosphate phosphohydrolase (ATPase) by 4-chloro 7-nitrobenzofurazan (Nbf-C1). The ATPase was initially simple (4 subunits) but later, possibly concomitant with its evolution to an ATP synthetase, became more complex (8 subunits). One of the steps in evolution probably involved gene duplication and divergence of 2 subunits (alpha and beta) from the largest of the ATPase subunits. From this stage, the general form of the ATPase was fixed, although sensitivity to, for example, oligomycin involved later, after divergence of the mitochondrial and chloroplast lines. A regulatory protein, the ATPase inhibitor, is found associated with a wide spectrum of coupling ATPases.},
}

Adenosine Triphosphatases/*metabolism
Amino Acid Sequence
Bacteria/metabolism
*Biological Evolution
Energy Metabolism
Ion Channels/metabolism
Mitochondria/metabolism
Oxidative Phosphorylation Coupling Factors/*metabolism
Proton-Translocating ATPases/*metabolism
Saccharomyces cerevisiae/enzymology

@article {pmid6453255,
year = {1980},
author = {Wilson, TH and Lin, EC},
title = {Evolution of membrane bioenergetics.},
journal = {Journal of supramolecular structure},
volume = {13},
number = {4},
pages = {421-446},
doi = {10.1002/jss.400130403},
pmid = {6453255},
issn = {0091-7419},
support = {AM-05736/AM/NIADDK NIH HHS/United States ; GM-11983/GM/NIGMS NIH HHS/United States ; },
mesh = {Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Bacteria/metabolism ; *Biological Evolution ; Biological Transport ; Cell Membrane/*metabolism ; DNA/metabolism ; Energy Metabolism ; Hydrogen-Ion Concentration ; Mitochondria/metabolism ; Oxidation-Reduction ; Photosynthesis ; Plants/metabolism ; Potassium/metabolism ; Sodium/metabolism ; Vertebrates ; },
abstract = {One of the first problems encountered by primitive cells was that of volume regulation; the continuous entry of ions, (eg, NaCl) and water in response to the internal colloid osmotic pressure threatening to destroy the cell by lysis. We propose that to meet this environmental challenge cells evolved an ATP-driven proton extrusion system plus a membrane carrier that would exchange external protons with internal Na+. With the appearance of the ability to generate proton gradients, additional mechanisms to harness this source of energy emerged. These would include proton-nutrient cotransport, K+ accumulation, nucleic acid entry, and motility. A more efficient system for the uptake of certain carbohydrates by vectorial phosphorylation via the PEP-phosphotransferase system probably appeared rather early in the evolution of anaerobic bacteria. The reversal of the proton-ATPase reaction to give net ATP synthesis became possible with the development of other types of efficient proton transporting machinery. Either light-driven bacterial rhodopsin or a redox system coupled to proton translocation would have served this function. Oxidation of one substrate coupled to the reduction of another substrate by membrane-bound enzymes evolved in such a manner that protons were extruded from the cell during the reaction. The progressive elaboration of this type of redox proton pump permitted the use of exogenous electron acceptors, such as fumarate, sulfate, and nitrate. The stepwise growth of these electron transport chains required the accretion of several flavoproteins, iron-sulfur proteins, quinones, and cytochromes. With modifications of these four basic components a chlorophyll-dependent photosynthetic system was subsequently evolved. The oxygen that was generated by this photosynthetic system from water would eventually accumulate in the atmosphere of the earth. With molecular oxygen present, the emergence of cytochrome oxidase would complete the respiratory chain. The proton economy of membrane energetics has been retained by most present-day microorganisms, mitochondria, chloroplasts, and cells of higher plants. A secondary use of the energy stored as an electrochemical difference of Na+ for powering membrane events probably also evolved in microorganisms. The exclusive age of the Na+ economy is distinctive of the plasma membrane of animal cells; the Na+-K+ ATPase sets up an electrochemical Na+ gradient that provides the energy for osmoregulation, Na+-nutrient co-transport, and the action potential of excitable cells.},
}

Adenosine Triphosphatases/metabolism
Adenosine Triphosphate/metabolism
Animals
Bacteria/metabolism
*Biological Evolution
Biological Transport
Cell Membrane/*metabolism
DNA/metabolism
Energy Metabolism
Hydrogen-Ion Concentration
Mitochondria/metabolism
Oxidation-Reduction
Photosynthesis
Plants/metabolism
Potassium/metabolism
Sodium/metabolism
Vertebrates

@article {pmid6521672,
year = {1984},
author = {Setälä, K},
title = {Carcinogenesis--devolution towards an ancient nucleated pre-eukaryotic level.},
journal = {Medical hypotheses},
volume = {15},
number = {3},
pages = {209-230},
doi = {10.1016/0306-9877(84)90015-x},
pmid = {6521672},
issn = {0306-9877},
mesh = {Animals ; Biological Evolution ; Carcinogens/pharmacology ; Cell Differentiation ; Energy Metabolism ; Eukaryotic Cells/physiology ; Humans ; Mice ; Mitochondria/*physiology ; Mitosis ; Neoplasms/*pathology/physiopathology ; Precancerous Conditions/pathology ; Skin/drug effects ; Skin Neoplasms/etiology/pathology ; Water ; },
abstract = {Because the mitochondria and the cells housing them are obligatory symbionts, the evolutionary history of cells forms the locus minoris resistentiae which is the prerequisite for the carcinogenetic process. During carcinogenesis, the cells devolve towards an ancient anaerobic nucleated pre-eukaryotic level. True carcinogens cause an accumulation of inclusion bodies in the inner, bacterial, mitochondrial membrane. The mitochondrial damage which is detectable only in the early pretumorous stages, results in the respiratory surface with its enzymes being specifically changed, the mitochondrial and nuclear cycles no longer coinciding, the energy generation being forced to reuse the latent, "prehistoric", mode of respiration and the mitochondrial enzyme systems of soil bacterial origin becoming adapted to use other and more versatile metabolic pathways with a wider variety of end-products than classical glycolysis which produces lactate only. Neither external carcinogens nor oncogens are necessary. An increased, prolonged cell replication activity of physiological type is sufficient to initiate and maintain the process in animals with an inherited neoplastic disposition located in the inner mitochondrial membrane. The neoplastic disposition is inherited maternally: in fertilization the ovum does not receive mitochondria from the spermatocyte. The final results are an overall retardation of cell processes and instability in its structural and functional repertoire, the cytoskeleton (differentiation organelle) of the malignant cell manifesting special patterns. The proposed devolutionary mechanism is feasible as DNA packages are physiological components of soil bacterial membrane and can remain dormant (repressed) for years, or for ever, but under suitable conditions can generate seemingly new species, and particularly because enzyme adaptability is the unique privilege of soil bacteria.},
}

Animals
Biological Evolution
Carcinogens/pharmacology
Cell Differentiation
Energy Metabolism
Eukaryotic Cells/physiology
Humans
Mice
Mitochondria/*physiology
Mitosis
Neoplasms/*pathology/physiopathology
Precancerous Conditions/pathology
Skin/drug effects
Skin Neoplasms/etiology/pathology
Water

@article {pmid7272468,
year = {1981},
author = {Schiff, JA},
title = {Evolution of the control of pigment and plastid development in photosynthetic organisms.},
journal = {Bio Systems},
volume = {14},
number = {1},
pages = {123-147},
doi = {10.1016/0303-2647(81)90027-7},
pmid = {7272468},
issn = {0303-2647},
support = {GM14595/GM/NIGMS NIH HHS/United States ; },
mesh = {*Biological Evolution ; Chloroplasts/*metabolism ; Darkness ; Energy Metabolism ; Light ; Mitochondria/metabolism ; *Photosynthesis ; Pigments, Biological/*metabolism ; Plants/*metabolism ; Species Specificity ; },
abstract = {How do bioenergetic organelles relate to the cells they are in and how was this relationship established over the course of evolution? Plastids and mitochondria are viewed as prokaryotic residents in eukaryotic cells. These organelles are semiautonomous: they perpetuate themselves by division but regulate and are subject to regulation by the cell in which they are residents. Although these organelles are usually constitutive, their development is arrested in certain organisms when an inducing substrate is absent (light, for example, in the case of the chloroplast) with the formation of precursor organelles such as proplastids. Various trends in the evolution of photo-control systems are discussed including those concerned with photoperception and photomorphogenesis. The photocontrol of chloroplast development by blue and red light is discussed in relation to its possible evolutionary origins in a system for finding the right light for photosynthesis. Models for various types of cellular regulation by light during chloroplast development are discussed. Also considered is the evolution of plastid pigments in response to available light. A parallel evolution of accessory pigments and chlorophylls is suggested which led to chlorophyll reaction centers serving as energy sinks for light absorbed by accessory pigments and, therefore, having their absorptions pushed to the longest possible wavelengths as accessory pigments evolved to fill the middle of the spectrum in response to ecological selection. An endosymbiotic origin of bioenergetic organelles is suggested based on polyphyletic origins of chloroplasts from a number of oxygenic procaryotic precursors. The similarity between proplastids and these oxygenic procaryotes suggests that the original invading organelle may have resembled a modern proplastid rather than a mature chloroplast.},
}

*Biological Evolution
Chloroplasts/*metabolism
Darkness
Energy Metabolism
Light
Mitochondria/metabolism
*Photosynthesis
Pigments, Biological/*metabolism
Plants/*metabolism
Species Specificity

@article {pmid7554586,
year = {1995},
author = {Mitchell, GA and Kassovska-Bratinova, S and Boukaftane, Y and Robert, MF and Wang, SP and Ashmarina, L and Lambert, M and Lapierre, P and Potier, E},
title = {Medical aspects of ketone body metabolism.},
journal = {Clinical and investigative medicine. Medecine clinique et experimentale},
volume = {18},
number = {3},
pages = {193-216},
pmid = {7554586},
issn = {0147-958X},
mesh = {3-Hydroxybutyric Acid ; Acetoacetates/metabolism ; Acetone/metabolism ; Biological Evolution ; Brain/metabolism ; Humans ; Hydroxybutyrates/metabolism ; Hypoglycemia/*diagnosis/metabolism ; Ketone Bodies/biosynthesis/*metabolism ; Ketosis/*diagnosis/metabolism/therapy ; Menotropins/metabolism ; Metabolism, Inborn Errors/*diagnosis/metabolism/therapy ; Mitochondria, Liver/enzymology/metabolism ; },
abstract = {Ketone bodies are produced in the liver, mainly from the oxidation of fatty acids, and are exported to peripheral tissues for use as an energy source. They are particularly important for the brain, which has no other substantial non-glucose-derived energy source. The 2 main ketone bodies are 3-hydroxybutyrate (3HB) and acetoacetate (AcAc). Biochemically, abnormalities of ketone body metabolism can present in 3 fashions: ketosis, hypoketotic hypoglycemia, and abnormalities of the 3HB/AcAc ratio. Normally, the presence of ketosis implies 2 things: that lipid energy metabolism has been activated and that the entire pathway of lipid degradation is intact. In rare patients, ketosis reflects an inability to utilize ketone bodies. Ketosis is normal during fasting, after prolonged exercise, and when a high-fat diet is consumed. During the neonatal period, infancy and pregnancy, times at which lipid energy metabolism is particularly active, ketosis develops readily. Pathologic causes of ketosis include diabetes, ketotic hypoglycemia of childhood, corticosteroid or growth hormone deficiency, intoxication with alcohol or salicylates, and several inborn errors of metabolism. The absence of ketosis in a patient with hypoglycemia is abnormal and suggests the diagnosis of either hyperinsulinism or an inborn error of fat energy metabolism. An abnormal elevation of the 3HB/AcAc ratio usually implies a non-oxidized state of the hepatocyte mitochondrial matrix resulting from hypoxia-ischemia or other causes. We summarize the differential diagnosis of abnormalities of ketone body metabolism, as well as pertinent recent advances in research.},
}

3-Hydroxybutyric Acid
Acetoacetates/metabolism
Acetone/metabolism
Biological Evolution
Brain/metabolism
Humans
Hydroxybutyrates/metabolism
Hypoglycemia/*diagnosis/metabolism
Ketone Bodies/biosynthesis/*metabolism
Ketosis/*diagnosis/metabolism/therapy
Menotropins/metabolism
Metabolism, Inborn Errors/*diagnosis/metabolism/therapy
Mitochondria, Liver/enzymology/metabolism

@article {pmid7599200,
year = {1995},
author = {Wallace, DC and Shoffner, JM and Trounce, I and Brown, MD and Ballinger, SW and Corral-Debrinski, M and Horton, T and Jun, AS and Lott, MT},
title = {Mitochondrial DNA mutations in human degenerative diseases and aging.},
journal = {Biochimica et biophysica acta},
volume = {1271},
number = {1},
pages = {141-151},
doi = {10.1016/0925-4439(95)00021-u},
pmid = {7599200},
issn = {0006-3002},
support = {HL45572/HL/NHLBI NIH HHS/United States ; NS21328/NS/NINDS NIH HHS/United States ; NS30164/NS/NINDS NIH HHS/United States ; },
mesh = {Adult ; Aged ; Aging/*genetics ; Amino Acid Sequence ; Animals ; *Biological Evolution ; Child ; Conserved Sequence ; DNA, Mitochondrial/*genetics ; Energy Metabolism ; Female ; Humans ; Male ; Middle Aged ; Mitochondria/*metabolism ; Mitochondrial Myopathies/*genetics/metabolism ; Molecular Sequence Data ; *Mutation ; Nervous System Diseases/genetics/metabolism ; Optic Atrophies, Hereditary/*genetics/metabolism ; Oxidative Phosphorylation ; Pedigree ; *Point Mutation ; Sequence Homology, Amino Acid ; },
abstract = {A wide variety of mitochondrial DNA (mtDNA) mutations have recently been identified in degenerative diseases of the brain, heart, skeletal muscle, kidney and endocrine system. Generally, individuals inheriting these mitochondrial diseases are relatively normal in early life, develop symptoms during childhood, mid-life, or old age depending on the severity of the maternally-inherited mtDNA mutation; and then undergo a progressive decline. These novel features of mtDNA disease are proposed to be the product of the high dependence of the target organs on mitochondrial bioenergetics, and the cumulative oxidative phosphorylation (OXPHOS) defect caused by the inherited mtDNA mutation together with the age-related accumulation mtDNA mutations in post-mitotic tissues.},
}

Adult
Aged
Aging/*genetics
Amino Acid Sequence
Animals
*Biological Evolution
Child
Conserved Sequence
DNA, Mitochondrial/*genetics
Energy Metabolism
Female
Humans
Male
Middle Aged
Mitochondria/*metabolism
Mitochondrial Myopathies/*genetics/metabolism
Molecular Sequence Data
*Mutation
Nervous System Diseases/genetics/metabolism
Optic Atrophies, Hereditary/*genetics/metabolism
Oxidative Phosphorylation
Pedigree
*Point Mutation
Sequence Homology, Amino Acid

@article {pmid7971961,
year = {1994},
author = {Shigenaga, MK and Hagen, TM and Ames, BN},
title = {Oxidative damage and mitochondrial decay in aging.},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
volume = {91},
number = {23},
pages = {10771-10778},
pmid = {7971961},
issn = {0027-8424},
support = {CA39910/CA/NCI NIH HHS/United States ; ESO1896/ES/NIEHS NIH HHS/United States ; },
mesh = {*Aging ; Animals ; DNA, Mitochondrial/chemistry ; Electron Transport ; Energy Metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Immune System/metabolism ; Intracellular Membranes/chemistry ; Lipids/chemistry ; Longevity ; Mitochondria/*physiology ; Mutation ; Neurons/metabolism ; Oxidation-Reduction ; Phylogeny ; Proteins/chemistry ; Superoxides/metabolism ; },
abstract = {We argue for the critical role of oxidative damage in causing the mitochondrial dysfunction of aging. Oxidants generated by mitochondria appear to be the major source of the oxidative lesions that accumulate with age. Several mitochondrial functions decline with age. The contributing factors include the intrinsic rate of proton leakage across the inner mitochondrial membrane (a correlate of oxidant formation), decreased membrane fluidity, and decreased levels and function of cardiolipin, which supports the function of many of the proteins of the inner mitochondrial membrane. Acetyl-L-carnitine, a high-energy mitochondrial substrate, appears to reverse many age-associated deficits in cellular function, in part by increasing cellular ATP production. Such evidence supports the suggestion that age-associated accumulation of mitochondrial deficits due to oxidative damage is likely to be a major contributor to cellular, tissue, and organismal aging.},
}

*Aging
Animals
DNA, Mitochondrial/chemistry
Electron Transport
Energy Metabolism
Humans
Hydrogen Peroxide/metabolism
Immune System/metabolism
Intracellular Membranes/chemistry
Lipids/chemistry
Longevity
Mitochondria/*physiology
Mutation
Neurons/metabolism
Oxidation-Reduction
Phylogeny
Proteins/chemistry
Superoxides/metabolism

@article {pmid8132485,
year = {1993},
author = {Klingenberg, M},
title = {Dialectics in carrier research: the ADP/ATP carrier and the uncoupling protein.},
journal = {Journal of bioenergetics and biomembranes},
volume = {25},
number = {5},
pages = {447-457},
pmid = {8132485},
issn = {0145-479X},
mesh = {Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Adipose Tissue, Brown/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*physiology ; *Energy Metabolism ; Intracellular Membranes/*metabolism ; Ion Channels ; Mammals/metabolism ; Membrane Proteins/chemistry/*physiology ; Mitochondria/*metabolism ; Mitochondrial ADP, ATP Translocases/chemistry/*physiology ; Mitochondrial Proteins ; Molecular Sequence Data ; Phylogeny ; Protein Structure, Tertiary ; Protons ; Structure-Activity Relationship ; Uncoupling Protein 1 ; },
abstract = {A concise review is given of the research in our laboratory on the ADP/ATP carrier (AAC) and the uncoupling protein (UCP). Although homologous proteins, their widely different functions and contrasts are stressed. The pioneer role of research on the AAC, not only for the mitochondrial but also for other carriers, and the present state of their structure-function relationship is reviewed. The function of UCP as a highly regulated H+ carrier is described in contrast to the largely unregulated ADP/ATP exchange in AAC. General principles of carrier catalysis as derived from studies on the AAC and UCP are elucidated.},
}

Adenosine Diphosphate/metabolism
Adenosine Triphosphate/metabolism
Adipose Tissue, Brown/metabolism
Amino Acid Sequence
Animals
Binding Sites
Biological Transport
Carrier Proteins/chemistry/*physiology
*Energy Metabolism
Intracellular Membranes/*metabolism
Ion Channels
Mammals/metabolism
Membrane Proteins/chemistry/*physiology
Mitochondria/*metabolism
Mitochondrial ADP, ATP Translocases/chemistry/*physiology
Mitochondrial Proteins
Molecular Sequence Data
Phylogeny
Protein Structure, Tertiary
Protons
Structure-Activity Relationship
Uncoupling Protein 1

@article {pmid8662000,
year = {1996},
author = {Allen, JF and Raven, JA},
title = {Free-radical-induced mutation vs redox regulation: costs and benefits of genes in organelles.},
journal = {Journal of molecular evolution},
volume = {42},
number = {5},
pages = {482-492},
pmid = {8662000},
issn = {0022-2844},
mesh = {Aging/genetics ; Cell Nucleus/genetics ; Chloroplasts/genetics ; DNA Repair/genetics ; DNA, Chloroplast/genetics ; DNA, Mitochondrial/genetics ; Electron Transport/genetics ; Energy Metabolism/genetics ; Eukaryotic Cells/metabolism/ultrastructure ; Evolution, Molecular ; Free Radicals ; Mitochondria/genetics ; *Mutation ; Nitrogen Fixation/genetics ; Organelles/*genetics ; Oxidation-Reduction ; Oxidative Stress/*genetics ; Prokaryotic Cells/metabolism/ultrastructure ; Reactive Oxygen Species/metabolism ; Recombination, Genetic ; Symbiosis ; },
}

Aging/genetics
Cell Nucleus/genetics
Chloroplasts/genetics
DNA Repair/genetics
DNA, Chloroplast/genetics
DNA, Mitochondrial/genetics
Electron Transport/genetics
Energy Metabolism/genetics
Eukaryotic Cells/metabolism/ultrastructure
Evolution, Molecular
Free Radicals
Mitochondria/genetics
*Mutation
Nitrogen Fixation/genetics
Organelles/*genetics
Oxidation-Reduction
Oxidative Stress/*genetics
Prokaryotic Cells/metabolism/ultrastructure
Reactive Oxygen Species/metabolism
Recombination, Genetic
Symbiosis

@article {pmid8663075,
year = {1996},
author = {Kobayashi, M and Matsuo, Y and Takimoto, A and Suzuki, S and Maruo, F and Shoun, H},
title = {Denitrification, a novel type of respiratory metabolism in fungal mitochondrion.},
journal = {The Journal of biological chemistry},
volume = {271},
number = {27},
pages = {16263-16267},
doi = {10.1074/jbc.271.27.16263},
pmid = {8663075},
issn = {0021-9258},
mesh = {*Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Adenosine Triphosphate/metabolism ; Antimycin A/pharmacology ; Cytochromes/metabolism ; Energy Metabolism ; Fusarium/*metabolism ; Guanine Nucleotide Exchange Factors ; Kinetics ; Microscopy, Fluorescence ; Mitochondria/drug effects/*metabolism ; Mitosporic Fungi/*metabolism ; Nitrate Reductases/antagonists & inhibitors/*metabolism ; Nitrite Reductases/antagonists & inhibitors/*metabolism ; *Oxygen Consumption/drug effects ; Proteins/isolation & purification/*metabolism ; Rotenone/pharmacology ; Shc Signaling Adaptor Proteins ; Spectrophotometry ; Thenoyltrifluoroacetone/pharmacology ; },
abstract = {Subcellular localization and coupling to ATP synthesis were investigated with respect to the denitrifying systems of two fungi, Fusarium oxysporum and Cylindrocarpon tonkinense. Dissimilatory nitrate reductase of F. oxysporum or nitrite reductase of C. tonkinense could be detected in the mitochondrial fraction prepared from denitrifying cells of each fungus. Fluorescence immunolocalization, cofractionation with mitochondrial marker enzymes, and cytochromes provided evidence that the denitrifying enzymes are co-purified with mitochondria. Respiratory substrates such as malate plus pyruvate, succinate, and formate were effective donors of electrons to these activities in the mitochondrial fractions. Moreover, nitrite and nitrate reduction were shown to be coupled to the synthesis of ATP with energy yields (P:NO3- or P:2e ratios) of 0.88 to 1.4, depending upon whether malate/pyruvate or succinate were provided as substrates. Nitrate or nitrite reductase activity was inhibited by inhibitors such as rotenone, antimycin A, and thenoyltrifluoroacetone. Thus, fungal denitrification activities are localized to mitochondria and are coupled to the synthesis of ATP. The existence of these novel respiration systems are discussed with regard to the origin and evolution of mitochondria.},
}

*Adaptor Proteins, Signal Transducing
*Adaptor Proteins, Vesicular Transport
Adenosine Triphosphate/metabolism
Antimycin A/pharmacology
Cytochromes/metabolism
Energy Metabolism
Fusarium/*metabolism
Guanine Nucleotide Exchange Factors
Kinetics
Microscopy, Fluorescence
Mitochondria/drug effects/*metabolism
Mitosporic Fungi/*metabolism
Nitrate Reductases/antagonists & inhibitors/*metabolism
Nitrite Reductases/antagonists & inhibitors/*metabolism
*Oxygen Consumption/drug effects
Proteins/isolation & purification/*metabolism
Rotenone/pharmacology
Shc Signaling Adaptor Proteins
Spectrophotometry
Thenoyltrifluoroacetone/pharmacology

@article {pmid9115381,
year = {1997},
author = {Sogin, ML},
title = {Organelle origins: energy-producing symbionts in early eukaryotes?.},
journal = {Current biology : CB},
volume = {7},
number = {5},
pages = {R315-7},
doi = {10.1016/s0960-9822(06)00147-3},
pmid = {9115381},
issn = {0960-9822},
mesh = {Animals ; *Biological Evolution ; *Energy Metabolism ; Eukaryotic Cells ; Genes, Protozoan ; Mitochondria/physiology ; Organelles/*physiology ; Symbiosis ; Trichomonas vaginalis/genetics/*physiology/ultrastructure ; },
abstract = {The discovery that Trichomonas vaginalis, an early diverging protist that lacks mitochondria but has energy-producing hydrogenosomes, makes bacterial-like heat shock proteins suggests that symbionts ancestral to mitochondria and hydrogenosomes were present at early stages of eukaryote evolution.},
}

Animals
*Biological Evolution
*Energy Metabolism
Eukaryotic Cells
Genes, Protozoan
Mitochondria/physiology
Organelles/*physiology
Symbiosis
Trichomonas vaginalis/genetics/*physiology/ultrastructure

@article {pmid9136629,
year = {1997},
author = {Danpure, CJ},
title = {Variable peroxisomal and mitochondrial targeting of alanine: glyoxylate aminotransferase in mammalian evolution and disease.},
journal = {BioEssays : news and reviews in molecular, cellular and developmental biology},
volume = {19},
number = {4},
pages = {317-326},
doi = {10.1002/bies.950190409},
pmid = {9136629},
issn = {0265-9247},
mesh = {Alanine Transaminase/*metabolism ; Animals ; Biological Transport ; Catalysis ; Cytosol/enzymology ; Diet ; Dimerization ; Energy Metabolism ; Enzyme Induction ; Evolution, Molecular ; Glucose/metabolism ; Glyoxylates/metabolism ; Humans ; Hyperoxaluria/*enzymology/genetics ; Mammals/*metabolism ; Microbodies/*enzymology ; Mitochondria/*enzymology ; Polymorphism, Genetic ; Protein Sorting Signals/physiology ; Selection, Genetic ; Species Specificity ; *Transaminases ; },
abstract = {Under the putative influence of dietary selection pressure, the subcellular distribution of alanine:glyoxylate aminotransferase 1 (AGT) has changed on many occasions during the evolution of mammals. Depending on the particular species, AGT can be found either in peroxisomes or mitochondria, or in both peroxisomes and mitochondria. This variable localization depends on the differential expression of N-terminal mitochondrial and C-terminal peroxisomal targeting sequences by the use of alternative transcription and translation initiation sites. AGT is peroxisomal in most humans, but it is mistargeted to the mitochondria in a subset of patients suffering from the rare hereditary disease primary hyperoxaluria type 1. Mistargeting is due to the unlikely combination of a normally occurring polymorphism that generates a functionally weak mitochondrial targeting sequence and a disease-specific mutation which, in combination with the polymorphism, inhibits AGT dimerization. The mechanisms by which AGT can be targeted differentially to peroxisomes and/or mitochondria highlight the different molecular requirements for protein import into these two organelles.},
}

Alanine Transaminase/*metabolism
Animals
Biological Transport
Catalysis
Cytosol/enzymology
Diet
Dimerization
Energy Metabolism
Enzyme Induction
Evolution, Molecular
Glucose/metabolism
Glyoxylates/metabolism
Humans
Hyperoxaluria/*enzymology/genetics
Mammals/*metabolism
Microbodies/*enzymology
Mitochondria/*enzymology
Polymorphism, Genetic
Protein Sorting Signals/physiology
Selection, Genetic
Species Specificity
*Transaminases

@article {pmid9156326,
year = {1997},
author = {Giannattasio, S and Jurgelevicius, V and Lattanzio, P and Cimbalistienè, L and Marra, E and Kucinskas, V},
title = {Phenylketonuria mutations and linked haplotypes in the Lithuanian population: origin of the most common R408W mutation.},
journal = {Human heredity},
volume = {47},
number = {3},
pages = {155-160},
doi = {10.1159/000154403},
pmid = {9156326},
issn = {0001-5652},
mesh = {Evolution, Molecular ; Founder Effect ; *Haplotypes ; Humans ; Lithuania ; Minisatellite Repeats/genetics ; Mutation/*genetics ; Phenylalanine Hydroxylase/genetics ; Phenylketonurias/ethnology/*genetics ; Repetitive Sequences, Nucleic Acid/genetics ; },
abstract = {A genealogical study was performed in Lithuanian phenylketonuria (PKU) families with the aim of tracing the origins of the R408W/haplotype 2/VNTR3 allele. The relative frequency of six phenylalanine hydroxylase (PAH) mutations (R408W, R158Q, R261Q, G272X, IVS10nt-11g --> a, and IVS12nt1g --> a) common in Eastern European populations and their association with variable number of tandem repeat (VNTR) and short tandem repeat (STR) sites in the PAH gene were examined in 130 PKU Lithuanian chromosomes, including 95 of Baltic, 28 of Slavonic and 7 of unknown origin. R408W was found to be the most frequent (70%) mutation in both Balts or Slavonians with a uniform frequency distribution. No statistically significant differences in the frequency distribution of the other mutations analysed were found. In Balts and Slavonians, the R408W mutation is strongly associated with the three-copy VNTR and the 240-bp STR allele. The frequency of this association is 68% in both ethnic groups. The genealogical data provided in this paper indicate that the most common R408W/VNTR3/STR240 allele arose in ancient times possibly among pre-Indo-Europeans and suggest that the high frequency of the R408W mutation and associated minihaplotype in Balts of Lithuania is due to a founder effect.},
}

Evolution, Molecular
Founder Effect
*Haplotypes
Humans
Lithuania
Minisatellite Repeats/genetics
Mutation/*genetics
Phenylalanine Hydroxylase/genetics
Phenylketonurias/ethnology/*genetics
Repetitive Sequences, Nucleic Acid/genetics

@article {pmid9249985,
year = {1997},
author = {Oh-hama, T},
title = {Evolutionary consideration on 5-aminolevulinate synthase in nature.},
journal = {Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life},
volume = {27},
number = {4},
pages = {405-412},
doi = {10.1023/a:1006583601341},
pmid = {9249985},
issn = {0169-6149},
mesh = {5-Aminolevulinate Synthetase/*genetics/*metabolism ; Acetyltransferases/genetics ; Acyltransferases/genetics ; Animals ; Bacteria/enzymology/genetics ; *Biological Evolution ; Birds ; Energy Metabolism ; Eukaryota/enzymology/genetics ; Eukaryotic Cells ; Gene Expression ; Humans ; Mammals ; Phylogeny ; Plants/enzymology/genetics ; Prokaryotic Cells ; Saccharomyces cerevisiae/enzymology/genetics ; },
abstract = {5-Aminolevulinic acid (ALA), a universal precursor of tetrapyrrole compounds can be synthesized by two pathways: the C5 (glutamate) pathway and ALA synthase. From the phylogenetic distribution it is shown that distribution of ALA synthase is restricted to the alpha subclass of purple bacteria in prokaryotes, and further distributed to mitochondria of eukaryotes. The monophyletic origin of bacterial and eukaryotic ALA synthase is shown by sequence analysis of the enzyme. Evolution of ALA synthase in the alpha subclass of purple bacteria is discussed in relation to the energy-generating and biosynthetic devices in subclasses of this bacteria.},
}

5-Aminolevulinate Synthetase/*genetics/*metabolism
Acetyltransferases/genetics
Acyltransferases/genetics
Animals
Bacteria/enzymology/genetics
*Biological Evolution
Birds
Energy Metabolism
Eukaryota/enzymology/genetics
Eukaryotic Cells
Gene Expression
Humans
Mammals
Phylogeny
Plants/enzymology/genetics
Prokaryotic Cells
Saccharomyces cerevisiae/enzymology/genetics

@article {pmid9260887,
year = {1997},
author = {Singh, B and Soltys, BJ and Wu, ZC and Patel, HV and Freeman, KB and Gupta, RS},
title = {Cloning and some novel characteristics of mitochondrial Hsp70 from Chinese hamster cells.},
journal = {Experimental cell research},
volume = {234},
number = {2},
pages = {205-216},
doi = {10.1006/excr.1997.3609},
pmid = {9260887},
issn = {0014-4827},
mesh = {Amino Acid Sequence ; Animals ; Antibody Specificity ; Base Sequence ; Biological Transport ; *CHO Cells ; Cloning, Molecular ; Cricetinae ; DNA, Complementary/genetics ; Escherichia coli ; HSP70 Heat-Shock Proteins/*analysis/*genetics/metabolism ; Mitochondria/*chemistry ; Mitochondria, Heart/metabolism ; Molecular Sequence Data ; Phylogeny ; Protein Processing, Post-Translational ; Rats ; Recombinant Fusion Proteins ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; },
abstract = {The cDNA for Chinese hamster mitochondrial Hsp70 (mHsp70) was cloned and sequenced using a polymerase chain reaction probe based on conserved regions in the Hsp70 family of proteins. The encoded protein consists of 679 amino acids which includes a N-terminal mitochondrial targeting sequence of 46 amino acids. The mHsp70 protein contains several sequence signatures that are characteristics of prokaryotic and eukaryotic organellar Hsp70 homologs. In a phylogenetic tree based on Hsp70 sequences, it branches with the gram-negative proteobacteria, supporting the endosymbiotic origin of mitochondria from this group of prokaryotes. The mHsp70 cDNA was transcribed and translated in vitro and its import into isolated rat heart mitochondria was examined. The precursor mHsp70 was converted into a mature form of lower molecular mass (approximately 71 kDa) which became resistant to trypsin digestion. The import of mHsp70 into mitochondria was not observed in the presence of an uncoupler of energy metabolism or when the N-terminal presequence was lacking. The cDNA for mHsp70 was expressed in Escherichia coli and a polyclonal antibody to the purified recombinant protein was raised. The antibody shows no cross-reactivity to recombinant cytosolic Hsp70 protein and in 2-D gel blots it reacted specifically with the mHsp70 protein only. In immunofluorescence experiments, the antibody predominantly labeled mitochondria, and the observed labeling pattern was identical to that seen with a monoclonal antibody to the mitochondrial Hsp60 chaperonin. The affinity-purified antibody to mHsp70 was also employed to examine the subcellular distribution of the protein by cryoelectron microscopy and the immunogold-labeling technique. In these experiments, in addition to mitochondria, labeling with mitochondrial Hsp70 antibody was also observed on the plasma membrane and in unidentified cytoplasmic vesicles and granules. These studies raise the possibility that similar to the Hsp60 chaperonin and a number of other mitochondrial proteins, mHsp70 may have an extramitochondrial role.},
}

Amino Acid Sequence
Animals
Antibody Specificity
Base Sequence
Biological Transport
*CHO Cells
Cloning, Molecular
Cricetinae
DNA, Complementary/genetics
Escherichia coli
HSP70 Heat-Shock Proteins/*analysis/*genetics/metabolism
Mitochondria/*chemistry
Mitochondria, Heart/metabolism
Molecular Sequence Data
Phylogeny
Protein Processing, Post-Translational
Rats
Recombinant Fusion Proteins
Sequence Alignment
Sequence Analysis, DNA
Sequence Homology, Amino Acid

@article {pmid9374771,
year = {1997},
author = {Consolini, AE and Márquez, MT and Ponce-Hornos, JE},
title = {Energetics of heart muscle contraction under high K perfusion: verapamil and Ca effects.},
journal = {The American journal of physiology},
volume = {273},
number = {5},
pages = {H2343-50},
doi = {10.1152/ajpheart.1997.273.5.H2343},
pmid = {9374771},
issn = {0002-9513},
mesh = {Animals ; Calcium/*pharmacology ; Calorimetry ; Electric Stimulation ; Energy Metabolism/drug effects ; Female ; Heart/*physiology ; Heart Ventricles ; In Vitro Techniques ; Kinetics ; Male ; Mitochondria, Heart/drug effects/*metabolism ; Myocardial Contraction/drug effects/*physiology ; Perfusion ; Potassium/*pharmacology ; Rats ; Rats, Wistar ; Verapamil/*pharmacology ; },
abstract = {Tension-dependent (TDH) and tension-independent heat (TIH) release were measured during single isovolumetric contractions in the arterially perfused rat ventricle. Under perfusion with 7 mM K-0.5 mM Ca, TDH showed only one component (H3), whereas TIH could be divided into two components (H1 and H2) of short evolution (similar to the classically identified activation heat) and one component (H4) of long duration (dependent on mitochondrial respiration). Under 25 mM K, TIH components (i.e., H1, H2, and H4) increased with the increase in extracellular Ca concentration ([Ca]o) from 0.5 to 4 mM, and H3 correlated with pressure at all [Ca]o, with regression parameters similar to those observed under 7 mM K. Under 25 mM K-2 mM Ca, peak pressure development (P), H1, H2, and H3, plotted against the number of beats under 0.4 microM verapamil, exponentially decreased, but H4 decreased to 5.5 +/- 2.9% in the first contraction and remained constant thereafter. Under hypoxia, P, H1, H2, and H3 progressively decreased for about six contractions, but H4 was not detectable from the second contraction. The results suggest that increasing extracellular K concentration decreases contractile economy mainly by increasing energy expenditure related to a Ca-dependent (verapamil-sensitive) mitochondrial activity that is not related to force generation.},
}

Animals
Calcium/*pharmacology
Calorimetry
Electric Stimulation
Energy Metabolism/drug effects
Female
Heart/*physiology
Heart Ventricles
In Vitro Techniques
Kinetics
Male
Mitochondria, Heart/drug effects/*metabolism
Myocardial Contraction/drug effects/*physiology
Perfusion
Potassium/*pharmacology
Rats
Rats, Wistar
Verapamil/*pharmacology

@article {pmid9387093,
year = {1997},
author = {Golshani-Hebroni, SG and Bessman, SP},
title = {Hexokinase binding to mitochondria: a basis for proliferative energy metabolism.},
journal = {Journal of bioenergetics and biomembranes},
volume = {29},
number = {4},
pages = {331-338},
pmid = {9387093},
issn = {0145-479X},
mesh = {Adenosine Triphosphate/biosynthesis ; Animals ; *Energy Metabolism ; Glycolysis ; Hexokinase/*metabolism ; Insulin/metabolism ; Mitochondria/*metabolism ; NAD/metabolism ; NADP/metabolism ; Protein Biosynthesis ; Tumor Cells, Cultured ; },
abstract = {Current thought is that proliferating cells undergo a shift from oxidative to glycolytic metabolism, where the energy requirements of the rapidly dividing cell are provided by ATP from glycolysis. Drawing on the hexokinase-mitochondrial acceptor theory of insulin action, this article presents evidence suggesting that the increased binding of hexokinase to porin on mitochondria of cancer cells not only accelerates glycolysis by providing hexokinase with better access to ATP, but also stimulates the TCA cycle by providing the mitochondrion with ADP that acts as an acceptor for phosphoryl groups. Furthermore, this acceleration of the TCA cycle stimulates protein synthesis via two mechanisms: first, by increasing ATP production, and second, by provision of certain amino acids required for protein synthesis, since the amino acids glutamate, alanine, and aspartate are either reduction products or partially oxidized products of the intermediates of glycolysis and the TCA cycle. The utilization of oxygen in the course of the TCA cycle turnover is relatively diminished even though TCA cycle intermediates are being consumed. With partial oxidation of TCA cycle intermediates into amino acids, there is necessarily a reduction in formation of CO2 from pyruvate, seen as a relative diminution in utilization of oxygen in relation to carbon utilization. This has been assumed to be an inhibition of oxygen uptake and therefore a diminution of TCA cycle activity. Therefore a switch from oxidative metabolism to glycolytic metabolism has been assumed (the Crabtree effect). By stimulating both ATP production and protein synthesis for the rapidly dividing cell, the binding of hexokinase to mitochondrial porin lies at the core of proliferative energy metabolism. This article further reviews literature on the binding of the isozymes of hexokinase to porin, and on the evolution of insulin, proposing that intracellular insulin-like proteins directly bind hexokinase to mitochondrial porin.},
}

Adenosine Triphosphate/biosynthesis
Animals
*Energy Metabolism
Glycolysis
Hexokinase/*metabolism
Insulin/metabolism
Mitochondria/*metabolism
NAD/metabolism
NADP/metabolism
Protein Biosynthesis
Tumor Cells, Cultured

@article {pmid9404460,
year = {1997},
author = {Lestienne, P},
title = {[Do mitochondria play a role in aging?].},
journal = {Comptes rendus des seances de la Societe de biologie et de ses filiales},
volume = {191},
number = {4},
pages = {579-592},
pmid = {9404460},
issn = {0037-9026},
mesh = {Aging/*physiology ; Alzheimer Disease/genetics/metabolism ; Animals ; DNA, Mitochondrial/genetics/metabolism ; Forecasting ; Free Radicals/metabolism ; Humans ; Mitochondria/*metabolism/physiology ; Parkinson Disease/genetics/metabolism ; },
abstract = {Ageing is an unavoidable and complex phenomenon which may be a price to pay to evolution. Thus genetics appear to play a predominant role besides environmental factors. Energetic metabolism slowly declines with ageing supporting a possible active role of mitochondria, the power supply of the cells, to this process. Mitochondrial DNA alterations appear during the mid-life and in degenerative diseases such as in Parkinson's and Alzheimer's; they include large scale deletions and point mutations. Since the respiratory chain plays a major role in the generation of superoxide anions which are converted into hydroxyl radicals that may impair lipids, proteins and DNA function in mitochondria, this vicious cycle may result from both an altered control of mitochondrial biogenesis dependent from the nucleus, and/or from a lack of repair and accumulation of somatic mitochondrial DNA mutations.},
}

Aging/*physiology
Alzheimer Disease/genetics/metabolism
Animals
DNA, Mitochondrial/genetics/metabolism
Forecasting
Free Radicals/metabolism
Humans
Mitochondria/*metabolism/physiology
Parkinson Disease/genetics/metabolism

@article {pmid9467721,
year = {1998},
author = {Miquel, J},
title = {An update on the oxygen stress-mitochondrial mutation theory of aging: genetic and evolutionary implications.},
journal = {Experimental gerontology},
volume = {33},
number = {1-2},
pages = {113-126},
doi = {10.1016/s0531-5565(97)00060-0},
pmid = {9467721},
issn = {0531-5565},
mesh = {Aging/*genetics ; Animals ; *Biological Evolution ; DNA, Mitochondrial/*genetics ; Drosophila/genetics ; Energy Metabolism/physiology ; Humans ; Mutation ; Oxidative Stress/drug effects/*physiology ; Stochastic Processes ; },
abstract = {The acceleration of fixed-postmitotic cell aging by a high metabolic rate and the age related loss of mitochondria found in that cell type led us to propose an oxygen stress-mitochondrial mutation theory of aging, according to which senescence may be linked to mutations of the mitochondrial genome (mtDNA) of the irreversibly differentiated cells. This extranuclear somatic gene mutation concept of aging is supported by the fact that mtDNA synthesis takes place at the inner mitochondrial membrane near the sites of formation of highly reactive oxygen species. Mitochondrial DNA may be unable to prevent the intrinsic mutagenesis caused by those byproducts of respiration because, in contrast to the nuclear genome, it lacks excision and recombination repair. The resulting mitochondrial impairment and concomitant cell bioenergetic decline may cause the senescent loss of physiological performance and may play a key role in the pathogenesis of many age-related degenerative diseases. These concepts are integrated with classic and contemporary hypotheses in a unitary theory that reconciles programmed and stochastic concepts of aging. Thus, it is suggested that cells are programmed to differentiate, and then they accumulate mitochondrial-genetic damage because of their high levels of oxyradical stress and the loss of the organelle rejuvenating power of mitosis.},
}

Aging/*genetics
Animals
*Biological Evolution
DNA, Mitochondrial/*genetics
Drosophila/genetics
Energy Metabolism/physiology
Humans
Mutation
Oxidative Stress/drug effects/*physiology
Stochastic Processes

@article {pmid9503641,
year = {1998},
author = {Moyes, CD and Battersby, BJ and Leary, SC},
title = {Regulation of muscle mitochondrial design.},
journal = {The Journal of experimental biology},
volume = {201},
number = {Pt 3},
pages = {299-307},
pmid = {9503641},
issn = {0022-0949},
mesh = {Animals ; Base Sequence ; Biological Evolution ; DNA, Mitochondrial/genetics ; DNA-Binding Proteins/genetics/metabolism ; Electron Transport Complex IV/genetics/metabolism ; Energy Metabolism ; Gene Expression Regulation ; Humans ; Mitochondria, Muscle/genetics/*metabolism ; Nuclear Respiratory Factors ; Oxidative Phosphorylation ; Trans-Activators/genetics/metabolism ; },
abstract = {Mitochondria are responsible for the generation of ATP to fuel muscle contraction. Hypermetabolic stresses imposed upon muscles can lead to mitochondrial proliferation, but the resulting mitochondria greatly resemble their progenitors. During the mitochondrial biogenesis that accompanies phenotypic adaptation, the stoichiometric relationships between functional elements are preserved through shared sensitivities of respiratory genes to specific transcription factors. Although the properties of muscle mitochondria are generally thought to be highly conserved across species, there are many examples of mitochondrial differences between muscle types, species and developmental states and even within single cells. In this review, we discuss (1) the nature and regulation of gene families that allow coordinated expression of genes for mitochondrial products and (2) the regulatory mechanisms by which mitochondrial differences can arise over physiological and evolutionary time.},
}

Animals
Base Sequence
Biological Evolution
DNA, Mitochondrial/genetics
DNA-Binding Proteins/genetics/metabolism
Electron Transport Complex IV/genetics/metabolism
Energy Metabolism
Gene Expression Regulation
Humans
Mitochondria, Muscle/genetics/*metabolism
Nuclear Respiratory Factors
Oxidative Phosphorylation
Trans-Activators/genetics/metabolism

@article {pmid9504342,
year = {1998},
author = {Brown, DM and Upcroft, JA and Edwards, MR and Upcroft, P},
title = {Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis.},
journal = {International journal for parasitology},
volume = {28},
number = {1},
pages = {149-164},
doi = {10.1016/s0020-7519(97)00172-0},
pmid = {9504342},
issn = {0020-7519},
mesh = {Amino Acids/metabolism ; Animals ; Bacteria, Anaerobic/*metabolism ; Biological Evolution ; Electron Transport ; Energy Metabolism ; Fermentation ; Giardia/genetics/*metabolism ; Models, Biological ; Oxidation-Reduction ; Oxidative Stress ; Oxygen Consumption ; },
abstract = {The protozoan parasite, Giardia duodenalis, shares many metabolic and genetic attributes of the bacteria, including fermentative energy metabolism which relies heavily on pyrophosphate rather than adenosine triphosphate and as a result contains two typically bacterial glycolytic enzymes which are pyrophosphate dependent. Pyruvate decarboxylation and subsequent electron transport to as yet unidentified anaerobic electron acceptors relies on a eubacterial-like pyruvate:ferredoxin oxidoreductase and an archaebacterial/eubacterial-like ferredoxin. The presence of another 2-ketoacid oxidoreductase (with a preference for alpha-ketobutyrate) and multiple ferredoxins in Giardia is also a trait shared with the anaerobic bacteria. Giardia pyruvate:ferredoxin oxidoreductase is distinct from the pyruvate dehydrogenase multienzyme complex invariably found in mitochondria. This is consistent with a lack of mitochondria, citric acid cycle, oxidative phosphorylation and glutathione in Giardia. Giardia duodenalis actively consumes oxygen and yet lacks the conventional mechanisms of oxidative stress management, including superoxide dismutase, catalase, peroxidase, and glutathione cycling, which are present in most eukaryotes. In their place Giardia contains a prokaryotic H2O-producing NADH oxidase, a membrane-associated NADH peroxidase, a broad-range prokaryotic thioredoxin reductase-like disulphide reductase and the low molecular weight thiols, cysteine, thioglycolate, sulphite and coenzyme A. NADH oxidase is a major component of the electron transport pathway of Giardia which, in conjunction with disulphide reductase, protects oxygen-labile proteins such as ferredoxin and pyruvate:ferredoxin oxidoreductase against oxidative stress by maintaining a reduced intracellular environment. As the terminal oxidase, NADH oxidase provides a means of removing excess H+, thereby enabling continued pyruvate decarboxylation and the resultant production of acetate and adenosine triphosphate. A further example of the bacterial-like metabolism of Giardia is the utilisation of the amino acid arginine as an energy source. Giardia contain the arginine dihydrolase pathway, which occurs in a number of anaerobic prokaryotes, but not in other eukaryotes apart from trichomonads and Chlamydomonas reinhardtii. The pathway includes substrate level phosphorylation and is sufficiently active to make a major contribution to adenosine triphosphate production. Two enzymes of the pathway, arginine deiminase and carbamate kinase, are rare in eukaryotes and do not occur in higher animals. Arginine is transported into the trophozoite via a bacterial-like arginine:ornithine antiport. Together these metabolic pathways in Giardia provide a wide range of potential drug targets for future consideration.},
}

Amino Acids/metabolism
Animals
Bacteria, Anaerobic/*metabolism
Biological Evolution
Electron Transport
Energy Metabolism
Fermentation
Giardia/genetics/*metabolism
Models, Biological
Oxidation-Reduction
Oxidative Stress
Oxygen Consumption

@article {pmid9545461,
year = {1998},
author = {Vellai, T and Takács, K and Vida, G},
title = {A new aspect to the origin and evolution of eukaryotes.},
journal = {Journal of molecular evolution},
volume = {46},
number = {5},
pages = {499-507},
doi = {10.1007/pl00006331},
pmid = {9545461},
issn = {0022-2844},
mesh = {*Biological Evolution ; DNA Replication ; Energy Metabolism ; Escherichia coli/genetics/growth & development ; Eukaryotic Cells/*physiology ; Genetic Vectors ; *Genome, Bacterial ; *Models, Biological ; Organelles/metabolism ; Prokaryotic Cells/*physiology ; },
abstract = {One of the most important omissions in recent evolutionary theory concerns how eukaryotes could emerge and evolve. According to the currently accepted views, the first eukaryotic cell possessed a nucleus, an endomembrane system, and a cytoskeleton but had an inefficient prokaryotic-like metabolism. In contrast, one of the most ancient eukaryotes, the metamonada Giardia lamblia, was found to have formerly possessed mitochondria. In sharp contrast with the traditional views, this paper suggests, based on the energetic aspect of genome organization, that the emergence of eukaryotes was promoted by the establishment of an efficient energy-converting organelle, such as the mitochondrion. Mitochondria were acquired by the endosymbiosis of ancient alpha-purple photosynthetic Gram-negative eubacteria that reorganized the prokaryotic metabolism of the archaebacterial-like ancestral host cells. The presence of an ATP pool in the cytoplasm provided by this cell organelle allowed a major increase in genome size. This evolutionary change, the remarkable increase both in genome size and complexity, explains the origin of the eukaryotic cell itself. The loss of cell wall and the appearance of multicellularity can also be explained by the acquisition of mitochondria. All bacteria use chemiosmotic mechanisms to harness energy; therefore the periplasm bounded by the cell wall is an essential part of prokaryotic cells. Following the establishment of mitochondria, the original plasma membrane-bound metabolism of prokaryotes, as well as the funcion of the periplasm providing a compartment for the formation of different ion gradients, has been transferred into the inner mitochondrial membrane and intermembrane space. After the loss of the essential function of periplasm, the bacterial cell wall could also be lost, which enabled the naked cells to establish direct connections among themselves. The relatively late emergence of mitochondria may be the reason why multicellularity evolved so slowly.},
}

*Biological Evolution
DNA Replication
Energy Metabolism
Escherichia coli/genetics/growth & development
Eukaryotic Cells/*physiology
Genetic Vectors
*Genome, Bacterial
*Models, Biological
Organelles/metabolism
Prokaryotic Cells/*physiology

@article {pmid9580216,
year = {1997},
author = {Chagoya de Sánchez, V and Hernández-Muñoz, R and López-Barrera, F and Yañez, L and Vidrio, S and Suárez, J and Cota-Garza, MD and Aranda-Fraustro, A and Cruz, D},
title = {Sequential changes of energy metabolism and mitochondrial function in myocardial infarction induced by isoproterenol in rats: a long-term and integrative study.},
journal = {Canadian journal of physiology and pharmacology},
volume = {75},
number = {12},
pages = {1300-1311},
pmid = {9580216},
issn = {0008-4212},
mesh = {Animals ; Blood Pressure/drug effects ; *Cardiotonic Agents ; Edema/complications/pathology ; Electrophysiology ; Energy Metabolism/*drug effects ; Heart/*drug effects/physiology ; Heart Rate/drug effects ; *Isoproterenol ; Male ; Microscopy, Electron ; Mitochondria, Heart/*drug effects/metabolism/pathology/ultrastructure ; Myocardial Infarction/*chemically induced/enzymology/pathology/physiopathology ; Rats ; Rats, Wistar ; },
abstract = {Acute myocardial infarction is the second cause of mortality in most countries, therefore, it is important to know the evolution and sequence of the physiological and biochemical changes involved in this pathology. This study attempts to integrate these changes and to correlate them in a long-term model (96 h) of isoproterenol-induced myocardial cell damage in the rat. We achieved an infarct-like damage in the apex region of the left ventricle, occurring 12-24 h after isoproterenol administration. The lesion was defined by histological criteria, continuous telemetric ECG recordings, and the increase in serum marker enzymes, specific for myocardial damage. A distinction is made among preinfarction, infarction, and postinfarction. Three minutes after drug administration, there was a 60% increase in heart rate and a lowering of blood pressure, resulting possibly in a functional ischemia. Ultrastructural changes and mitochondrial swelling were evident from the first hour of treatment, but functional alterations in isolated mitochondria, such as decreases in oxygen consumption, respiratory quotient, ATP synthesis, and membrane potential, were noticed only 6 h after drug administration and lasted until 72 h later. Mitochondrial proteins decreased after 3 h of treatment, reaching almost a 50% diminution, which was maintained during the whole study. An energy imbalance, reflected by a decrease in energy charge and in the creatine phosphate/creatine ratio, was observed after 30 min of treatment; however, ATP and total adenine nucleotides diminished clearly only after 3 h of treatment. All these alterations reached a maximum at the onset of infarction and were accompanied by damage to the myocardial function, drastically decreasing left ventricular pressure and shortening the atrioventricular interval. During postinfarction, a partial recovery of energy charge, creatine phosphate/creatine ratio, membrane potential, and myocardial function occurred, but not of mitochondrial oxygen consumption, rate of ATP synthesis, total adenine nucleotides, or mitochondrial proteins. Interesting correlations of the sequential changes in heart and mitochondrial functions with energy metabolism were obtained at different stages of the isoproterenol-induced cardiotoxicity. These correlations could be useful to study and understand the cellular events involved in this pathology.},
}

Animals
Blood Pressure/drug effects
*Cardiotonic Agents
Edema/complications/pathology
Electrophysiology
Energy Metabolism/*drug effects
Heart/*drug effects/physiology
Heart Rate/drug effects
*Isoproterenol
Male
Microscopy, Electron
Mitochondria, Heart/*drug effects/metabolism/pathology/ultrastructure
Myocardial Infarction/*chemically induced/enzymology/pathology/physiopathology
Rats
Rats, Wistar

@article {pmid9693729,
year = {1998},
author = {Andersson, SG},
title = {Bioenergetics of the obligate intracellular parasite Rickettsia prowazekii.},
journal = {Biochimica et biophysica acta},
volume = {1365},
number = {1-2},
pages = {105-111},
doi = {10.1016/s0005-2728(98)00050-4},
pmid = {9693729},
issn = {0006-3002},
mesh = {Citric Acid/metabolism ; Electron Transport ; Energy Metabolism/genetics/*physiology ; Genome, Bacterial ; Mitochondria/physiology ; Mitochondrial ADP, ATP Translocases/genetics ; Operon ; Oxidation-Reduction ; Proton-Translocating ATPases/genetics ; Rickettsia prowazekii/genetics/*physiology ; },
abstract = {Mitochondria are thought to be derived from an ancestor of the alpha-proteobacteria and more specifically from the Rickettsiaceae. The bioenergetic repertoire of the obligate intracellular parasite Rickettsia prowazekii is consistent with its postulated role as the ancestor of the mitochondria. For example, the R. prowazekii genome contains genes encoding components of the tricarboxylic acid cycle as well as of the electron transport system, but lacks genes to support glycolysis. In addition, the R. prowazekii genome contains multiple genes coding for adenine nucleotide translocators which enables this intracellular parasite to exploit the cytoplasmic ATP of its host cell as a source of energy. The aim of this review is to describe the different aspects of the bioenergetic system in R. prowazekii and to discuss the results of phylogenetic reconstructions based on a variety of bioenergetic molecules which shed light on the origin and evolution of the mitochondrial genomes.},
}

Citric Acid/metabolism
Electron Transport
Energy Metabolism/genetics/*physiology
Genome, Bacterial
Mitochondria/physiology
Mitochondrial ADP, ATP Translocases/genetics
Operon
Oxidation-Reduction
Proton-Translocating ATPases/genetics
Rickettsia prowazekii/genetics/*physiology

@article {pmid9714744,
year = {1998},
author = {Di Lisa, F and Menabò, R and Canton, M and Petronilli, V},
title = {The role of mitochondria in the salvage and the injury of the ischemic myocardium.},
journal = {Biochimica et biophysica acta},
volume = {1366},
number = {1-2},
pages = {69-78},
doi = {10.1016/s0005-2728(98)00121-2},
pmid = {9714744},
issn = {0006-3002},
mesh = {Adenosine Triphosphate/metabolism ; Calcium/metabolism ; Cell Death/*physiology ; Cytochrome c Group/metabolism ; Energy Metabolism ; Humans ; Membrane Potentials ; Mitochondria, Heart/*physiology ; Mitochondrial ADP, ATP Translocases/metabolism ; Myocardial Ischemia/physiopathology ; Myocardial Reperfusion Injury/physiopathology ; Oxygen Consumption ; Proton-Translocating ATPases/metabolism ; },
abstract = {The relationships between mitochondrial derangements and cell necrosis are exemplified by the changes in the function and metabolism of mitochondria that occur in the ischemic heart. From a mitochondrial point of view, the evolution of ischemic damage can be divided into three phases. The first is associated with the onset of ischemia, and changes mitochondria from ATP producers into powerful ATP utilizers. During this phase, the inverse operation of F0F1 ATPase maintains the mitochondrial membrane potential by using the ATP made available by glycolysis. The second phase can be identified from the functional and structural alterations of mitochondria caused by prolongation of ischemia, such as decreased utilization of NAD-linked substrates, release of cytochrome c and involvement of mitochondrial channels. These events indicate that the relationship between ischemic damage and mitochondria is not limited to the failure in ATP production. Finally, the third phase links mitochondria to the destiny of the myocytes upon post-ischemic reperfusion. Indeed, depending on the duration and the severity of ischemia, not only is mitochondrial function necessary for cell recovery, but it can also exacerbate cell injury.},
}

Adenosine Triphosphate/metabolism
Calcium/metabolism
Cell Death/*physiology
Cytochrome c Group/metabolism
Energy Metabolism
Humans
Membrane Potentials
Mitochondria, Heart/*physiology
Mitochondrial ADP, ATP Translocases/metabolism
Myocardial Ischemia/physiopathology
Myocardial Reperfusion Injury/physiopathology
Oxygen Consumption
Proton-Translocating ATPases/metabolism

@article {pmid9746319,
year = {1998},
author = {Qin, W and Khuchua, Z and Cheng, J and Boero, J and Payne, RM and Strauss, AW},
title = {Molecular characterization of the creatine kinases and some historical perspectives.},
journal = {Molecular and cellular biochemistry},
volume = {184},
number = {1-2},
pages = {153-167},
pmid = {9746319},
issn = {0300-8177},
mesh = {Amino Acid Sequence ; Cloning, Molecular ; Creatine Kinase/*genetics ; Evolution, Molecular ; Gene Expression Regulation, Enzymologic/genetics ; Humans ; Isoenzymes ; Mitochondria/*genetics ; Molecular Sequence Data ; Muscles/*metabolism ; RNA, Messenger/genetics ; Sequence Alignment ; },
abstract = {Over the last 15 years, molecular characterization of the creatine kinase (CK) gene family has paralleled the molecular revolution of understanding gene structure, function, and regulation. In this review, we present a summary of advances in molecular analysis of the CK gene family with a few vignettes of historical interest. We describe how the muscle CK gene provided an essential model system to examine myogenic regulatory mechanisms, leading to the discovery of the binding site for the MyoD family of basic helix-loop-helix transcription factors essential in skeletal myogenesis and the characterization of the MEF2 family of factors with an A/T rich consensus binding site essential in skeletal myogenesis and cardiogenesis. Cloning and characterization of the four mRNAs and nuclear genes encoding the cytosolic CKs, muscle and brain CKs, and the mitochondrial (Mt) CKs, sarcomeric MtCK and ubiquitous MtCK, has allowed intriguing study of tissue-specific and cell-specific expression of the different CKs and analysis of structural, functional, regulatory, and evolutionary relationships among both the four CK proteins and genes. Current and future studies focus on understanding both cellular energetics facilitated by the CK enzymes, especially energy channelling from the site of production, the mitochondrial matrix and inner membrane, to various cytosolic foci of utilization, and regulation of MtCK gene expression at the cell and tissue-specific level as models of regulation of energy producing genes.},
}

Amino Acid Sequence
Cloning, Molecular
Creatine Kinase/*genetics
Evolution, Molecular
Gene Expression Regulation, Enzymologic/genetics
Humans
Isoenzymes
Mitochondria/*genetics
Molecular Sequence Data
Muscles/*metabolism
RNA, Messenger/genetics
Sequence Alignment

@article {pmid9859981,
year = {1998},
author = {Embley, TM and Martin, W},
title = {A hydrogen-producing mitochondrion.},
journal = {Nature},
volume = {396},
number = {6711},
pages = {517-519},
doi = {10.1038/24994},
pmid = {9859981},
issn = {0028-0836},
mesh = {Adenosine Triphosphate/biosynthesis ; Anaerobiosis ; Animals ; Biological Evolution ; Ciliophora/genetics/*metabolism/ultrastructure ; Cockroaches/parasitology ; DNA, Mitochondrial ; DNA, Protozoan ; Energy Metabolism ; Hydrogen/*metabolism ; Mitochondria/genetics/*metabolism ; Organelles/metabolism ; },
}

Adenosine Triphosphate/biosynthesis
Anaerobiosis
Animals
Biological Evolution
Ciliophora/genetics/*metabolism/ultrastructure
Cockroaches/parasitology
DNA, Mitochondrial
DNA, Protozoan
Energy Metabolism
Hydrogen/*metabolism
Mitochondria/genetics/*metabolism
Organelles/metabolism

@article {pmid9914833,
year = {1998},
author = {Azzone, GF},
title = {From bioenergetics to philosophy of science: a brief report of an exciting cultural journey.},
journal = {BioFactors (Oxford, England)},
volume = {8},
number = {3-4},
pages = {305-316},
doi = {10.1002/biof.5520080319},
pmid = {9914833},
issn = {0951-6433},
mesh = {Animals ; Biological Evolution ; *Energy Metabolism ; History, 20th Century ; Humans ; Italy ; Membrane Potentials ; Mitochondria/*physiology ; Physiology/history ; Proton Pumps ; },
}

Animals
Biological Evolution
*Energy Metabolism
History, 20th Century
Humans
Italy
Membrane Potentials
Mitochondria/*physiology
Physiology/history
Proton Pumps

@article {pmid10400536,
year = {1999},
author = {Hederstedt, L},
title = {Respiration without O2.},
journal = {Science (New York, N.Y.)},
volume = {284},
number = {5422},
pages = {1941-1942},
doi = {10.1126/science.284.5422.1941},
pmid = {10400536},
issn = {0036-8075},
mesh = {Anaerobiosis ; Bacillus subtilis/enzymology ; Binding Sites ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Dimerization ; Electron Transport ; *Energy Metabolism ; Escherichia coli/*enzymology ; Evolution, Molecular ; Fumarates/metabolism ; Mitochondria/enzymology ; Oxidation-Reduction ; Oxygen Consumption ; Protein Conformation ; Protein Structure, Secondary ; Succinate Dehydrogenase/*chemistry/*metabolism ; Succinic Acid/metabolism ; },
}

Anaerobiosis
Bacillus subtilis/enzymology
Binding Sites
Cell Membrane/enzymology
Crystallography, X-Ray
Dimerization
Electron Transport
*Energy Metabolism
Escherichia coli/*enzymology
Evolution, Molecular
Fumarates/metabolism
Mitochondria/enzymology
Oxidation-Reduction
Oxygen Consumption
Protein Conformation
Protein Structure, Secondary
Succinate Dehydrogenase/*chemistry/*metabolism
Succinic Acid/metabolism

@article {pmid10430918,
year = {1999},
author = {Karlin, S and Brocchieri, L and Mrázek, J and Campbell, AM and Spormann, AM},
title = {A chimeric prokaryotic ancestry of mitochondria and primitive eukaryotes.},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
volume = {96},
number = {16},
pages = {9190-9195},
pmid = {10430918},
issn = {0027-8424},
support = {R01 GM010452/GM/NIGMS NIH HHS/United States ; 5R01GM10452-34/GM/NIGMS NIH HHS/United States ; 5R01HG00335-11/HG/NHGRI NIH HHS/United States ; },
mesh = {Amino Acid Sequence ; Animals ; Archaea/*genetics ; Bacteria/*genetics ; *Biological Evolution ; *Chimera ; Clostridium/genetics ; DNA, Mitochondrial/*genetics ; Energy Metabolism/genetics ; Eukaryotic Cells ; Heat-Shock Proteins/genetics ; Humans ; Mitochondria/*genetics ; *Models, Genetic ; Proteins/chemistry/genetics ; Sulfolobus/genetics ; Vertebrates ; },
abstract = {We provide data and analysis to support the hypothesis that the ancestor of animal mitochondria (Mt) and many primitive amitochondrial (a-Mt) eukaryotes was a fusion microbe composed of a Clostridium-like eubacterium and a Sulfolobus-like archaebacterium. The analysis is based on several observations: (i) The genome signatures (dinucleotide relative abundance values) of Clostridium and Sulfolobus are compatible (sufficiently similar) and each has significantly more similarity in genome signatures with animal Mt sequences than do all other available prokaryotes. That stable fusions may require compatibility in genome signatures is suggested by the compatibility of plasmids and hosts. (ii) The expanded energy metabolism of the fusion organism was strongly selective for cementing such a fusion. (iii) The molecular apparatus of endospore formation in Clostridium serves as raw material for the development of the nucleus and cytoplasm of the eukaryotic cell.},
}

Amino Acid Sequence
Animals
Archaea/*genetics
Bacteria/*genetics
*Biological Evolution
*Chimera
Clostridium/genetics
DNA, Mitochondrial/*genetics
Energy Metabolism/genetics
Eukaryotic Cells
Heat-Shock Proteins/genetics
Humans
Mitochondria/*genetics
*Models, Genetic
Proteins/chemistry/genetics
Sulfolobus/genetics
Vertebrates

@article {pmid10467746,
year = {1999},
author = {Vellai, T and Vida, G},
title = {The origin of eukaryotes: the difference between prokaryotic and eukaryotic cells.},
journal = {Proceedings. Biological sciences},
volume = {266},
number = {1428},
pages = {1571-1577},
pmid = {10467746},
issn = {0962-8452},
mesh = {Animals ; *Biological Evolution ; DNA/genetics ; Eukaryotic Cells/*classification ; Genome ; Models, Genetic ; Phylogeny ; Prokaryotic Cells/*classification ; },
abstract = {Eukaryotes have long been thought to have arisen by evolving a nucleus, endomembrane, and cytoskeleton. In contrast, it was recently proposed that the first complex cells, which were actually proto-eukaryotes, arose simultaneously with the acquisition of mitochondria. This so-called symbiotic association hypothesis states that eukaryotes emerged when some ancient anaerobic archaebacteria (hosts) engulfed respiring alpha-proteobacteria (symbionts), which evolved into the first energy-producing organelles. Therefore, the intracellular compartmentalization of the energy-converting metabolism that was bound originally to the plasma membrane appears to be the key innovation towards eukaryotic genome and cellular organization. The novel energy metabolism made it possible for the nucleotide synthetic apparatus of cells to be no longer limited by subsaturation with substrates and catalytic components. As a consequence, a considerable increase has occurred in the size and complexity of eukaryotic genomes, providing the genetic basis for most of the further evolutionary changes in cellular complexity. On the other hand, the active uptake of exogenous DNA, which is general in bacteria, was no longer essential in the genome organization of eukaryotes. The mitochondrion-driven scenario for the first eukaryotes explains the chimera-like composition of eukaryotic genomes as well as the metabolic and cellular organization of eukaryotes.},
}

Animals
*Biological Evolution
DNA/genetics
Eukaryotic Cells/*classification
Genome
Models, Genetic
Phylogeny
Prokaryotic Cells/*classification

@article {pmid10486982,
year = {1999},
author = {Horner, DS and Hirt, RP and Embley, TM},
title = {A single eubacterial origin of eukaryotic pyruvate: ferredoxin oxidoreductase genes: implications for the evolution of anaerobic eukaryotes.},
journal = {Molecular biology and evolution},
volume = {16},
number = {9},
pages = {1280-1291},
doi = {10.1093/oxfordjournals.molbev.a026218},
pmid = {10486982},
issn = {0737-4038},
support = {//Wellcome Trust/United Kingdom ; },
mesh = {Anaerobiosis ; Animals ; Base Sequence ; Clostridium/enzymology/genetics ; DNA Primers/genetics ; Diplomonadida/enzymology/genetics ; Eukaryotic Cells ; *Evolution, Molecular ; Gene Duplication ; Gene Transfer, Horizontal ; *Genes, Bacterial ; Genes, Protozoan ; Giardia lamblia/enzymology/genetics ; Ketone Oxidoreductases/*genetics ; Models, Genetic ; Molecular Sequence Data ; Phylogeny ; Pyruvate Synthase ; },
abstract = {The iron sulfur protein pyruvate: ferredoxin oxidoreductase (PFO) is central to energy metabolism in amitochondriate eukaryotes, including those with hydrogenosomes. Thus, revealing the evolutionary history of PFO is critical to understanding the origin(s) of eukaryote anaerobic energy metabolism. We determined a complete PFO sequence for Spironucleus barkhanus, a large fragment of a PFO sequence from Clostridium pasteurianum, and a fragment of a new PFO from Giardia lamblia. Phylogenetic analyses of eubacterial and eukaryotic PFO genes suggest a complex history for PFO, including possible gene duplications and horizontal transfers among eubacteria. Our analyses favor a common origin for eukaryotic cytosolic and hydrogenosomal PFOs from a single eubacterial source, rather than from separate horizontal transfers as previously suggested. However, with the present sampling of genes and species, we were unable to infer a specific eubacterial sister group for eukaryotic PFO. Thus, we find no direct support for the published hypothesis that the donor of eukaryote PFO was the common alpha-proteobacterial ancestor of mitochondria and hydrogenosomes. We also report that several fungi and protists encode proteins with PFO domains that are likely monophyletic with PFOs from anaerobic protists. In Saccharomyces cerevisiae, PFO domains combine with fragments of other redox proteins to form fusion proteins which participate in methionine biosynthesis. Our results are consistent with the view that PFO, an enzyme previously considered to be specific to energy metabolism in amitochondriate protists, was present in the common ancestor of contemporary eukaryotes and was retained, wholly or in part, during the evolution of oxygen-dependent and mitochondrion-bearing lineages.},
}

Anaerobiosis
Animals
Base Sequence
Clostridium/enzymology/genetics
DNA Primers/genetics
Diplomonadida/enzymology/genetics
Eukaryotic Cells
*Evolution, Molecular
Gene Duplication
Gene Transfer, Horizontal
*Genes, Bacterial
Genes, Protozoan
Giardia lamblia/enzymology/genetics
Ketone Oxidoreductases/*genetics
Models, Genetic
Molecular Sequence Data
Phylogeny
Pyruvate Synthase

@article {pmid10508728,
year = {1999},
author = {Andersson, SG and Kurland, CG},
title = {Origins of mitochondria and hydrogenosomes.},
journal = {Current opinion in microbiology},
volume = {2},
number = {5},
pages = {535-541},
doi = {10.1016/s1369-5274(99)00013-2},
pmid = {10508728},
issn = {1369-5274},
mesh = {*Evolution, Molecular ; Genome, Bacterial ; Hydrogen/*metabolism ; Mitochondria/*genetics ; Organelles/*genetics ; },
abstract = {Complete genome sequences for many mitochondria, as well as for some bacteria, together with the nuclear genome sequence of yeast have provided a coherent view of the origin of mitochondria. In particular, conventional phylogenetic reconstructions with genes coding for proteins active in energy metabolism and translation have confirmed the simplest version of the endosymbiosis hypothesis. In contrast, the hydrogen and the syntrophy hypotheses for the origin of mitochondria do not receive support from the available data. It remains to be seen how the evolution of hydrogenosomes is related to that of mitochondria.},
}

*Evolution, Molecular
Genome, Bacterial
Hydrogen/*metabolism
Mitochondria/*genetics
Organelles/*genetics

@article {pmid10620491,
year = {2000},
author = {Ricquier, D and Bouillaud, F},
title = {The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP.},
journal = {The Biochemical journal},
volume = {345 Pt 2},
number = {Pt 2},
pages = {161-179},
pmid = {10620491},
issn = {0264-6021},
mesh = {Adipose Tissue, Brown/metabolism ; Amino Acid Sequence ; Animals ; Carrier Proteins/classification/genetics/*metabolism ; Energy Metabolism/*physiology ; Evolution, Molecular ; Hot Temperature ; Humans ; Mice ; Mitochondria/*metabolism ; Molecular Sequence Data ; Oxygen Consumption ; Plant Proteins/classification/genetics/metabolism ; Uncoupling Agents/*metabolism ; },
abstract = {Animal and plant uncoupling protein (UCP) homologues form a subfamily of mitochondrial carriers that are evolutionarily related and possibly derived from a proton/anion transporter ancestor. The brown adipose tissue (BAT) UCP1 has a marked and strongly regulated uncoupling activity, essential to the maintenance of body temperature in small mammals. UCP homologues identified in plants are induced in a cold environment and may be involved in resistance to chilling. The biochemical activities and biological functions of the recently identified mammalian UCP2 and UCP3 are not well known. However, recent data support a role for these UCPs in State 4 respiration, respiration uncoupling and proton leaks in mitochondria. Moreover, genetic studies suggest that UCP2 and UCP3 play a part in energy expenditure in humans. The UCPs may also be involved in adaptation of cellular metabolism to an excessive supply of substrates in order to regulate the ATP level, the NAD(+)/NADH ratio and various metabolic pathways, and to contain superoxide production. A major goal will be the analysis of mice that either lack the UCP2 or UCP3 gene or overexpress these genes. Other aims will be to investigate the possible roles of UCP2 and UCP3 in response to oxidative stress, lipid peroxidation, inflammatory processes, fever and regulation of temperature in certain specific parts of the body.},
}

Adipose Tissue, Brown/metabolism
Amino Acid Sequence
Animals
Carrier Proteins/classification/genetics/*metabolism
Energy Metabolism/*physiology
Evolution, Molecular
Hot Temperature
Humans
Mice
Mitochondria/*metabolism
Molecular Sequence Data
Oxygen Consumption
Plant Proteins/classification/genetics/metabolism
Uncoupling Agents/*metabolism

@article {pmid10629653,
year = {1999},
author = {Rocchi, E and Vigo, J and Viallet, P and Bonnard, I and Banaigs, B and Salmon, JM},
title = {Multiwavelength videomicrofluorometric study of cytotoxic properties of a marine peptide, didemnin B, using adriamycin as reference compound.},
journal = {Anticancer research},
volume = {19},
number = {4C},
pages = {3559-3568},
pmid = {10629653},
issn = {0250-7005},
mesh = {Apoptosis ; Benzimidazoles/metabolism ; Cell Cycle/drug effects ; Cell Nucleus/drug effects ; *Depsipeptides ; Dose-Response Relationship, Drug ; Doxorubicin/*chemistry/pharmacokinetics/pharmacology ; Fluorescent Dyes/metabolism ; Fluorometry ; Humans ; Inhibitory Concentration 50 ; Microscopy, Video ; Mitochondria/drug effects ; Oxazines/metabolism ; Peptides, Cyclic/*chemistry/*pharmacokinetics/pharmacology ; Rhodamine 123/metabolism ; Time Factors ; Tumor Cells, Cultured ; },
abstract = {Didemnin B (DB), a marine natural product, has very encouraging biological activity in vitro (Antineoplastic, immunosuppressive, antiviral). To learn more about its intracellular effects and targets, videomicrofluorometry on single living cells and a protocol of multiple labeling: Hoechst 342 for nuclear DNA, Rhodamine 123 for mitochondria and Nile Red for plasma membrane, have been used. DB behaves differently from Adriamycin, inducing at its IC50 dose of (20 nM) an accumulation of the CEM-WT lymphoblasts in the S phase of the cell cycle while we observed a 50% decrease of the mitochondrial labeling by R123, showing a decrease of the mitochondrial energetic state. Cytostatic dose of DB (250 nM) confirms these observations. However the treatment with a dose reported as apoptotic (1000 nM) induces a much faster effect (corresponding to that of 72 hours at the IC50 dose), 24 hours incubation induced a drastic decrease of nuclear DNA content as well as of the mitochondria energetic state. The evolution of NAD(P)H cellular content exhibited an increase that seems to indicate that the decrease of mitochondrial energetic state was dependent on inhibition of the mitochondrial activity due to an effect of DB at the mitochondrial level, either direct or mediated. Furthermore, the decrease of mitochondrial labeling appears as a very early event in the mechanisms leading to apoptosis.},
}

Apoptosis
Benzimidazoles/metabolism
Cell Cycle/drug effects
Cell Nucleus/drug effects
*Depsipeptides
Dose-Response Relationship, Drug
Doxorubicin/*chemistry/pharmacokinetics/pharmacology
Fluorescent Dyes/metabolism
Fluorometry
Humans
Inhibitory Concentration 50
Microscopy, Video
Mitochondria/drug effects
Oxazines/metabolism
Peptides, Cyclic/*chemistry/*pharmacokinetics/pharmacology
Rhodamine 123/metabolism
Time Factors
Tumor Cells, Cultured

@article {pmid10644738,
year = {2000},
author = {Saas, J and Ziegelbauer, K and von Haeseler, A and Fast, B and Boshart, M},
title = {A developmentally regulated aconitase related to iron-regulatory protein-1 is localized in the cytoplasm and in the mitochondrion of Trypanosoma brucei.},
journal = {The Journal of biological chemistry},
volume = {275},
number = {4},
pages = {2745-2755},
doi = {10.1074/jbc.275.4.2745},
pmid = {10644738},
issn = {0021-9258},
mesh = {Aconitate Hydratase/*genetics/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Cytoplasm/*enzymology ; DNA, Complementary ; *Gene Expression Regulation, Enzymologic ; Iron Regulatory Protein 1 ; Iron-Regulatory Proteins ; Iron-Sulfur Proteins/*genetics ; Kinetics ; Mitochondria/*enzymology ; Molecular Sequence Data ; Open Reading Frames ; Phylogeny ; RNA-Binding Proteins/*genetics ; Recombinant Proteins/genetics/metabolism ; Sequence Homology, Amino Acid ; Trypanosoma brucei brucei/*enzymology ; },
abstract = {Mitochondrial energy metabolism and Krebs cycle activities are developmentally regulated in the life cycle of the protozoan parasite Trypanosoma brucei. Here we report cloning of a T. brucei aconitase gene that is closely related to mammalian iron-regulatory protein 1 (IRP-1) and plant aconitases. Kinetic analysis of purified recombinant TbACO expressed in Escherichia coli resulted in a K(m) (isocitrate) of 3 +/- 0.4 mM, similar to aconitases of other organisms. This was unexpected since an arginine conserved in the aconitase protein family and crucial for substrate positioning in the catalytic center and for activity of pig mitochondrial aconitase (Zheng, L., Kennedy, M. C., Beinert, H., and Zalkin, H. (1992) J. Biol. Chem. 267, 7895-7903) is substituted by leucine in the TbACO sequence. Expression of the 98-kDa TbACO was shown to be lowest in the slender bloodstream stage of the parasite, 8-fold elevated in the stumpy stage, and increased a further 4-fold in the procyclic stage. The differential expression of TbACO protein contrasted with only minor changes in TbACO mRNA, indicating translational or post-translational mechanisms of regulation. Whereas animal cells express two distinct compartmentalized aconitases, mitochondrial aconitase and cytoplasmic aconitase/IRP-1, TbACO accounts for total aconitase activity in trypanosomes. By cell fractionation and immunofluorescence microscopy, we show that native as well as a transfected epitope-tagged TbACO localizes in both the mitochondrion (30%) and in the cytoplasm (70%). Together with phylogenetic reconstructions of the aconitase family, this suggests that animal IRPs have evolved from a multicompartmentalized ancestral aconitase. The possible functions of a cytoplasmic aconitase in trypanosomes are discussed.},
}

Aconitate Hydratase/*genetics/metabolism
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Cytoplasm/*enzymology
DNA, Complementary
*Gene Expression Regulation, Enzymologic
Iron Regulatory Protein 1
Iron-Regulatory Proteins
Iron-Sulfur Proteins/*genetics
Kinetics
Mitochondria/*enzymology
Molecular Sequence Data
Open Reading Frames
Phylogeny
RNA-Binding Proteins/*genetics
Recombinant Proteins/genetics/metabolism
Sequence Homology, Amino Acid
Trypanosoma brucei brucei/*enzymology

@article {pmid10713172,
year = {2000},
author = {Dyall, SD and Koehler, CM and Delgadillo-Correa, MG and Bradley, PJ and Plümper, E and Leuenberger, D and Turck, CW and Johnson, PJ},
title = {Presence of a member of the mitochondrial carrier family in hydrogenosomes: conservation of membrane-targeting pathways between hydrogenosomes and mitochondria.},
journal = {Molecular and cellular biology},
volume = {20},
number = {7},
pages = {2488-2497},
pmid = {10713172},
issn = {0270-7306},
support = {T32 AI007323/AI/NIAID NIH HHS/United States ; R01 AI027857/AI/NIAID NIH HHS/United States ; AI07323/AI/NIAID NIH HHS/United States ; AI27857/AI/NIAID NIH HHS/United States ; /WT_/Wellcome Trust/United Kingdom ; R37 AI027857/AI/NIAID NIH HHS/United States ; },
mesh = {Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*genetics/metabolism ; Cloning, Molecular ; Energy Metabolism ; Evolution, Molecular ; Fungal Proteins/chemistry ; Membrane Proteins/chemistry/genetics/metabolism ; Mitochondria/*metabolism ; Mitochondrial ADP, ATP Translocases/chemistry/genetics/metabolism ; Molecular Sequence Data ; Phylogeny ; Protein Sorting Signals/chemistry/metabolism ; Protozoan Proteins/chemistry/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Trichomonas vaginalis/*chemistry/cytology ; },
abstract = {A number of microaerophilic eukaryotes lack mitochondria but possess another organelle involved in energy metabolism, the hydrogenosome. Limited phylogenetic analyses of nuclear genes support a common origin for these two organelles. We have identified a protein of the mitochondrial carrier family in the hydrogenosome of Trichomonas vaginalis and have shown that this protein, Hmp31, is phylogenetically related to the mitochondrial ADP-ATP carrier (AAC). We demonstrate that the hydrogenosomal AAC can be targeted to the inner membrane of mitochondria isolated from Saccharomyces cerevisiae through the Tim9-Tim10 import pathway used for the assembly of mitochondrial carrier proteins. Conversely, yeast mitochondrial AAC can be targeted into the membranes of hydrogenosomes. The hydrogenosomal AAC contains a cleavable, N-terminal presequence; however, this sequence is not necessary for targeting the protein to the organelle. These data indicate that the membrane-targeting signal(s) for hydrogenosomal AAC is internal, similar to that found for mitochondrial carrier proteins. Our findings indicate that the membrane carriers and membrane protein-targeting machinery of hydrogenosomes and mitochondria have a common evolutionary origin. Together, they provide strong evidence that a single endosymbiont evolved into a progenitor organelle in early eukaryotic cells that ultimately give rise to these two distinct organelles and support the hydrogen hypothesis for the origin of the eukaryotic cell.},
}

Amino Acid Sequence
Animals
Carrier Proteins/chemistry/*genetics/metabolism
Cloning, Molecular
Energy Metabolism
Evolution, Molecular
Fungal Proteins/chemistry
Membrane Proteins/chemistry/genetics/metabolism
Mitochondria/*metabolism
Mitochondrial ADP, ATP Translocases/chemistry/genetics/metabolism
Molecular Sequence Data
Phylogeny
Protein Sorting Signals/chemistry/metabolism
Protozoan Proteins/chemistry/*genetics/metabolism
*Saccharomyces cerevisiae Proteins
Sequence Alignment
Trichomonas vaginalis/*chemistry/cytology

@article {pmid10867997,
year = {2000},
author = {Schipke, JD and Birkenkamp-Demtröder, K and Schwanke, U},
title = {[Myocardial hibernation: another view].},
journal = {Zeitschrift fur Kardiologie},
volume = {89},
number = {4},
pages = {259-263},
doi = {10.1007/s003920050482},
pmid = {10867997},
issn = {0300-5860},
mesh = {Animals ; Biological Evolution ; Coronary Circulation/*physiology ; Energy Metabolism/*physiology ; Humans ; Myocardial Stunning/*physiopathology ; Opioid Peptides/physiology ; Oxygen Consumption/*physiology ; },
abstract = {In the following, three newer concepts are brought together: myocardial hibernation, heterogeneity in myocardial blood flow and oxidative metabolism, and effects of hibernating animal serum on non-hibernators. Myocardial hibernation is viewed as a protective mechanism that helps to maintain myocardial integrity and viability by down-regulating contractile function as an adaptation to reduced blood flow. Myocardial flow is considerably heterogeneous. Consequently, oxygen supply to the myocardium is also heterogeneous. Many lines of evidence show a close correlation between regional flow and regional metabolism. In low-flow/low-metabolism areas, myocardial function must be reduced, since the myocardium would otherwise undergo necrosis. Thus, others and we hypothesize that function must be down-regulated to induce hibernation in low-flow areas. Because no regional histologic differences exist (the mitochondria are uniformly distributed within the myocardium), the pattern of heterogeneity seems to shift over time. Hence, we hypothesize that such very regional hibernation presents an evolutionary, protective mechanism, permitting subsequent myocardial areas to rest within the ceaselessly working heart. We also hypothesize that this mechanism ensures the down-regulation of function following myocardial ischemia in order to induce myocardial hibernation on a broader level. Surprisingly, a substance (opioid in nature) contained in hibernator serum both induced hibernation-like state in non-hibernators and suppressed myocardial oxygen consumption. Thus, we lastly hypothesize that myocardial hibernation is a remnant of the early stages of evolution and is closer to physiologic hibernation than traditionally viewed.},
}

Animals
Biological Evolution
Coronary Circulation/*physiology
Energy Metabolism/*physiology
Humans
Myocardial Stunning/*physiopathology
Opioid Peptides/physiology
Oxygen Consumption/*physiology

@article {pmid11063052,
year = {2000},
author = {Fiskum, G},
title = {Mitochondrial participation in ischemic and traumatic neural cell death.},
journal = {Journal of neurotrauma},
volume = {17},
number = {10},
pages = {843-855},
doi = {10.1089/neu.2000.17.843},
pmid = {11063052},
issn = {0897-7151},
support = {NS34152/NS/NINDS NIH HHS/United States ; },
mesh = {Animals ; Apoptosis/*physiology ; Astrocytes/metabolism ; Brain Injuries/*metabolism/pathology/physiopathology ; Brain Ischemia/*metabolism/pathology/physiopathology ; Calcium/metabolism ; Cytochrome c Group/metabolism ; Energy Metabolism/physiology ; Humans ; Mitochondria/*metabolism/pathology ; Nerve Degeneration/*metabolism/pathology/physiopathology ; Neurons/metabolism ; Neurotoxins/metabolism ; Reactive Oxygen Species/metabolism ; },
abstract = {Mitochondria play critical roles in cerebral energy metabolism and in the regulation of cellular Ca2+ homeostasis. They are also the primary intracellular source of reactive oxygen species, due to the tremendous number of oxidation-reduction reactions and the massive utilization of O2 that occur there. Metabolic trafficking among cells is also highly dependent upon normal, well-controlled mitochondrial activities. Alterations of any of these functions can cause cell death directly or precipitate death indirectly by compromising the ability of cells to withstand stressful stimuli. Abnormal accumulation of Ca2+ by mitochondria in response to exposure of neurons to excitotoxic levels of excitatory neurotransmitters, for example, glutamate, is a primary mediator of mitochondrial dysfunction and delayed cell death. Excitoxicity, along with inflammatory reactions, mechanical stress, and altered trophic signal transduction, all likely contribute to mitochondrial damage observed during the evolution of traumatic brain injury. The release of apoptogenic proteins from mitochondria into the cytosol serves as a primary mechanism responsible for inducing apoptosis, a form of cell death that contributes significantly to neurologic impairment following neurotrauma. Although several signals for the release of mitochondrial cell death proteins have been identified, the mechanisms by which these signals increase the permeability of the mitochondrial outer membrane to apoptogenic proteins is controversial. Elucidation of the precise biochemical mechanisms responsible for mitochondrial dysfunction during neurotrauma and the roles that mitochondria play in both necrotic and apoptotic cell death should provide new molecular targets for neuroprotective interventions.},
}

Animals
Apoptosis/*physiology
Astrocytes/metabolism
Brain Injuries/*metabolism/pathology/physiopathology
Brain Ischemia/*metabolism/pathology/physiopathology
Calcium/metabolism
Cytochrome c Group/metabolism
Energy Metabolism/physiology
Humans
Mitochondria/*metabolism/pathology
Nerve Degeneration/*metabolism/pathology/physiopathology
Neurons/metabolism
Neurotoxins/metabolism
Reactive Oxygen Species/metabolism

@article {pmid11104819,
year = {2000},
author = {Kurland, CG and Andersson, SG},
title = {Origin and evolution of the mitochondrial proteome.},
journal = {Microbiology and molecular biology reviews : MMBR},
volume = {64},
number = {4},
pages = {786-820},
pmid = {11104819},
issn = {1092-2172},
mesh = {Alphaproteobacteria/genetics ; *Biological Evolution ; Energy Metabolism ; Eukaryotic Cells ; *Mitochondria/genetics ; Models, Biological ; *Proteome ; Saccharomyces cerevisiae/physiology ; Symbiosis ; },
abstract = {The endosymbiotic theory for the origin of mitochondria requires substantial modification. The three identifiable ancestral sources to the proteome of mitochondria are proteins descended from the ancestral alpha-proteobacteria symbiont, proteins with no homology to bacterial orthologs, and diverse proteins with bacterial affinities not derived from alpha-proteobacteria. Random mutations in the form of deletions large and small seem to have eliminated nonessential genes from the endosymbiont-mitochondrial genome lineages. This process, together with the transfer of genes from the endosymbiont-mitochondrial genome to nuclei, has led to a marked reduction in the size of mitochondrial genomes. All proteins of bacterial descent that are encoded by nuclear genes were probably transferred by the same mechanism, involving the disintegration of mitochondria or bacteria by the intracellular membranous vacuoles of cells to release nucleic acid fragments that transform the nuclear genome. This ongoing process has intermittently introduced bacterial genes to nuclear genomes. The genomes of the last common ancestor of all organisms, in particular of mitochondria, encoded cytochrome oxidase homologues. There are no phylogenetic indications either in the mitochondrial proteome or in the nuclear genomes that the initial or subsequent function of the ancestor to the mitochondria was anaerobic. In contrast, there are indications that relatively advanced eukaryotes adapted to anaerobiosis by dismantling their mitochondria and refitting them as hydrogenosomes. Accordingly, a continuous history of aerobic respiration seems to have been the fate of most mitochondrial lineages. The initial phases of this history may have involved aerobic respiration by the symbiont functioning as a scavenger of toxic oxygen. The transition to mitochondria capable of active ATP export to the host cell seems to have required recruitment of eukaryotic ATP transport proteins from the nucleus. The identity of the ancestral host of the alpha-proteobacterial endosymbiont is unclear, but there is no indication that it was an autotroph. There are no indications of a specific alpha-proteobacterial origin to genes for glycolysis. In the absence of data to the contrary, it is assumed that the ancestral host cell was a heterotroph.},
}

Alphaproteobacteria/genetics
*Biological Evolution
Energy Metabolism
Eukaryotic Cells
*Mitochondria/genetics
Models, Biological
*Proteome
Saccharomyces cerevisiae/physiology
Symbiosis

@article {pmid11121736,
year = {2000},
author = {Schneider, A and Maréchal-Drouard, L},
title = {Mitochondrial tRNA import: are there distinct mechanisms?.},
journal = {Trends in cell biology},
volume = {10},
number = {12},
pages = {509-513},
doi = {10.1016/s0962-8924(00)01854-7},
pmid = {11121736},
issn = {0962-8924},
mesh = {Animals ; Biological Transport ; Cell Nucleus/genetics/metabolism ; Humans ; Mitochondria/*genetics/metabolism ; Models, Biological ; Nucleic Acid Conformation ; Phylogeny ; RNA/genetics/*metabolism ; RNA, Mitochondrial ; RNA, Transfer/genetics/*metabolism ; },
abstract = {Sequence information from an increasing number of complete mitochondrial genomes indicates that a large number of evolutionary distinct organisms import nucleus-encoded tRNAs. In the past five years, much research has been initiated on the features of imported tRNAs, the mechanism and the energetics of the process as well as on the components of the import machinery. In summary, these studies show that the import systems of different species exhibit some unique features, suggesting that more than one mechanism might exist to import tRNAs.},
}

Animals
Biological Transport
Cell Nucleus/genetics/metabolism
Humans
Mitochondria/*genetics/metabolism
Models, Biological
Nucleic Acid Conformation
Phylogeny
RNA/genetics/*metabolism
RNA, Mitochondrial
RNA, Transfer/genetics/*metabolism

@article {pmid11212890,
year = {2000},
author = {Beech, PL and Landweber, LF and Gilson, PR},
title = {Meeting report: XIIIth meeting of the International Society for Evolutionary Protistology, Ceské Budejovice, Czech Republic, July 31-August 4, 2000.},
journal = {Protist},
volume = {151},
number = {4},
pages = {299-305},
doi = {10.1078/S1434-4610(04)70028-0},
pmid = {11212890},
issn = {1434-4610},
support = {GM59708/GM/NIGMS NIH HHS/United States ; },
mesh = {Animals ; *Biological Evolution ; Chloroplasts/physiology ; Ciliophora/physiology ; *Energy Metabolism ; Euglenida/physiology ; Eukaryota/*physiology ; Eukaryotic Cells/*physiology ; Microsporidia/physiology ; Mitochondria/metabolism ; Organelles/metabolism ; Trypanosoma/physiology ; },
}

Animals
*Biological Evolution
Chloroplasts/physiology
Ciliophora/physiology
*Energy Metabolism
Euglenida/physiology
Eukaryota/*physiology
Eukaryotic Cells/*physiology
Microsporidia/physiology
Mitochondria/metabolism
Organelles/metabolism
Trypanosoma/physiology

@article {pmid11357388,
year = {2001},
author = {Kuznetsov, AP and Lebkova, NP},
title = {[Significance of the energy of symbiotic bacteria in metabolism of hydrothermal and other chemotrophic biota of the ocean].},
journal = {Izvestiia Akademii nauk. Seriia biologicheskaia},
volume = {},
number = {2},
pages = {220-226},
pmid = {11357388},
issn = {1026-3470},
mesh = {Aerobiosis ; Animals ; Bacteria/*metabolism ; Biological Evolution ; Ecosystem ; *Energy Metabolism ; Microscopy, Electron ; Mitochondria/*metabolism ; Mollusca/*metabolism/microbiology/ultrastructure ; Oceans and Seas ; Symbiosis ; },
abstract = {The bacterial origin of eukaryotic mitochondria, specifically in Metazoa, as a mechanism of their basic (aerobic) respiration and the role of symbiotic bacteria during the supply of energy to the metazoan host is proved for the first time from the viewpoint of the monophyletic development of the organic world and the origin of eukaryotes as descendants of prokaryotes Representatives of the hydrothermal bacteriochemosymbiotrophic bottom fauna of the open sea were used as examples.},
}

Aerobiosis
Animals
Bacteria/*metabolism
Biological Evolution
Ecosystem
*Energy Metabolism
Microscopy, Electron
Mitochondria/*metabolism
Mollusca/*metabolism/microbiology/ultrastructure
Oceans and Seas
Symbiosis

@article {pmid11377800,
year = {2001},
author = {Scheffler, IE},
title = {Mitochondria make a come back.},
journal = {Advanced drug delivery reviews},
volume = {49},
number = {1-2},
pages = {3-26},
doi = {10.1016/s0169-409x(01)00123-5},
pmid = {11377800},
issn = {0169-409X},
mesh = {Animals ; Biological Evolution ; DNA, Mitochondrial/drug effects/*physiology/ultrastructure ; Electron Transport/drug effects/physiology ; Energy Metabolism ; Enzyme Inhibitors/pharmacology ; Eukaryotic Cells/drug effects/*physiology/ultrastructure ; Humans ; Mitochondria/drug effects/*physiology/ultrastructure ; Molecular Biology ; Oxidative Phosphorylation/drug effects ; },
abstract = {This review attempts to summarize our present state of knowledge of mitochondria in relation to a number of areas of biology, and to indicate where future research might be directed. In the evolution of eukaryotic cells mitochondria have for a long time played a prominent role. Nowadays their integration into many activities of a cell, and their dynamic behavior as subcellular organelles within a cell and during cell division are a major focus of attention. The crystal structures of the major complexes of the electron transport chain (except complex I) have been established, permitting increasingly detailed analyses of the important mechanism of proton pumping coupled to electron transport. The mitochondrial genome and its replication and expression are beginning to be understood in considerable detail, but more questions remain with regard to mutations and their repair, and the segregation of the mtDNA in oogenesis and development. Much emphasis and a large effort have recently been devoted to understand the role of mitochondria in programmed cell death (apoptosis). The understanding of their central role in mitochondrial diseases is a major achievement of the past decade. Finally, various drugs have traditionally played a part in understanding biochemical mechanisms within mitochondria; the repertoire of drugs with novel and interesting targets is expanding.},
}

Animals
Biological Evolution
DNA, Mitochondrial/drug effects/*physiology/ultrastructure
Electron Transport/drug effects/physiology
Energy Metabolism
Enzyme Inhibitors/pharmacology
Eukaryotic Cells/drug effects/*physiology/ultrastructure
Humans
Mitochondria/drug effects/*physiology/ultrastructure
Molecular Biology
Oxidative Phosphorylation/drug effects

@article {pmid11457448,
year = {2001},
author = {Emelyanov, VV},
title = {Evolutionary relationship of Rickettsiae and mitochondria.},
journal = {FEBS letters},
volume = {501},
number = {1},
pages = {11-18},
doi = {10.1016/s0014-5793(01)02618-7},
pmid = {11457448},
issn = {0014-5793},
mesh = {Energy Metabolism ; Genome ; Mitochondria/genetics/metabolism/*physiology ; *Models, Biological ; *Phylogeny ; Rickettsia/classification/genetics/*physiology ; Symbiosis ; },
abstract = {Phylogenetic data support an origin of mitochondria from the alpha-proteobacterial order Rickettsiales. This high-rank taxon comprises exceptionally obligate intracellular endosymbionts of eukaryotic cells, and includes family Rickettsiaceae and a group of microorganisms termed Rickettsia-like endosymbionts (RLEs). Most detailed phylogenetic analyses of small subunit rRNA and chaperonin 60 sequences consistently show the RLEs to have emerged before Rickettsiaceae and mitochondria sister clades. These data suggest that the origin of mitochondria and Rickettsiae has been preceded by the long-term mutualistic relationship of an intracellular bacterium with a pro-eukaryote, in which an invader has lost many dispensable genes, yet evolved carrier proteins to exchange respiration-derived ATP for host metabolites as envisaged in classic endosymbiont theory.},
}

Energy Metabolism
Genome
Mitochondria/genetics/metabolism/*physiology
*Models, Biological
*Phylogeny
Rickettsia/classification/genetics/*physiology
Symbiosis

@article {pmid11508688,
year = {2001},
author = {Emelyanov, VV},
title = {Rickettsiaceae, rickettsia-like endosymbionts, and the origin of mitochondria.},
journal = {Bioscience reports},
volume = {21},
number = {1},
pages = {1-17},
doi = {10.1023/a:1010409415723},
pmid = {11508688},
issn = {0144-8463},
mesh = {Animals ; Bacteria/cytology/genetics/metabolism ; Chaperonin 60/genetics/metabolism ; Energy Metabolism/genetics ; Eukaryotic Cells/*cytology/metabolism ; Humans ; Mitochondria/genetics/metabolism/*ultrastructure ; *Phylogeny ; Rickettsiaceae/*cytology/genetics/metabolism ; Symbiosis/*genetics ; },
abstract = {Accumulating evolutionary data point to a monophyletic origin of mitochondria from the order Rickettsiales. This large group of obligate intracellular alpha-Proteobacteria includes the family Rickettsiaceae and several rickettsia-like endosymbionts (RLEs). Detailed phylogenetic analysis of small subunit (SSU) rRNA and chaperonin 60 (Cpn60) sequences testify to polyphyly of the Rickettsiales, and consistently indicate a sisterhood of Rickettsiaceae and mitochondria that excludes RLEs. Thus RLEs are considered as the nearest extant relatives of an extinct last common ancestor of mitochondria and rickettsiae. Phylogenetic inferences prompt the following assumptions. (1) Mitochondrial origin has been predisposed by the long-term endosymbiotic relationship between rickettsia-like bacteria and proto-eukaryotes, in which many endosymbiont genes have been lost while some indispensable genes have been transferred to the host genome. (2) The obligate dependence of rickettsiae upon a eukaryotic host rests on the import of proteins encoded by these transferred genes. The nature of a proto-eukaryotic cell still remains elusive. The divergence of Rickettsiaceae and mitochondria based on Cpn60, and the evolutionary history of two aminoacyl-tRNA synthetases favor the hypothesis that it was a chimera created by fusion of an archaebacterium and a eubacterium not long before an endosymbiotic event. These and other, mostly biochemical data suggest that all the mitochondrion-related organelles, i.e., both aerobically and anaerobically respiring mitochondria and hydrogenosomes, have originated from the same RLE, while hydrogenosomal energy metabolism may have a separate origin resulting from a eubacterial fusion partner.},
}

Animals
Bacteria/cytology/genetics/metabolism
Chaperonin 60/genetics/metabolism
Energy Metabolism/genetics
Eukaryotic Cells/*cytology/metabolism
Humans
Mitochondria/genetics/metabolism/*ultrastructure
*Phylogeny
Rickettsiaceae/*cytology/genetics/metabolism
Symbiosis/*genetics

@article {pmid11557797,
year = {2001},
author = {Tachezy, J and Sánchez, LB and Müller, M},
title = {Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS.},
journal = {Molecular biology and evolution},
volume = {18},
number = {10},
pages = {1919-1928},
doi = {10.1093/oxfordjournals.molbev.a003732},
pmid = {11557797},
issn = {0737-4038},
support = {AI11942/AI/NIAID NIH HHS/United States ; },
mesh = {Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics ; Carbon-Sulfur Lyases/*genetics/metabolism ; DNA, Protozoan/chemistry/genetics ; Giardia lamblia/enzymology/*genetics ; Iron-Sulfur Proteins/*biosynthesis ; Mitochondria/*metabolism ; Molecular Sequence Data ; *Phylogeny ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Trichomonas vaginalis/enzymology/*genetics ; },
abstract = {Pyridoxal-5'-phosphate-dependent cysteine desulfurase (IscS) is an essential enzyme in the assembly of FeS clusters in bacteria as well as in the mitochondria of eukaryotes. Although FeS proteins are particularly important for the energy metabolism of amitochondrial anaerobic eukaryotes, there is no information about FeS cluster formation in these organisms. We identified and sequenced two IscS homologs of Trichomonas vaginalis (TviscS-1 and TviscS-2) and one of Giardia intestinalis (GiiscS). TviscS-1, TviscS-2, and GiiscS possess the typical conserved regions implicated in cysteine desulfurase activity. N-termini of TviscS-1 and TviscS-2 possess eight amino acid extensions, which resemble the N-terminal presequences that target proteins to hydrogenosomes in trichomonads. No presequence was evident in GiiscS from Giardia, an organism that apparently lacks hydrogenosmes or mitochondria. Phylogenetic analysis showed a close relationship among all eukaryotic IscS genes including those of amitochondriates. IscS of proteobacteria formed a sister group to the eukaryotic clade, suggesting that isc-related genes were present in the proteobacterial endosymbiotic ancestor of mitochondria and hydrogenosomes. NifS genes of nitrogen-fixing bacteria, which are IscS homologs required for specific formation of FeS clusters in nitrogenase, formed a more distant group. The phylogeny indicates the presence of a common mechanism for FeS cluster formation in mitochondriates as well as in amitochondriate eukaryotes. Furthermore, the analyses support a common origin of Trichomonas hydrogenosomes and mitochondria, as well as secondary loss of mitochondrion/hydrogenosome-like organelles in Giardia.},
}

Amino Acid Sequence
Animals
Bacterial Proteins/genetics
Carbon-Sulfur Lyases/*genetics/metabolism
DNA, Protozoan/chemistry/genetics
Giardia lamblia/enzymology/*genetics
Iron-Sulfur Proteins/*biosynthesis
Mitochondria/*metabolism
Molecular Sequence Data
*Phylogeny
Sequence Alignment
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Trichomonas vaginalis/enzymology/*genetics

@article {pmid11560369,
year = {2001},
author = {Heininger, K},
title = {The deprivation syndrome is the driving force of phylogeny, ontogeny and oncogeny.},
journal = {Reviews in the neurosciences},
volume = {12},
number = {3},
pages = {217-287},
doi = {10.1515/revneuro.2001.12.3.217},
pmid = {11560369},
issn = {0334-1763},
mesh = {Aging/physiology ; Animals ; Apoptosis/physiology ; Cell Communication/physiology ; Cell Differentiation/physiology ; Energy Metabolism/*physiology ; General Adaptation Syndrome/*physiopathology ; Homeostasis ; Mitochondria/metabolism ; Mutagenesis ; Neoplasms/*physiopathology ; *Phylogeny ; Prokaryotic Cells/*physiology ; Sex ; Signal Transduction/physiology ; *Stress, Physiological ; },
abstract = {Energy is the motor of life. Energy ensures the organism's survival and competitive advantage for reproductive success. For almost 3 billion years, unicellular organisms were the only life form on earth. Competition for limited energy resources and raw materials exerted an incessant selective pressure on organisms. In the adverse environment and due to their 'feast and famine' life style, hardiness to a variety of stressors, particularly to nutrient deprivation, was the selection principle. Both resistance and mutagenic adaptation to stressors were established as survival strategies by means of context-specific processes creating stability or variability of DNA sequence. The conservation of transduction pathways and functional homology of effector molecules clearly bear witness that the principles of life established during prokaryotic and eukaryotic unicellular evolution, although later diversified, have been unshakably cast to persist during metazoan phylogenesis. A wealth of evidence suggests that unicellular organisms evolved the phenomena of differentiation and apoptosis, sexual reproduction, and even aging, as responses to environmental challenges. These evolutionary accomplishments were elaborated from the dichotomous resistance/mutagenesis response and sophisticated the capacity of cells to tune their genetic information to changing environmental conditions. Notably, the social deprivation responses, differentiation and apoptosis, evolved as intercellularly coordinated events: a multitude of differentiation processes were elaborated from sporulation, the prototypic stress resistance response, while apoptosis, contrary to current concepts, is no altruistic cell suicide but was programmed as a mutagenic survival response; this response, however, is socially thwarted leading into mutagenic error catastrophe. In the hybrid differentiation-apoptosis process, cytocide and cannibalism of apoptotic cells thus serve the purpose of fueling the survival of the selfish genes in the differentiating cells. However, successful mutagenesis, although repressed, persisted in the asocial stress response of carcinogenesis as a regression to primitive unicellular behavior following failure of intercellular communication. While somatic mutagenesis was largely prevented, Metazoa elaborated germ cell mutagenesis as an evolutionary vehicle. Genetic competence, a primitive, stress-induced mating behavior, evolved into sexual reproduction which harnessed mutagenesis by subjecting highly mutable germ cells to a rigid viability selection. These processes were programmatically fixed as life- and cell-cycle events but retained their deprivation response phenotypes. Thus, the differentiation-apoptosis tandem evolved as the 'clay' to mold the specialized structures and functions of a multicellular organism while sexual reproduction elaborated the principle of quality-checked mutagenesis to create the immense diversity of Metazoa following the Cambrian explosion. Throughout these events, reactive oxygen and nitrogen species, which are regulated by energy homeostasis, shape the genetic information in a regulated but random, uncoded process providing the fitness-related feedback of phenotype to genotype. The interplay of genes and environment establishes a dynamic stimulus-response feedback cycle which, in animate nature, may be the organizing principle to contrive the reciprocal duality of energy and matter.},
}

Aging/physiology
Animals
Apoptosis/physiology
Cell Communication/physiology
Cell Differentiation/physiology
Energy Metabolism/*physiology
General Adaptation Syndrome/*physiopathology
Homeostasis
Mitochondria/metabolism
Mutagenesis
Neoplasms/*physiopathology
*Phylogeny
Prokaryotic Cells/*physiology
Sex
Signal Transduction/physiology
*Stress, Physiological

@article {pmid11767942,
year = {2001},
author = {Martin, W and Hoffmeister, M and Rotte, C and Henze, K},
title = {An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle.},
journal = {Biological chemistry},
volume = {382},
number = {11},
pages = {1521-1539},
doi = {10.1515/BC.2001.187},
pmid = {11767942},
issn = {1431-6730},
mesh = {Adenosine Triphosphate/*biosynthesis ; *Biological Evolution ; Mitochondria/*metabolism ; Models, Biological ; Organelles/*metabolism ; *Plant Physiological Phenomena ; Plants/*metabolism/ultrastructure ; },
abstract = {The evolutionary processes underlying the differentness of prokaryotic and eukaryotic cells and the origin of the latter's organelles are still poorly understood. For about 100 years, the principle of endosymbiosis has figured into thoughts as to how these processes might have occurred. A number of models that have been discussed in the literature and that are designed to explain this difference are summarized. The evolutionary histories of the enzymes of anaerobic energy metabolism (oxygen-independent ATP synthesis) in the three basic types of heterotrophic eukaryotes those that lack organelles of ATP synthesis, those that possess mitochondria and those that possess hydrogenosomes--play an important role in this issue. Traditional endosymbiotic models generally do not address the origin of the heterotrophic lifestyle and anaerobic energy metabolism in eukaryotes. Rather they take it as a given, a direct inheritance from the host that acquired mitochondria. Traditional models are contrasted to an alternative endosymbiotic model (the hydrogen hypothesis), which addresses the origin of heterotrophy and the origin of compartmentalized energy metabolism in eukaryotes.},
}

Adenosine Triphosphate/*biosynthesis
*Biological Evolution
Mitochondria/*metabolism
Models, Biological
Organelles/*metabolism
*Plant Physiological Phenomena
Plants/*metabolism/ultrastructure

@article {pmid11779548,
year = {2001},
author = {Castresana, J},
title = {Comparative genomics and bioenergetics.},
journal = {Biochimica et biophysica acta},
volume = {1506},
number = {3},
pages = {147-162},
doi = {10.1016/s0005-2728(01)00227-4},
pmid = {11779548},
issn = {0006-3002},
mesh = {Archaea/enzymology/*genetics ; Bacteria/enzymology/*genetics ; *Energy Metabolism ; Evolution, Molecular ; *Genomics ; Photosynthesis ; Phylogeny ; },
abstract = {Bacterial and archaeal complete genome sequences have been obtained from a wide range of evolutionary lines, which allows some general conclusions about the phylogenetic distribution and evolution of bioenergetic pathways to be drawn. In particular, I searched in the complete genomes for key enzymes involved in aerobic and anaerobic respiratory pathways and in photosynthesis, and mapped them into an rRNA tree of sequenced species. The phylogenetic distribution of these enzymes is very irregular, and clearly shows the diverse strategies of energy conservation used by prokaryotes. In addition, a thorough phylogenetic analysis of other bioenergetic protein families of wide distribution reveals a complex evolutionary history for the respective genes. A parsimonious explanation for these complex phylogenetic patterns and for the irregular distribution of metabolic pathways is that the last common ancestor of Bacteria and Archaea contained several members of every gene family as a consequence of previous gene or genome duplications, while different patterns of gene loss occurred during the evolution of every gene family. This would imply that the last universal ancestor was a bioenergetically sophisticated organism. Finally, important steps that occurred during the evolution of energetic machineries, such as the early evolution of aerobic respiration and the acquisition of eukaryotic mitochondria from a proteobacterium ancestor, are supported by the analysis of the complete genome sequences.},
}

Archaea/enzymology/*genetics
Bacteria/enzymology/*genetics
*Energy Metabolism
Evolution, Molecular
*Genomics
Photosynthesis
Phylogeny

@article {pmid11801237,
year = {2002},
author = {Sluse, FE and Jarmuszkiewicz, W},
title = {Uncoupling proteins outside the animal and plant kingdoms: functional and evolutionary aspects.},
journal = {FEBS letters},
volume = {510},
number = {3},
pages = {117-120},
doi = {10.1016/s0014-5793(01)03229-x},
pmid = {11801237},
issn = {0014-5793},
mesh = {Acanthamoeba/*metabolism ; Animals ; Candida/*metabolism ; Carrier Proteins/*metabolism ; Dictyostelium/*metabolism ; Energy Metabolism/physiology ; *Evolution, Molecular ; Ion Channels ; Membrane Proteins/*metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins ; Oxidoreductases/metabolism ; Reactive Oxygen Species/metabolism ; Uncoupling Protein 1 ; },
abstract = {The appearance of intracellular oxidative phosphorylation at the time of acquisition of mitochondria in Eukarya was very soon accompanied by the emergence of uncoupling protein, a carrier specialized in free fatty acid-mediated H(+) recycling that can modulate the tightness of coupling between mitochondrial respiration and ATP synthesis, thereby maintaining a balance between energy supply and demand in the cell and defending cells against damaging reactive oxygen species production when electron carriers of the respiratory chain become over-reduced. The simultaneous occurrence of redox free energy-dissipating oxidase, which has the same final effect, could be related to the functional interactions between both dissipative systems.},
}

Acanthamoeba/*metabolism
Animals
Candida/*metabolism
Carrier Proteins/*metabolism
Dictyostelium/*metabolism
Energy Metabolism/physiology
*Evolution, Molecular
Ion Channels
Membrane Proteins/*metabolism
Mitochondria/metabolism
Mitochondrial Proteins
Oxidoreductases/metabolism
Reactive Oxygen Species/metabolism
Uncoupling Protein 1

@article {pmid11803022,
year = {2002},
author = {Kita, K and Hirawake, H and Miyadera, H and Amino, H and Takeo, S},
title = {Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum.},
journal = {Biochimica et biophysica acta},
volume = {1553},
number = {1-2},
pages = {123-139},
doi = {10.1016/s0005-2728(01)00237-7},
pmid = {11803022},
issn = {0006-3002},
mesh = {Amino Acid Sequence ; Anaerobiosis ; Animals ; Ascaris suum/*enzymology ; Electron Transport Complex II ; Energy Metabolism ; Fumarates/metabolism ; Life Cycle Stages ; Mitochondria/metabolism ; Models, Chemical ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/*metabolism ; Oxidoreductases/chemistry/*metabolism ; *Oxidoreductases Acting on CH-CH Group Donors ; Phylogeny ; Plasmodium falciparum/*enzymology ; Sequence Alignment ; Succinate Dehydrogenase/chemistry/*metabolism ; Succinic Acid/metabolism ; },
abstract = {Parasites have developed a variety of physiological functions necessary for existence within the specialized environment of the host. Regarding energy metabolism, which is an essential factor for survival, parasites adapt to low oxygen tension in host mammals using metabolic systems that are very different from that of the host. The majority of parasites do not use the oxygen available within the host, but employ systems other than oxidative phosphorylation for ATP synthesis. In addition, all parasites have a life cycle. In many cases, the parasite employs aerobic metabolism during their free-living stage outside the host. In such systems, parasite mitochondria play diverse roles. In particular, marked changes in the morphology and components of the mitochondria during the life cycle are very interesting elements of biological processes such as developmental control and environmental adaptation. Recent research has shown that the mitochondrial complex II plays an important role in the anaerobic energy metabolism of parasites inhabiting hosts, by acting as quinol-fumarate reductase.},
}

Amino Acid Sequence
Anaerobiosis
Animals
Ascaris suum/*enzymology
Electron Transport Complex II
Energy Metabolism
Fumarates/metabolism
Life Cycle Stages
Mitochondria/metabolism
Models, Chemical
Molecular Sequence Data
Multienzyme Complexes/chemistry/*metabolism
Oxidoreductases/chemistry/*metabolism
*Oxidoreductases Acting on CH-CH Group Donors
Phylogeny
Plasmodium falciparum/*enzymology
Sequence Alignment
Succinate Dehydrogenase/chemistry/*metabolism
Succinic Acid/metabolism

@article {pmid11820431,
year = {2001},
author = {Pérez-Castiñeira, JR and Gómez-García, R and López-Marqués, RL and Losada, M and Serrano, A},
title = {Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remnants or metabolic cornerstones?.},
journal = {International microbiology : the official journal of the Spanish Society for Microbiology},
volume = {4},
number = {3},
pages = {135-142},
doi = {10.1007/s10123-001-0028-x},
pmid = {11820431},
issn = {1139-6709},
mesh = {Animals ; Biological Evolution ; Diphosphates/*metabolism ; Energy Metabolism ; Eukaryota/*enzymology/genetics/metabolism ; Intracellular Membranes/enzymology ; Mitochondria/enzymology ; Molecular Sequence Data ; Photosynthesis ; Phylogeny ; Plastids/enzymology ; Pyrophosphatases/chemistry/*physiology ; },
abstract = {An increasing body of biochemical and genetic evidence suggests that inorganic pyrophosphate (PPi) plays an important role in protist bioenergetics. In these organisms, two types of inorganic pyrophosphatases [EC 3.6.1.1, namely soluble PPases (sPPases) and proton-translocating PPases (H+-PPases)] that hydrolyse the PPi generated by cell anabolism, thereby replenishing the orthophosphate pool needed for phosphorylation reactions, are present in different cellular compartments. Photosynthetic and heterotrophic protists possess sPPases located in cellular organelles (plastids and mitochondria), where many anabolic and biosynthetic reactions take place, in addition to H+-PPases, which are integral membrane proteins of the vacuolysosomal membranes and use the chemical energy of PPi to generate an electrochemical proton gradient useful in cell bioenergetics. This last category of proton pumps was considered to be restricted to higher plants and some primitive photosynthetic bacteria, but it has been found recently in many protists (microalgae and protozoa) and bacteria, thus indicating that H+-PPases are much more widespread than previously thought. No cytosolic sPPase (in bacteria, fungi and animal cells) has been shown to occur in these lower eukaryotes. The widespread occurrence of these key enzymes of PPi metabolism among evolutionarily divergent protists strongly supports the ancestral character of the bioenergetics based on this simple energy-rich compound, which may play an important role in survival under different biotic and abiotic stress conditions.},
}

Animals
Biological Evolution
Diphosphates/*metabolism
Energy Metabolism
Eukaryota/*enzymology/genetics/metabolism
Intracellular Membranes/enzymology
Mitochondria/enzymology
Molecular Sequence Data
Photosynthesis
Phylogeny
Plastids/enzymology
Pyrophosphatases/chemistry/*physiology

@article {pmid11828469,
year = {2001},
author = {Ludwig, B and Bender, E and Arnold, S and Hüttemann, M and Lee, I and Kadenbach, B},
title = {Cytochrome C oxidase and the regulation of oxidative phosphorylation.},
journal = {Chembiochem : a European journal of chemical biology},
volume = {2},
number = {6},
pages = {392-403},
doi = {10.1002/1439-7633(20010601)2:6<392::AID-CBIC392>3.0.CO;2-N},
pmid = {11828469},
issn = {1439-4227},
mesh = {Adenosine Triphosphate/metabolism ; Animals ; Bacterial Proteins/chemistry/*metabolism ; Diiodothyronines/metabolism ; Electron Transport Complex IV/chemistry/classification/*metabolism ; Heart/physiology ; Humans ; Membrane Potentials/physiology ; Mitochondria/enzymology/*metabolism ; Models, Molecular ; *Oxidative Phosphorylation ; Oxygen/metabolism ; Phylogeny ; Protein Structure, Tertiary ; Protein Subunits ; Reactive Oxygen Species/metabolism ; },
abstract = {Life of higher organisms is essentially dependent on the efficient synthesis of ATP by oxidative phosphorylation in mitochondria. An important and as yet unsolved question of energy metabolism is how are the variable rates of ATP synthesis at maximal work load during exercise or mental work and at rest or during sleep regulated. This article reviews our present knowledge on the structure of bacterial and eukaryotic cytochrome c oxidases and correlates it with recent results on the regulatory functions of nuclear-coded subunits of the eukaryotic enzyme, which are absent from the bacterial enzyme. A new molecular hypothesis on the physiological regulation of oxidative phosphorylation is proposed, assuming a hormonally controlled dynamic equilibrium in vivo between two states of energy metabolism, a relaxed state with low ROS (reactive oxygen species) formation, and an excited state with elevated formation of ROS, which are known to accelerate aging and to cause degenerative diseases and cancer. The hypothesis is based on the allosteric ATP inhibition of cytochrome c oxidase at high intramitochondrial ATP/ADP ratios ("second mechanism of respiratory control"), which is switched on by cAMP-dependent phosphorylation and switched off by calcium-induced dephosphorylation of the enzyme.},
}

Adenosine Triphosphate/metabolism
Animals
Bacterial Proteins/chemistry/*metabolism
Diiodothyronines/metabolism
Electron Transport Complex IV/chemistry/classification/*metabolism
Heart/physiology
Humans
Membrane Potentials/physiology
Mitochondria/enzymology/*metabolism
Models, Molecular
*Oxidative Phosphorylation
Oxygen/metabolism
Phylogeny
Protein Structure, Tertiary
Protein Subunits
Reactive Oxygen Species/metabolism

@article {pmid12014002,
year = {2002},
author = {Ohta, S},
title = {[The origin of mitochondria].},
journal = {Nihon rinsho. Japanese journal of clinical medicine},
volume = {60 Suppl 4},
number = {},
pages = {799-804},
pmid = {12014002},
issn = {0047-1852},
mesh = {Amino Acyl-tRNA Synthetases/genetics ; Animals ; Biological Evolution ; Cell Nucleus/genetics ; DNA, Mitochondrial ; Energy Metabolism ; Eukaryotic Cells/cytology ; Humans ; *Mitochondria/genetics/physiology ; Oxygen ; },
}

Amino Acyl-tRNA Synthetases/genetics
Animals
Biological Evolution
Cell Nucleus/genetics
DNA, Mitochondrial
Energy Metabolism
Eukaryotic Cells/cytology
Humans
*Mitochondria/genetics/physiology
Oxygen

@article {pmid12039439,
year = {2002},
author = {Arking, R and Buck, S and Novoseltev, VN and Hwangbo, DS and Lane, M},
title = {Genomic plasticity, energy allocations, and the extended longevity phenotypes of Drosophila.},
journal = {Ageing research reviews},
volume = {1},
number = {2},
pages = {209-228},
doi = {10.1016/s1568-1637(01)00010-1},
pmid = {12039439},
issn = {1568-1637},
mesh = {Aging/*genetics ; Animals ; Drosophila ; Energy Metabolism/*genetics ; Genome ; Longevity/*genetics ; Phenotype ; },
abstract = {The antagonistic pleiotropy theory of the evolution of aging is shown to be too simple to fully apply to the situation in which Drosophila are selected directly for delayed female fecundity and indirectly for extended longevity. We re-evaluated our own previously reported selection experiments using previously unreported data, as well as new data from the literature. The facts that led to this re-evaluation were: (1) the recognition that there are at least three different extended longevity phenotypes; (2) the existence of metabolic and mitochondrial differences between normal- and long-lived organisms; and most importantly; (3) the observation that animals selected for extended longevity are both more fecund and longer-lived than their progenitor control animals. This latter observation appears to contradict the theory. A revised interpretation of the events underlying the selection process indicates that there is a two-step change in energy allocations leading to a complex phenotype. Initial selection first allows the up-regulation of the antioxidant defense system genes and a shift to the use of the pentose shunt. This is later followed by alterations in mitochondrial fatty acid composition and other changes necessary to reduce the leakage of H(2)O(2) from the mitochondria into the cytosol. The recaptured energy available from the latter step is diverted from somatic maintenance back into reproduction, resulting in animals that are both long-lived and fecund. Literature review suggests the involvement of mitochondrial and antioxidant changes are likely universal in the Type 1 extended longevity phenotype.},
}

Aging/*genetics
Animals
Drosophila
Energy Metabolism/*genetics
Genome
Longevity/*genetics
Phenotype

@article {pmid12122455,
year = {2002},
author = {Hulbert, AJ and Else, PL and Manolis, SC and Brand, MD},
title = {Proton leak in hepatocytes and liver mitochondria from archosaurs (crocodiles) and allometric relationships for ectotherms.},
journal = {Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology},
volume = {172},
number = {5},
pages = {387-397},
doi = {10.1007/s00360-002-0264-1},
pmid = {12122455},
issn = {0174-1578},
mesh = {Alligators and Crocodiles/*metabolism ; Animals ; Biological Evolution ; Body Constitution ; Body Temperature Regulation/*physiology ; Cell Respiration/physiology ; Energy Metabolism/physiology ; Hepatocytes/*metabolism ; Mitochondria, Liver/chemistry/*metabolism ; Phospholipids/analysis ; Protons ; },
abstract = {It has previously been shown that mitochondrial proton conductance decreases with increasing body mass in mammals and is lower in a 250-g lizard than the laboratory rat. To examine whether mitochondrial proton conductance is extremely low in very large reptiles, hepatocytes and mitochondria were prepared from saltwater crocodiles (Crocodylus porosus) and freshwater crocodiles (Crocodylus johnstoni). Respiration rates of hepatocytes and liver mitochondria were measured at 37 degrees C and compared with values obtained for rat or previously measured for other species. Respiration rates of hepatocytes from either species of crocodile were similar to those reported for lizards and approximately one fifth of the rates measured using cells from mammals (rat and sheep). Ten-to-thirty percent of crocodile hepatocyte respiration was used to drive mitochondrial proton leak, similar to the proportion in other species. Respiration rates of crocodile liver mitochondria were similar to those of mammalian species. Proton leak rate in isolated liver mitochondria was measured as a function of membrane potential. Contrary to our prediction, the mitochondrial proton conductance of liver mitochondria from crocodiles was greater than that of liver mitochondria from lizards and was similar to that of rats. The acyl composition of liver mitochondrial phospholipids from the crocodiles was more similar to that in mitochondria from rats than in mitochondria from lizards. The relatively high mitochondrial proton conductance was associated with a relatively small liver, which seems to be characteristic of crocodilians. Comparison of data from a number of diverse ectothermic species suggested that hepatocyte respiration rate may decrease with body mass, with an allometric exponent of about -0.2, similar to the exponent in mammalian hepatocytes. However, unlike mammals, liver mitochondrial proton conductance in ectotherms showed no allometric relationship with body size.},
}

Alligators and Crocodiles/*metabolism
Animals
Biological Evolution
Body Constitution
Body Temperature Regulation/*physiology
Cell Respiration/physiology
Energy Metabolism/physiology
Hepatocytes/*metabolism
Mitochondria, Liver/chemistry/*metabolism
Phospholipids/analysis
Protons

@article {pmid12138089,
year = {2002},
author = {Besteiro, S and Biran, M and Biteau, N and Coustou, V and Baltz, T and Canioni, P and Bringaud, F},
title = {Succinate secreted by Trypanosoma brucei is produced by a novel and unique glycosomal enzyme, NADH-dependent fumarate reductase.},
journal = {The Journal of biological chemistry},
volume = {277},
number = {41},
pages = {38001-38012},
doi = {10.1074/jbc.M201759200},
pmid = {12138089},
issn = {0021-9258},
mesh = {Animals ; Biomarkers ; Cell Line ; Citric Acid Cycle ; Crithidia fasciculata/metabolism ; Digitonin/pharmacology ; Glucose/metabolism ; Leishmania/metabolism ; Magnetic Resonance Spectroscopy ; Microbodies/*enzymology ; Mitochondria/metabolism ; Molecular Sequence Data ; NADH Dehydrogenase/metabolism ; Oxidoreductases/classification/genetics/*metabolism ; *Oxidoreductases Acting on CH-CH Group Donors ; Phenotype ; Phylogeny ; Protozoan Proteins/classification/genetics/*metabolism ; Rats ; Succinic Acid/*metabolism ; Trypanosoma brucei brucei/cytology/drug effects/genetics/*metabolism ; },
abstract = {In all trypanosomatids, including Trypanosoma brucei, glycolysis takes place in peroxisome-like organelles called glycosomes. These are closed compartments wherein the energy and redox (NAD(+)/NADH) balances need to be maintained. We have characterized a T. brucei gene called FRDg encoding a protein 35% identical to Saccharomyces cerevisiae fumarate reductases. Microsequencing of FRDg purified from glycosome preparations, immunofluorescence, and Western blot analyses clearly identified this enzyme as a glycosomal protein that is only expressed in the procyclic form of T. brucei but is present in all the other trypanosomatids studied, i.e. Trypanosoma congolense, Crithidia fasciculata and Leishmania amazonensis. The specific inactivation of FRDg gene expression by RNA interference showed that FRDg is responsible for the NADH-dependent fumarate reductase activity detected in glycosomal fractions and that at least 60% of the succinate secreted by the T. brucei procyclic form (in the presence of d-glucose as the sole carbon source) is produced in the glycosome by FRDg. We conclude that FRDg plays a key role in the energy metabolism by participating in the maintenance of the glycosomal NAD(+)/NADH balance. We have also detected a significant pyruvate kinase activity in the cytosol of the T. brucei procyclic cells that was not observed previously. Consequently, we propose a revised model of glucose metabolism in procyclic trypanosomes that may also be valid for all other trypanosomatids except the T. brucei bloodstream form. Interestingly, H. Gest has hypothesized previously (Gest, H. (1980) FEMS Microbiol. Lett. 7, 73-77) that a soluble NADH-dependent fumarate reductase has been present in primitive organisms and evolved into the present day fumarate reductases, which are quinol-dependent. FRDg may have the characteristics of such an ancestral enzyme and is the only NADH-dependent fumarate reductase characterized to date.},
}

Animals
Biomarkers
Cell Line
Citric Acid Cycle
Crithidia fasciculata/metabolism
Digitonin/pharmacology
Glucose/metabolism
Leishmania/metabolism
Magnetic Resonance Spectroscopy
Microbodies/*enzymology
Mitochondria/metabolism
Molecular Sequence Data
NADH Dehydrogenase/metabolism
Oxidoreductases/classification/genetics/*metabolism
*Oxidoreductases Acting on CH-CH Group Donors
Phenotype
Phylogeny
Protozoan Proteins/classification/genetics/*metabolism
Rats
Succinic Acid/*metabolism
Trypanosoma brucei brucei/cytology/drug effects/genetics/*metabolism

@article {pmid12180017,
year = {2002},
author = {Kuznetsov, AP and Lebkova, NP},
title = {[On bacterial origin of mitochondria in eukaryotes in the light of current ideas of evolution of the organic world].},
journal = {Izvestiia Akademii nauk. Seriia biologicheskaia},
volume = {},
number = {4},
pages = {501-507},
pmid = {12180017},
issn = {1026-3470},
mesh = {Aerobiosis ; Animals ; *Bacterial Physiological Phenomena ; *Biological Evolution ; Eukaryotic Cells/*physiology ; Mitochondria/*physiology ; Mollusca/physiology ; Symbiosis ; },
abstract = {The hypothesis of bacterial origin of mitochondria, which existed until the end of the 20th century, has been confirmed on the basis of the current concepts of organic world evolution in the open sea hydrosphere and original data on the entry of bacteria (prokaryotes0 in the cells of eukaryotes and their transformation into the mitochondrial mechanism of aerobic energy metabolism. This hypothesis can now be considered as a factually substantiated theory. The process of endocytosis of bacteria in the tissues of eukaryotes, which began at the onset of transition of the anaerobic state of open sea hydrosphere and land atmosphere (Early Proterozoic), is considered as the beginning of symbiotic mode of life of organisms of the Proterozoic and Postproterozoic organic world.},
}

Aerobiosis
Animals
*Bacterial Physiological Phenomena
*Biological Evolution
Eukaryotic Cells/*physiology
Mitochondria/*physiology
Mollusca/physiology
Symbiosis

@article {pmid12238891,
year = {2002},
author = {Kita, K and Takamiya, S},
title = {Electron-transfer complexes in Ascaris mitochondria.},
journal = {Advances in parasitology},
volume = {51},
number = {},
pages = {95-131},
doi = {10.1016/s0065-308x(02)51004-6},
pmid = {12238891},
issn = {0065-308X},
mesh = {Anaerobiosis/physiology ; Animals ; Ascaris suum/growth & development/*metabolism/physiology ; DNA, Mitochondrial/genetics/metabolism ; Electron Transport/genetics/physiology ; Evolution, Molecular ; Fatty Acid Desaturases/metabolism ; Life Cycle Stages/physiology ; Mitochondria/*metabolism ; Models, Biological ; Models, Molecular ; Oxidoreductases/metabolism ; *Oxidoreductases Acting on CH-CH Group Donors ; Phosphoenolpyruvate Carboxykinase (ATP)/metabolism ; Succinic Acid/metabolism ; Ubiquinone/*analogs & derivatives/physiology ; },
abstract = {Parasites have developed a variety of physiological functions necessary for their survival within the specialized environment of the host. Using metabolic systems that are very different from those of the host, they can adapt to low oxygen tension present within the host animals. Most parasites do not use the oxygen available within the host to generate ATP, but rather employ anaerobic metabolic pathways. In addition, all parasites have a life cycle. In many cases, the parasite employs aerobic metabolism during its free-living stage outside the host. In such systems, parasite mitochondria play diverse roles. In particular, marked changes in the morphology and components of the mitochondria during the life cycle are very interesting elements of biological processes such as developmental control and environmental adaptation. Recent research on the respiratory chain of the parasitic helminth Ascaris suum has shown that the mitochondrial NADH-fumarate reductase system plays an important role in the anaerobic energy metabolism of adult parasites inhabiting hosts, as well as describing unique features of the developmental changes that occur during its life cycle.},
}

Anaerobiosis/physiology
Animals
Ascaris suum/growth & development/*metabolism/physiology
DNA, Mitochondrial/genetics/metabolism
Electron Transport/genetics/physiology
Evolution, Molecular
Fatty Acid Desaturases/metabolism
Life Cycle Stages/physiology
Mitochondria/*metabolism
Models, Biological
Models, Molecular
Oxidoreductases/metabolism
*Oxidoreductases Acting on CH-CH Group Donors
Phosphoenolpyruvate Carboxykinase (ATP)/metabolism
Succinic Acid/metabolism
Ubiquinone/*analogs & derivatives/physiology

@article {pmid12392880,
year = {2002},
author = {Opie, LH and Sack, MN},
title = {Metabolic plasticity and the promotion of cardiac protection in ischemia and ischemic preconditioning.},
journal = {Journal of molecular and cellular cardiology},
volume = {34},
number = {9},
pages = {1077-1089},
doi = {10.1006/jmcc.2002.2066},
pmid = {12392880},
issn = {0022-2828},
mesh = {Adenosine Triphosphate/metabolism ; Animals ; Energy Metabolism ; Glycolysis ; Humans ; *Ischemic Preconditioning, Myocardial ; Mitochondria, Heart/metabolism ; Models, Cardiovascular ; Myocardial Ischemia/*metabolism ; Myocardium/metabolism ; },
abstract = {The concept of metabolic protection of the ischemic myocardium is in constant evolution and has recently been supported by clinical studies. Historically, enhanced glucose metabolism and glycolysis were proposed as anti-ischemic cardioprotection. This hypothesis is supported by the sub-cellular linkage between key glycolytic enzymes and the activity of two survival-promoting membrane-bound pumps, namely the sodium-potassium ATPase, and the calcium uptake pump of the sarcoplasmic reticulum. Moreover, improved resistance against ischemia follows the administration of glucose-insulin-potassium in a variety of animal models and in patients following acute myocardial infarction. The metabolic plasticity paradigm has now been expanded to include (1) the benefit of improved coupling of glycolysis to glucose oxidation, which explains the action of anti-ischemic fatty acid inhibitors such as trimetazidine and ranolazine; (2) the role of malonyl CoA in the glucose-fatty acid interaction; and (3) the anti-apoptotic role of insulin. Furthermore, we argue for a protective role of increased glucose uptake in the preconditioning paradigm. Additionally, we postulate an adaptive role of mitochondrial respiration in the promotion of cardioprotection in the context of ischemic preconditioning. The mechanisms driving these mitochondrial perturbations are still unknown, but are hypothesized to involve an initial modest uncoupling of respiration from the production of mitochondrial ATP. These perturbations are in turn thought to prime the mitochondria to augment mitochondrial respiration during a subsequent ischemic insult to the heart. In this review we discuss studies that demonstrate how metabolic plasticity can promote cardioprotection against ischemia and reperfusion injury and highlight areas that require further characterization.},
}

Adenosine Triphosphate/metabolism
Animals
Energy Metabolism
Glycolysis
Humans
*Ischemic Preconditioning, Myocardial
Mitochondria, Heart/metabolism
Models, Cardiovascular
Myocardial Ischemia/*metabolism
Myocardium/metabolism

@article {pmid12417132,
year = {2002},
author = {Tielens, AG and Rotte, C and van Hellemond, JJ and Martin, W},
title = {Mitochondria as we don't know them.},
journal = {Trends in biochemical sciences},
volume = {27},
number = {11},
pages = {564-572},
doi = {10.1016/s0968-0004(02)02193-x},
pmid = {12417132},
issn = {0968-0004},
mesh = {Adenosine Triphosphate/*biosynthesis ; Animals ; Electron Transport/physiology ; Energy Metabolism ; Eukaryotic Cells/physiology ; Mitochondria/classification/*metabolism ; Oxygen/metabolism ; Phylogeny ; Proton Pumps/metabolism ; Succinate Dehydrogenase/genetics/metabolism ; },
abstract = {Biochemistry textbooks depict mitochondria as oxygen-dependent organelles, but many mitochondria can produce ATP without using any oxygen. In fact, several other types of mitochondria exist and they occur in highly diverse groups of eukaryotes - protists as well as metazoans - and possess an often overlooked diversity of pathways to deal with the electrons resulting from carbohydrate oxidation. These anaerobically functioning mitochondria produce ATP with the help of proton-pumping electron transport, but they do not need oxygen to do so. Recent advances in understanding of mitochondrial biochemistry provide many surprises and furthermore, give insights into the evolutionary history of ATP-producing organelles.},
}

Adenosine Triphosphate/*biosynthesis
Animals
Electron Transport/physiology
Energy Metabolism
Eukaryotic Cells/physiology
Mitochondria/classification/*metabolism
Oxygen/metabolism
Phylogeny
Proton Pumps/metabolism
Succinate Dehydrogenase/genetics/metabolism

@article {pmid12524465,
year = {2003},
author = {Moyes, CD and Hood, DA},
title = {Origins and consequences of mitochondrial variation in vertebrate muscle.},
journal = {Annual review of physiology},
volume = {65},
number = {},
pages = {177-201},
doi = {10.1146/annurev.physiol.65.092101.142705},
pmid = {12524465},
issn = {0066-4278},
mesh = {Animals ; Biological Evolution ; Energy Metabolism/*physiology ; Genetic Variation ; Humans ; Mitochondria/genetics/*metabolism ; Muscle, Skeletal/*metabolism ; Vertebrates ; },
abstract = {This review addresses the mechanisms by which mitochondrial structure and function are regulated, with a focus on vertebrate muscle. We consider the adaptive remodeling that arises during physiological transitions such as differentiation, development, and contractile activity. Parallels are drawn between such phenotypic changes and the pattern of change arising over evolutionary time, as suggested by interspecies comparisons. We address the physiological and evolutionary relationships between ATP production, thermogenesis, and superoxide generation in the context of mitochondrial function. Our discussion of mitochondrial structure focuses on the regulation of membrane composition and maintenance of the three-dimensional reticulum. Current studies of mitochondrial biogenesis strive to integrate muscle functional parameters with signal transduction and molecular genetics, providing insight into the origins of variation arising between physiological states, fiber types, and species.},
}

Animals
Biological Evolution
Energy Metabolism/*physiology
Genetic Variation
Humans
Mitochondria/genetics/*metabolism
Muscle, Skeletal/*metabolism
Vertebrates

@article {pmid12574861,
year = {2003},
author = {Seligmann, H},
title = {Cost-minimization of amino acid usage.},
journal = {Journal of molecular evolution},
volume = {56},
number = {2},
pages = {151-161},
doi = {10.1007/s00239-002-2388-z},
pmid = {12574861},
issn = {0022-2844},
mesh = {Amino Acids/chemistry/*metabolism ; Animals ; Archaea/genetics/metabolism ; Bacteria/genetics/metabolism ; Base Composition ; Codon ; Energy Metabolism/*physiology ; Eukaryotic Cells/physiology ; Genome ; *Models, Biological ; Molecular Weight ; *Protein Biosynthesis ; Proteins/chemistry ; },
abstract = {The negative correlation between the frequencies of usage of amino acids and their biosynthetic cost suggests that organisms minimize costs of protein biosynthesis. Empirical results support that: (1) free-living organisms (Archaea, Bacteria, and Eucaryota) minimize the usage of heavy amino acids more than intracellular organisms (viruses, chloroplasts, and mitochondria), a result confirmed by comparing intracellular Bacteria with other Bacteria; (2) avoidance of amino acids with low impact on protein structure (Chou-Fasman indices) is greater than for those with equal molecular weight but greater structural impact: constraints on protein function limit cost-minimization; (3) amino acid weight minimization (WM) for a protein correlates positively with the protein's expression level and with its size; (4) preliminary results suggest that for different proteins, the evolutionary rate of amino acid replacements correlates negatively with WM in these proteins; (5) results suggest that WM decreases with genome-size; and (6) developmental rates correlate positively with WM (within primates and rodents), even after confounding factors were accounted for. Effects of biosynthetic cost-minimization at whole-organism levels vary with metabolic and ecological strategies. Biosynthetic cost-minimization is an adaptive hypothesis that yields a semi-mechanistic explanation for small differences in allele fitness.},
}

Amino Acids/chemistry/*metabolism
Animals
Archaea/genetics/metabolism
Bacteria/genetics/metabolism
Base Composition
Codon
Energy Metabolism/*physiology
Eukaryotic Cells/physiology
Genome
*Models, Biological
Molecular Weight
*Protein Biosynthesis
Proteins/chemistry

@article {pmid12678440,
year = {2002},
author = {Almeida, AM and Navet, R and Jarmuszkiewicz, W and Vercesi, AE and Sluse-Goffart, CM and Sluse, FE},
title = {The energy-conserving and energy-dissipating processes in mitochondria isolated from wild type and nonripening tomato fruits during development on the plant.},
journal = {Journal of bioenergetics and biomembranes},
volume = {34},
number = {6},
pages = {487-498},
pmid = {12678440},
issn = {0145-479X},
mesh = {Adenosine Triphosphate/biosynthesis ; Carrier Proteins/metabolism ; Energy Metabolism ; Fatty Acids, Nonesterified/metabolism ; Ion Channels ; Solanum lycopersicum/genetics/growth & development/*metabolism ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins ; Mutation ; Oxidoreductases/metabolism ; Oxygen Consumption ; Plant Proteins/metabolism ; Uncoupling Protein 1 ; Alternative Oxidase ; },
abstract = {Bioenergetics of tomato (Lycopersicon esculentum) development on the plant was followed from the early growing stage to senescence in wild type (climacteric) and nonripening mutant (nor, non-climacteric) fruits. Fruit development was expressed in terms of evolution of chlorophyll a content allowing the assessment of a continuous time-course in both cultivars. Measured parameters: the cytochrome pathway-dependent respiration, i.e., the ATP synthesis-sustained respiration (energy-conserving), the uncoupling protein (UCP) activity-sustained respiration (energy-dissipating), the alternative oxidase(AOX)-mediated respiration (energy-dissipating), as well as the protein expression of UCP and AOX, and free fatty acid content exhibited different evolution patterns in the wild type and nor mutant that can be attributed to their climacteric/nonclimacteric properties, respectively. In the wild type, the climacteric respiratory burst observed in vitro depended totally on an increse in the cytochrome pathway activity sustained by ATP synthesis, while the second respiratory rise during the ripening stage was linked to a strong increase in AOX activity accompanied by an overexpression of AOX protein. In wild type mitochondria, the 10-microM linoleic acid-stimulated UCP-activity-dependent respiration remained constant during the whole fruit development except in senescence where general respiratory decay was observed.},
}

Adenosine Triphosphate/biosynthesis
Carrier Proteins/metabolism
Energy Metabolism
Fatty Acids, Nonesterified/metabolism
Ion Channels
Solanum lycopersicum/genetics/growth & development/*metabolism
Membrane Proteins/metabolism
Mitochondria/metabolism
Mitochondrial Proteins
Mutation
Oxidoreductases/metabolism
Oxygen Consumption
Plant Proteins/metabolism
Uncoupling Protein 1
Alternative Oxidase

@article {pmid12694174,
year = {2003},
author = {Emelyanov, VV},
title = {Mitochondrial connection to the origin of the eukaryotic cell.},
journal = {European journal of biochemistry},
volume = {270},
number = {8},
pages = {1599-1618},
doi = {10.1046/j.1432-1033.2003.03499.x},
pmid = {12694174},
issn = {0014-2956},
mesh = {Amino Acid Sequence ; Animals ; Conserved Sequence ; Energy Metabolism ; Eukaryotic Cells/metabolism ; Glycolysis/genetics ; Humans ; Mitochondria/genetics/*metabolism ; Molecular Sequence Data ; Phylogeny ; Sequence Alignment ; Valine-tRNA Ligase/chemistry/genetics ; },
abstract = {Phylogenetic evidence is presented that primitively amitochondriate eukaryotes containing the nucleus, cytoskeleton, and endomembrane system may have never existed. Instead, the primary host for the mitochondrial progenitor may have been a chimeric prokaryote, created by fusion between an archaebacterium and a eubacterium, in which eubacterial energy metabolism (glycolysis and fermentation) was retained. A Rickettsia-like intracellular symbiont, suggested to be the last common ancestor of the family Rickettsiaceae and mitochondria, may have penetrated such a host (pro-eukaryote), surrounded by a single membrane, due to tightly membrane-associated phospholipase activity, as do present-day rickettsiae. The relatively rapid evolutionary conversion of the invader into an organelle may have occurred in a safe milieu via numerous, often dramatic, changes involving both partners, which resulted in successful coupling of the host glycolysis and the symbiont respiration. Establishment of a potent energy-generating organelle made it possible, through rapid dramatic changes, to develop genuine eukaryotic elements. Such sequential, or converging, global events could fill the gap between prokaryotes and eukaryotes known as major evolutionary discontinuity.},
}

Amino Acid Sequence
Animals
Conserved Sequence
Energy Metabolism
Eukaryotic Cells/metabolism
Glycolysis/genetics
Humans
Mitochondria/genetics/*metabolism
Molecular Sequence Data
Phylogeny
Sequence Alignment
Valine-tRNA Ligase/chemistry/genetics

@article {pmid12765765,
year = {2003},
author = {Kadenbach, B},
title = {Intrinsic and extrinsic uncoupling of oxidative phosphorylation.},
journal = {Biochimica et biophysica acta},
volume = {1604},
number = {2},
pages = {77-94},
doi = {10.1016/s0005-2728(03)00027-6},
pmid = {12765765},
issn = {0006-3002},
mesh = {Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Biological Evolution ; Electron Transport Complex IV/metabolism ; Energy Metabolism ; Fatty Acids/metabolism ; Intracellular Membranes/metabolism ; Membrane Potentials ; Membrane Proteins/metabolism ; Mitochondria/drug effects/metabolism ; Models, Biological ; *Oxidative Phosphorylation/drug effects ; Proton Pumps/drug effects/metabolism ; Proton-Translocating ATPases/metabolism ; Protons ; Reactive Oxygen Species/metabolism ; Thyroid Hormones/metabolism ; Uncoupling Agents/*metabolism/pharmacology ; },
abstract = {This article reviews parameters of extrinsic uncoupling of oxidative phosphorylation (OxPhos) in mitochondria, based on induction of a proton leak across the inner membrane. The effects of classical uncouplers, fatty acids, uncoupling proteins (UCP1-UCP5) and thyroid hormones on the efficiency of OxPhos are described. Furthermore, the present knowledge on intrinsic uncoupling of cytochrome c oxidase (decrease of H(+)/e(-) stoichiometry=slip) is reviewed. Among the three proton pumps of the respiratory chain of mitochondria and bacteria, only cytochrome c oxidase is known to exhibit a slip of proton pumping. Intrinsic uncoupling was shown after chemical modification, by site-directed mutagenesis of the bacterial enzyme, at high membrane potential DeltaPsi, and in a tissue-specific manner to increase thermogenesis in heart and skeletal muscle by high ATP/ADP ratios, and in non-skeletal muscle tissues by palmitate. In addition, two mechanisms of respiratory control are described. The first occurs through the membrane potential DeltaPsi and maintains high DeltaPsi values (150-200 mV). The second occurs only in mitochondria, is suggested to keep DeltaPsi at low levels (100-150 mV) through the potential dependence of the ATP synthase and the allosteric ATP inhibition of cytochrome c oxidase at high ATP/ADP ratios, and is reversibly switched on by cAMP-dependent phosphorylation. Finally, the regulation of DeltaPsi and the production of reactive oxygen species (ROS) in mitochondria at high DeltaPsi values (150-200 mV) are discussed.},
}

Adenosine Diphosphate/metabolism
Adenosine Triphosphate/metabolism
Animals
Biological Evolution
Electron Transport Complex IV/metabolism
Energy Metabolism
Fatty Acids/metabolism
Intracellular Membranes/metabolism
Membrane Potentials
Membrane Proteins/metabolism
Mitochondria/drug effects/metabolism
Models, Biological
*Oxidative Phosphorylation/drug effects
Proton Pumps/drug effects/metabolism
Proton-Translocating ATPases/metabolism
Protons
Reactive Oxygen Species/metabolism
Thyroid Hormones/metabolism
Uncoupling Agents/*metabolism/pharmacology

@article {pmid12972297,
year = {2003},
author = {Godbole, A and Varghese, J and Sarin, A and Mathew, MK},
title = {VDAC is a conserved element of death pathways in plant and animal systems.},
journal = {Biochimica et biophysica acta},
volume = {1642},
number = {1-2},
pages = {87-96},
doi = {10.1016/s0167-4889(03)00102-2},
pmid = {12972297},
issn = {0006-3002},
mesh = {Animals ; Apoptosis/*physiology ; Cotyledon/drug effects/metabolism ; Cucumis sativus/metabolism ; Energy Metabolism/physiology ; Enzyme Inhibitors/pharmacology ; Eukaryotic Cells/*metabolism ; Evolution, Molecular ; Gene Expression Regulation, Plant/drug effects/physiology ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Jurkat Cells ; Mitochondria/*metabolism ; Oryza/genetics ; Plant Proteins/genetics/metabolism ; Plants/genetics/*metabolism ; Porins/genetics/*metabolism ; Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors/metabolism ; Voltage-Dependent Anion Channels ; },
abstract = {Programmed cell death (PCD) is very much a part of plant life, although the underlying mechanisms are not so well understood as in animals. In animal cells, the voltage-dependent anion channel (VDAC), a major mitochondrial outer membrane transporter, plays an important role in apoptosis by participating in the release of intermembrane space proteins. To characterize plant PCD pathways by investigating the function of putative components in a mammalian apoptotic context, we have overexpressed a rice VDAC (osVDAC4) in the Jurkat T-cell line. Overexpression of osVDAC4 induces apoptosis, which can be blocked by Bcl-2 and the VDAC inhibitor DIDS. Modifying endogenous VDAC function by DIDS and hexokinase II (HxKII) in Jurkat cells inhibits mitochondria-mediated apoptotic pathways. Finally, we show that DIDS also abrogates heat-induced PCD in cucumber cotyledons. Our data suggest that VDAC is a conserved mitochondrial element of the death machinery in both plant and animal cells.},
}

Animals
Apoptosis/*physiology
Cotyledon/drug effects/metabolism
Cucumis sativus/metabolism
Energy Metabolism/physiology
Enzyme Inhibitors/pharmacology
Eukaryotic Cells/*metabolism
Evolution, Molecular
Gene Expression Regulation, Plant/drug effects/physiology
HeLa Cells
Humans
Intracellular Membranes/metabolism
Jurkat Cells
Mitochondria/*metabolism
Oryza/genetics
Plant Proteins/genetics/metabolism
Plants/genetics/*metabolism
Porins/genetics/*metabolism
Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors/metabolism
Voltage-Dependent Anion Channels

@article {pmid14531549,
year = {2003},
author = {Müller, W and Mennel, HD and Bewermeyer, K and Bewermeyer, H},
title = {Is there a final common pathway in mitochondrial encephalomyopathies? Considerations based on an autopsy case of Kearns-Sayre syndrome.},
journal = {Clinical neuropathology},
volume = {22},
number = {5},
pages = {240-245},
pmid = {14531549},
issn = {0722-5091},
mesh = {Adult ; Atrophy ; Brain/pathology/physiopathology ; Cerebellum/pathology/physiopathology ; Cerebral Infarction/pathology/physiopathology ; Disease Progression ; Dominance, Cerebral/physiology ; Energy Metabolism/*physiology ; Female ; Gliosis/pathology/physiopathology ; Humans ; Kearns-Sayre Syndrome/*pathology/physiopathology ; Mitochondria/pathology/physiology ; Mitochondrial Encephalomyopathies/*pathology/physiopathology ; Neurologic Examination ; Tomography, X-Ray Computed ; },
abstract = {A case of Kearns-Sayre syndrome (KSS) diagnosed 18 years prior to death due to stroke and heart failure with postnatal onset was followed over 15 years and confirmed by postmortem examination. Within the brain, an old cystic infarction of the left hemisphere was found. Other features included white matter gliosis and cerebellar atrophy. Equal or similar features were observed in other conditions thought to be due to failure of mitochondrial metabolism, therefore, a common evolution of neuropathological changes must be discussed.},
}

Adult
Atrophy
Brain/pathology/physiopathology
Cerebellum/pathology/physiopathology
Cerebral Infarction/pathology/physiopathology
Disease Progression
Dominance, Cerebral/physiology
Energy Metabolism/*physiology
Female
Gliosis/pathology/physiopathology
Humans
Kearns-Sayre Syndrome/*pathology/physiopathology
Mitochondria/pathology/physiology
Mitochondrial Encephalomyopathies/*pathology/physiopathology
Neurologic Examination
Tomography, X-Ray Computed

@article {pmid14613499,
year = {2003},
author = {Hannaert, V and Bringaud, F and Opperdoes, FR and Michels, PA},
title = {Evolution of energy metabolism and its compartmentation in Kinetoplastida.},
journal = {Kinetoplastid biology and disease},
volume = {2},
number = {1},
pages = {11},
pmid = {14613499},
issn = {1475-9292},
abstract = {Kinetoplastida are protozoan organisms that probably diverged early in evolution from other eukaryotes. They are characterized by a number of unique features with respect to their energy and carbohydrate metabolism. These organisms possess peculiar peroxisomes, called glycosomes, which play a central role in this metabolism; the organelles harbour enzymes of several catabolic and anabolic routes, including major parts of the glycolytic and pentosephosphate pathways. The kinetoplastid mitochondrion is also unusual with regard to both its structural and functional properties.In this review, we describe the unique compartmentation of metabolism in Kinetoplastida and the metabolic properties resulting from this compartmentation. We discuss the evidence for our recently proposed hypothesis that a common ancestor of Kinetoplastida and Euglenida acquired a photosynthetic alga as an endosymbiont, contrary to the earlier notion that this event occurred at a later stage of evolution, in the Euglenida lineage alone. The endosymbiont was subsequently lost from the kinetoplastid lineage but, during that process, some of its pathways of energy and carbohydrate metabolism were sequestered in the kinetoplastid peroxisomes, which consequently became glycosomes. The evolution of the kinetoplastid glycosomes and the possible selective advantages of these organelles for Kinetoplastida are discussed. We propose that the possession of glycosomes provided metabolic flexibility that has been important for the organisms to adapt easily to changing environmental conditions. It is likely that metabolic flexibility has been an important selective advantage for many kinetoplastid species during their evolution into the highly successful parasites today found in many divergent taxonomic groups.Also addressed is the evolution of the kinetoplastid mitochondrion, from a supposedly pluripotent organelle, attributed to a single endosymbiotic event that resulted in all mitochondria and hydrogenosomes of extant eukaryotes. Furthermore, indications are presented that Kinetoplastida may have acquired other enzymes of energy and carbohydrate metabolism by various lateral gene transfer events different from those that involved the algal- and alpha-proteobacterial-like endosymbionts responsible for the respective formation of the glycosomes and mitochondria.},
}

@article {pmid14630958,
year = {2003},
author = {Cardol, P and Gloire, G and Havaux, M and Remacle, C and Matagne, R and Franck, F},
title = {Photosynthesis and state transitions in mitochondrial mutants of Chlamydomonas reinhardtii affected in respiration.},
journal = {Plant physiology},
volume = {133},
number = {4},
pages = {2010-2020},
pmid = {14630958},
issn = {0032-0889},
mesh = {Animals ; Chlamydomonas reinhardtii/*genetics/metabolism ; Darkness ; Energy Metabolism ; Kinetics ; Light ; Mitochondria/*genetics ; Oxygen Consumption/*genetics ; Photosynthesis/*physiology ; },
abstract = {Photosynthetic activities were analyzed in Chlamydomonas reinhardtii mitochondrial mutants affected in different complexes (I, III, IV, I + III, and I + IV) of the respiratory chain. Oxygen evolution curves showed a positive relationship between the apparent yield of photosynthetic linear electron transport and the number of active proton-pumping sites in mitochondria. Although no significant alterations of the quantitative relationships between major photosynthetic complexes were found in the mutants, 77 K fluorescence spectra showed a preferential excitation of photosystem I (PSI) compared with wild type, which was indicative of a shift toward state 2. This effect was correlated with high levels of phosphorylation of light-harvesting complex II polypeptides, indicating the preferential association of light-harvesting complex II with PSI. The transition to state 1 occurred in untreated wild-type cells exposed to PSI light or in 3-(3,4-dichlorophenyl)-1,1-dimethylureatreated cells exposed to white light. In mutants of the cytochrome pathway and in double mutants, this transition was only observed in white light in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea. This suggests higher rates of nonphotochemical plastoquinone reduction through the chlororespiratory pathway, which was confirmed by measurements of the complementary area above the fluorescence induction curve in dark-adapted cells. Photo-acoustic measurements of energy storage by PSI showed a stimulation of PSI-driven cyclic electron flow in the most affected mutants. The present results demonstrate that in C. reinhardtii mutants, permanent defects in the mitochondrial electron transport chain stabilize state 2, which favors cyclic over linear electron transport in the chloroplast.},
}

Animals
Chlamydomonas reinhardtii/*genetics/metabolism
Darkness
Energy Metabolism
Kinetics
Light
Mitochondria/*genetics
Oxygen Consumption/*genetics
Photosynthesis/*physiology

@article {pmid14662295,
year = {2003},
author = {Johnston, IA},
title = {Muscle metabolism and growth in Antarctic fishes (suborder Notothenioidei): evolution in a cold environment.},
journal = {Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
volume = {136},
number = {4},
pages = {701-713},
doi = {10.1016/s1096-4959(03)00258-6},
pmid = {14662295},
issn = {1096-4959},
mesh = {Animals ; Antarctic Regions ; *Biological Evolution ; *Cold Temperature ; Fishes/*metabolism ; Muscle, Skeletal/*growth & development/*metabolism ; Oxygen Consumption ; Phylogeny ; },
abstract = {The radiation of notothenioid fishes (order Perciformes) in the Southern Ocean provides a model system for investigating evolution and adaptation to a low temperature environment. The Notothenioid fishes comprising eight families, 43 genera and 122 species dominate the fish fauna in Antarctica. The diversification of the clade probably began 15-20 million years ago after the formation of the Antarctic Polar Front. The radiation was, therefore, associated with climatic cooling down to the present day temperature of -1.86 degrees C. Origins and Evolution of the Antarctic Biota Geological Society Special Publication No. 47, Geological Society of London. pp. 253-268). The success of the group has been closely linked with the evolution of glycopeptide and peptide antifreezes, which are amongst the most abundant proteins in blood and interstitial fluid. The radiation of the clade has been associated with disaptation (evolutionary loss of function) and recovery. For example, it is thought that the icefishes (Channichyidae) lost haemoglobin through a single mutational event leading to the deletion of the entire beta-globin gene and the 5' end of the linked alpha-globin gene, resulting in compensatory adaptations of the cardiovascular system. Phylogenetically based statistical methods also indicate a progressive and dramatic reduction in the number of skeletal muscle fibres (FN(max)) at the end of the recruitment phase of growth in basal compared to derived families. The reduction in FN(max) is associated with a compensatory increase in the maximum fibre diameter, which can reach 100 microm in slow and 600 microm in fast muscle fibres. At -1 to 0 degrees C, the oxygen consumption of isolated mitochondria per mg mitochondrial protein shows no evidence of up-regulation relative to mitochondria from temperate and tropical Perciform fishes. The mitochondria content of slow muscle fibres in Antarctic notothenioids is towards the upper end of the range reported for teleosts with similar lifestyles, reaching 50% in Channichthyids. High mitochondrial densities facilitate ATP production and oxygen diffusion through the membrane lipid compartment of the fibre. Modelling studies suggest that adequate oxygen flux in the large diameter muscle fibres of notothenioids is possible because of the reduced metabolic demand and enhanced solubility of oxygen associated with low temperature. At the whole animal level size-corrected resting metabolic rate fits on the same temperature relationship as for Perciformes from warmer climates. It seems likely that the additional energetic costs associated with antifreeze synthesis and high mitochondrial densities are compensated for by reductions in other energy requiring processes: a hypothesis that could be tested with detailed energy budget studies. One plausible candidate is a reduction in membrane leak pathways linked to the loss of muscle fibres, which would serve to minimise the cost of maintaining ionic gradients.},
}

Animals
Antarctic Regions
*Biological Evolution
*Cold Temperature
Fishes/*metabolism
Muscle, Skeletal/*growth & development/*metabolism
Oxygen Consumption
Phylogeny