oligomycins and malic-acid

The sites and rates of mitochondrial production of superoxide and H2O2 in vivo are not yet defined. At least 10 different mitochondrial sites can generate these species. Each site has a different maximum capacity (e.g. the outer quinol site in complex III (site IIIQo) has a very high capacity in rat skeletal muscle mitochondria, whereas the flavin site in complex I (site IF) has a very low capacity). The maximum capacities can greatly exceed the actual rates observed in the absence of electron transport chain inhibitors, so maximum capacities are a poor guide to actual rates. Here, we use new approaches to measure the rates at which different mitochondrial sites produce superoxide/H2O2 using isolated muscle mitochondria incubated in media mimicking the cytoplasmic substrate and effector mix of skeletal muscle during rest and exercise. We find that four or five sites dominate during rest in this ex vivo system. Remarkably, the quinol site in complex I (site IQ) and the flavin site in complex II (site IIF) each account for about a quarter of the total measured rate of H2O2 production. Site IF, site IIIQo, and perhaps site EF in the β-oxidation pathway account for most of the remainder. Under conditions mimicking mild and intense aerobic exercise, total production is much less, and the low capacity site IF dominates. These results give novel insights into which mitochondrial sites may produce superoxide/H2O2 in vivo.

Topics: Animals; Cytochromes b; Electron Transport Complex I; Electron Transport Complex II; Female; Hydrogen Peroxide; Malates; Mitochondria, Muscle; Muscle, Skeletal; Oligomycins; Oxygen Consumption; Physical Conditioning, Animal; Rats; Rats, Wistar; Rest; Succinic Acid; Superoxides; Tissue Culture Techniques; Uncoupling Agents

The influence ofadenosine diphosphate (ADP) on respiration of pancreatic acinar cell mitochondria in situ was studied. The model of digitonin-treated pancreatic acini was used. It was found that succinate or a mixture of pyruvate, glutamate and malate intensified respiration ofpermeabilized cells. Low ADP concentration (100 microM) did not influence the rate of oxygen uptake, whereas at higher concentration (750 microM) brief intensification of respiration was observed when using nominally Ca(2+)-free medium. When the medium with 100 nM Ca2+ was used, ADP had no effect on oxygen uptake, while the rate of respiration stimulated by a mixture of pyruvate, glutamate and malate increased. Rate of succinate-stimulated respiration did not depend on Ca2+ content in medium. The presence of ATP in the medium reduced the stimulatory effect of ADP, but increased its duration. Intensification of respiration by ADP, occurred only at elevated Ca2+ content, was not associated with oxidative phosphorylation because oligomycin did not inhibit it. The effect ofADP might be a novel "functional marker" of development of pathological processes in the mitochondria of acinar pancreacytes.

Topics: Acinar Cells; Adenosine Diphosphate; Animals; Calcium; Cell Fractionation; Digitonin; Glutamic Acid; Malates; Male; Mitochondria; Oligomycins; Oxidative Phosphorylation; Oxygen; Pancreas; Permeability; Pyruvic Acid; Rats

No studies have been performed on the mitochondria of malaria vector mosquitoes. This information would be valuable in understanding mosquito aging and detoxification of insecticides, two parameters that have a significant impact on malaria parasite transmission in endemic regions. In the present study, we report the analyses of respiration and oxidative phosphorylation in mitochondria of cultured cells [ASE (Anopheles stephensi Mos. 43) cell line] from A. stephensi, a major vector of malaria in India, South-East Asia and parts of the Middle East. ASE cell mitochondria share many features in common with mammalian muscle mitochondria, despite the fact that these cells are of larval origin. However, two major differences with mammalian mitochondria were apparent. One, the glycerol-phosphate shuttle plays as major a role in NADH oxidation in ASE cell mitochondria as it does in insect muscle mitochondria. In contrast, mammalian white muscle mitochondria depend primarily on lactate dehydrogenase, whereas red muscle mitochondria depend on the malate-oxaloacetate shuttle. Two, ASE mitochondria were able to oxidize proline at a rate comparable with that of alpha-glycerophosphate. However, the proline pathway appeared to differ from the currently accepted pathway, in that oxoglutarate could be catabolized completely by the tricarboxylic acid cycle or via transamination, depending on the ATP need.

Topics: Amino Acids; Animals; Anopheles; Antimycin A; Carbohydrate Metabolism; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Cell Line; Cell Respiration; Chromatography, Liquid; Citric Acid Cycle; Glutamic Acid; Insect Vectors; Malaria; Malates; Metabolic Networks and Pathways; Mitochondria; Oligomycins; Oxidation-Reduction; Oxidative Phosphorylation; Oxygen Consumption; Pyruvic Acid; Tandem Mass Spectrometry

Mitochondrial calcium-activated K(+) (mitoK(Ca)) channels have been described as channels that are activated by Ca(2+), inner mitochondrial membrane depolarization and drugs such as NS-1619. NS-1619 is cardioprotective, leading to the assumption that this effect is related to the opening of mitoK(Ca) channels. Here, we show several weaknesses in this hypothesis.. Isolated mitochondria from rat hearts were tested for evidence of mitoK(Ca) activity by analyzing functional parameters in K(+)-rich and K(+)-free media.. NS-1619 promoted mitochondrial depolarization both in K(+)-rich and K(+)-free media. Respiratory rate increments were also seen in the presence of NS-1619 for both media. In parallel, NS-1619 promoted respiratory inhibition, as evidenced by respiratory measurements in state 3. Mitochondrial volume measurements conducted using light scattering showed that NS-1619 led to swelling, in a manner unaltered by inhibitors of mitoK(Ca) channels, antagonists of adenosine triphosphate-sensitive potassium channels or inhibitors of the permeability transition. Swelling was also maintained when K(+) in the media was substituted with tetraethylammonium (TEA(+)), which is not transported by any known K(+) carrier. Electron microscopy experiments gave support to the idea that NS-1619-induced mitochondrial swelling took place in the absence of K(+). In addition to testing the pharmacological effects of NS-1619, we attempted, unsuccessfully, to promote mitoK(Ca) activity by altering Ca(2+) concentrations in the medium and inducing mitochondrial uncoupling.. Our data indicate that NS-1619 promotes non-selective permeabilization of the inner mitochondrial membrane to ions, in addition to partial respiratory inhibition. Furthermore, we found no specific K(+) transport in isolated heart mitochondria compatible with mitoK(Ca) opening, whether by pharmacological or physiological stimuli. Our results indicate that NS-1619 has extensive mitochondrial effects unrelated to mitoK(Ca) and suggest that tissue protection mediated by NS-1619 may occur through mechanisms other than activation of these channels.

Topics: Animals; Benzimidazoles; Calcium; Culture Media; Glutamic Acid; Ion Channel Gating; Malates; Membrane Potentials; Microscopy, Electron, Transmission; Microscopy, Fluorescence; Mitochondria, Heart; Mitochondrial Membranes; Mitochondrial Swelling; NADP; Oligomycins; Oxidation-Reduction; Oxygen Consumption; Phenazines; Potassium; Potassium Channels, Calcium-Activated; Rats; Rats, Sprague-Dawley; Rotenone; Sodium; Succinic Acid; Tetraethylammonium; Tissue Culture Techniques; Uncoupling Agents

Mitochondrial membrane potential (delta psi(m)) plays an important role in cellular activity. Although delta psi(m) of intracellular mitochondria are relatively stable, the recent experiments with isolated mitochondria demonstrate that individual mitochondria show frequent fluctuations of delta psi(m). The current study is performed to investigate the factors that stabilize delta psi(m) in cells by observing delta psi(m) of individual isolated mitochondria with fluorescence microscopy. Here, we report that (1) the transient depolarizations are also induced for mitochondria in plasma membrane permeabilized cells, (2) almost all mitochondria isolated from porcine hearts show the transient depolarizations that is enhanced with the net efflux of protons from the matrix to the intermembrane space, and (3) ATP and ADP significantly inhibit the transient depolarizations by plural mechanisms. These results suggest that the suppression of acute alkalinization of the matrix together with the presence of ATP and ADP contributes to the stabilization of delta psi(m) in cells.

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Malates; Membrane Potentials; Mitochondria, Heart; NADP; Oligomycins; Rats; Rotenone; Succinic Acid; Swine

The mitochondrial membrane potential measured in isolated rat kidney mitochondria and in digitonin-permeabilized MDCK type II cells pre-energized with succinate, glutamate, and/or malate was reduced by micromolar diclofenac dose-dependently. However, ATP biosynthesis from glutamate/malate was significantly more compromised compared to that from succinate. Inhibition of the malate-aspartate shuttle by diclofenac with a resultant decrease in the ability of mitochondria to generate NAD(P)H was demonstrated. Diclofenac however had no effect on the activities of NADH dehydrogenase, glutamate dehydrogenase, and malate dehydrogenase. In conclusion, decreased NAD(P)H production due to an inhibition of the entry of malate and glutamate via the malate-aspartate shuttle explained the more pronounced decreased rate of ATP biosynthesis from glutamate and malate by diclofenac. This drug, therefore affects the bioavailability of two major respiratory complex I substrates which would normally contribute substantially to supplying the reducing equivalents for mitochondrial electron transport for generation of ATP in the renal cell.

Topics: Acute Kidney Injury; Adenosine Triphosphate; Animals; Aspartic Acid; Benzimidazoles; Carbocyanines; Cells, Cultured; Diclofenac; Dogs; Glutamate Dehydrogenase; Kidney; Malate Dehydrogenase; Malates; Membrane Potentials; Mitochondria; Mitochondrial Membranes; NADH Dehydrogenase; Oligomycins; Rats

We measured production of reactive oxygen species by intact mitochondria from rat skeletal muscle, heart, and liver under various experimental conditions. By using different substrates and inhibitors, we determined the sites of production (which complexes in the electron transport chain produced superoxide). By measuring hydrogen peroxide production in the absence and presence of exogenous superoxide dismutase, we established the topology of superoxide production (on which side of the mitochondrial inner membrane superoxide was produced). Mitochondria did not release measurable amounts of superoxide or hydrogen peroxide when respiring on complex I or complex II substrates. Mitochondria from skeletal muscle or heart generated significant amounts of superoxide from complex I when respiring on palmitoyl carnitine. They produced superoxide at considerable rates in the presence of various inhibitors of the electron transport chain. Complex I (and perhaps the fatty acid oxidation electron transfer flavoprotein and its oxidoreductase) released superoxide on the matrix side of the inner membrane, whereas center o of complex III released superoxide on the cytoplasmic side. These results do not support the idea that mitochondria produce considerable amounts of reactive oxygen species under physiological conditions. Our upper estimate of the proportion of electron flow giving rise to hydrogen peroxide with palmitoyl carnitine as substrate (0.15%) is more than an order of magnitude lower than commonly cited values. We observed no difference in the rate of hydrogen peroxide production between rat and pigeon heart mitochondria respiring on complex I substrates. However, when complex I was fully reduced using rotenone, rat mitochondria released significantly more hydrogen peroxide than pigeon mitochondria. This difference was solely due to an elevated concentration of complex I in rat compared with pigeon heart mitochondria.

Topics: Aging; Animals; Antimycin A; Columbidae; Electron Transport; Enzyme Inhibitors; Female; Hydrogen Peroxide; Liver; Malates; Methacrylates; Mitochondria, Liver; Mitochondria, Muscle; Muscle, Skeletal; Myocardium; Oligomycins; Oxidants; Palmitoylcarnitine; Pyruvic Acid; Rats; Rats, Wistar; Reactive Oxygen Species; Reference Standards; Rotenone; Succinic Acid; Superoxide Dismutase; Superoxides; Thiazoles; Uncoupling Agents

Epididymal sperm maturation culminates in the acquisition of functional competence by testicular spermatozoa. The expression of this functional state is dependent upon a redox-regulated, cAMP-mediated signal transduction cascade that controls the tyrosine phosphorylation status of the spermatozoa during capacitation. Analysis of superoxide anion (O2(-.)) generation by rat epididymal spermatozoa has revealed a two-component process involving electron leakage from the sperm mitochondria at complexes I and II and a plasma membrane NAD(P)H oxidoreductase. Following incubation in a glucose-, lactate-, and pyruvate-free medium (-GLP), O2(-.) generation was suppressed by 86% and 96% in caput and cauda spermatozoa, respectively. The addition of lactate, malate, or succinate to spermatozoa incubated in medium -GLP stimulated O2(-.) generation. This increase could be blocked by rotenone and oligomycin (R/O) in the presence of malate or lactate but not succinate. Stimulation with all three substrates, as well as spontaneous O2(-.) production in +GLP medium, was blocked by the flavoprotein inhibitor, diphenylene iodonium. Diphenylene iodonium, but not R/O, suppressed NAD(P)H-induced lucigenin-dependent chemiluminescence. This NAD(P)H-dependent enzyme resided in the sperm plasma membrane and its activity was regulated by zinc and uncharacterized cytosolic factors. Reverse transcription-polymerase chain reaction analysis indicated that the sperm NAD(P)H oxidoreductase complex is quite distinct from the equivalent leukocyte system.

Topics: Animals; Cell Membrane; Epididymis; Lactic Acid; Leukocytes; Malates; Male; Mitochondria; NAD; NADP; NADPH Oxidases; Oligomycins; Onium Compounds; Oxidation-Reduction; Rats; Reactive Oxygen Species; Rotenone; Spermatozoa; Succinic Acid; Superoxides; Uncoupling Agents; Zinc

Acetoacetate provision to Ca(2+)-loaded liver mitochondria (less than 40 micrograms-ion Ca2+ x g protein-1), supplied with 2 mM Pi and 2-oxoglutarate as substrate, was found to prevent the mitochondrial deenergization and Ca2+ release induced by either rotenone during aerobic incubations or by O2 deprivation. Under the latter condition, the acetoacetate-promoted Ca2+ retention was entirely supported by ATP produced anaerobically at the succinylthiokinase step of the tricarboxylic acid cycle and was therefore abolished by addition of oligomycin. Surprisingly, oligomycin was also found to trigger Ca2+ release in rotenone-inhibited mitochondria in the presence of acetoacetate under aerobic conditions, unless a Pi acceptor was supplied. ADP deprivation at the succinylthiokinase step is likely to be involved. As estimated from rates of succinate production in O2-deprived mitochondria or from respiration rates in rotenone-inhibited mitochondria at supramaximal acetoacetate concentrations (above 1.2 mM) in the presence of a Pi acceptor, ATP production by substrate-level phosphorylation was close to 10 mumol.g protein-1.min-1 and appeared to be limited by rates of ketone body transport across the inner membrane. The rates of anaerobic energy production obtained by coupling 2-oxoglutarate oxidation to acetoacetate reduction were markedly higher than those obtained by reactions involved in the anaerobic metabolism of amino acids, simulated by providing 2-oxoglutarate and malate to mitochondria. Energy production was limited by rates of oxidant equivalent generation under the latter condition. Our data suggest that acetoacetate could effectively contribute to sustaining anaerobic energy production from endogenous substrates in liver tissue.

Topics: Acetoacetates; Adenosine Diphosphate; Adenosine Triphosphate; Anaerobiosis; Animals; Calcium; Citric Acid Cycle; Energy Metabolism; Ketoglutaric Acids; Malates; Mitochondria, Liver; NAD; Oligomycins; Oxygen; Phosphates; Rats; Rats, Inbred Strains; Rotenone; Succinates; Succinic Acid

The effects of amiodarone on the respiration of isolated mouse liver mitochondria have been determined. Amiodarone (200 microM) had a biphasic effect on state 4 respiration supported by either glutamate plus malate or succinate. Initially, the respiratory rate was increased. This stimulatory effect was not prevented by oligomycin (an inhibitor of ATP synthase). It was associated with marked accumulation of amiodarone in the mitochondria, and with collapse of the mitochondrial membrane potential. This initial uncoupling effect was followed by a progressive decrease in the state 4 respiration rate, leading eventually to marked inhibition. Preincubation for 5 min with amiodarone (200 microM) also decreased markedly ADP-stimulated (state 3) respiration, ATP production and dinitrophenol-stimulated (uncoupled) respiration supported by glutamate plus malate (which donate electrons to complex I), and respiration supported by succinate (which donate electrons to complex II), but did not affect respiration supported by duroquinol (donating electrons to complex III) or by ascorbate plus N,N,N',N'-tetramethyl-p-phenylenediamine (donating electrons to cytochrome c). Preincubation with amiodarone (150-200 microM) decreased markedly respiration mediated by fatty acids of various chain length and respiration mediated by citrate, a tricarboxylic acid cycle substrate. We conclude that amiodarone has a dual effect on mitochondrial respiration. The initial uncoupling effect is probably due to the entry of protonated amiodarone, releasing a proton in the matrix. Accumulation of amiodarone soon leads to inhibition of the respiratory chain at the levels of complex I and complex II and to decreased ATP formation.

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amiodarone; Animals; Dinitrophenols; Drug Synergism; Fatty Acids; Glutamates; Glutamic Acid; Malates; Male; Membrane Potentials; Mice; Mitochondria, Liver; Oligomycins; Oxygen Consumption; Protons; Stimulation, Chemical; Succinates; Succinic Acid; Tetraphenylborate

Mitochondrial dysfunction has been implicated as the cause of irreversible injury in the ischemic heart. To circumvent artifacts associated with organelle isolation, mitochondrial function was studied in intact isolated, Ca2+-tolerant rat ventricular myocytes. After 30 min of anaerobic incubation, myocyte viability decreased from 76 +/- 1 to 33 +/- 4%. Basal O2 consumption rates (nanoatoms . mg cell protein-1 . min-1) were 17.1 +/- 1.3 in aerobic cells and 51.0 +/- 9.8 in anoxic cells. Carbonylcyanide-p-trifluoromethoxyphenyl hydrazone (FCCP)-stimulated rates were 65.5 +/- 9.2 and 84.5 +/- 15.3 in aerobic and anoxic cells, respectively. Respiratory control ratio was lower in anoxic cells: 2.3 +/- 0.3 versus 4.2 +/- 0.4 in aerobic cells. These data suggest that early anoxic mitochondrial injury is due to increased permeability of the inner membrane. Addition of pyruvate, malate, and FCCP to cells made permeable by digitonin resulted in similar maximal O2 consumption rates: 276.5 +/- 31.8 in aerobic and 299.3 +/- 31.9 in anoxic cells, suggesting the electron transport chain is intact in anoxic cells. For purposes of investigating whether anoxic mitochondrial dysfunction is secondary to cellular or mitochondrial Ca2+ overload, total cell Ca2+, cytosolic free Ca2+ levels (measured by null-point titration), and mitochondrial Ca2+ contents (measured as FCCP-releasable Ca2+) were measured. There were no differences in these three parameters between aerobic and anoxic cells, suggesting that mitochondrial dysfunction and irreversible hypercontraction of isolated cardiac myocytes exposed to 30 min of anoxia are not related to Ca2+ overload.

Topics: Animals; Calcimycin; Calcium; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Cell Membrane Permeability; Digitonin; Malates; Mitochondria, Heart; Myocardial Contraction; Oligomycins; Oxygen; Oxygen Consumption; Pyruvates; Pyruvic Acid; Rats; Ruthenium Red; Time Factors

With a variety of forms of ischemic and toxic tissue injury, cellular accumulation of Ca2+ and generation of oxygen free radicals may have adverse effects upon cellular and, in particular, mitochondrial membranes. Damage to mitochondria, resulting in impaired ATP synthesis and diminished activity of cellular energy-dependent processes, could contribute to cell death. In order to model, in vitro, conditions present post-ischemia or during toxin exposure, the interactions between Ca2+ and oxygen free radicals on isolated renal mitochondria were characterized. The oxygen free radicals were generated by hypoxanthine and xanthine oxidase to simulate in vitro one of the sources of oxygen free radicals in the early post-ischemic period in vivo. With site I substrates, pyruvate and malate, Ca2+ pretreatment, followed by exposure to oxygen free radicals, resulted in an inhibition of electron transport chain function and complete uncoupling of oxidative phosphorylation. These effects were partially mitigated by dibucaine, a phospholipase A2 inhibitor. With the site II substrate, succinate, the electron transport chain defect was not manifest and respiration remained partially coupled. The electron transport chain defect produced by Ca2+ and oxygen free radicals was localized to NADH CoQ reductase. Calcium and oxygen free radicals reduced mitochondrial ATPase activity by 55% and adenine nucleotide translocase activity by 65%. By contrast oxygen free radicals alone reduced ATPase activity by 32% and had no deleterious effects on translocase activity. Dibucaine partially prevented the Ca2+-dependent reduction in ATPase activity and totally prevented the Ca2+-dependent translocase damage observed in the presence of oxygen free radicals. These findings indicate that calcium potentiates oxygen free radical injury to mitochondria. The Ca2+-induced potentiation of oxygen free radical injury likely is due in part to activation of phospholipase A2. This detrimental interaction associated with Ca2+ uptake by mitochondria and exposure of the mitochondria to oxygen free radicals may explain the enhanced cellular injury observed during post-ischemic reperfusion.

Topics: Animals; ATP Synthetase Complexes; Calcium; Dibucaine; Free Radicals; Ischemia; Kidney; Malates; Male; Mitochondria; Models, Biological; Multienzyme Complexes; Oligomycins; Oxygen; Oxygen Consumption; Phosphotransferases; Proton-Translocating ATPases; Pyruvates; Pyruvic Acid; Quinone Reductases; Rats; Rats, Inbred Strains

Oxygen electrode polarographic measurements of the rate of oxygen consumption by isolated rat liver mitochondria revealed that oligomycin inhibition of respiration was offset to different degrees by varying concentrations of perfluidone (1,1,1-trifluoro-N-(2 methyl-4-(phenylsulfonyl) methanesulfonamide). Using any of pyruvate-malate, succinate or ascorbate-TMPD (N,N,N',N'-tetramethyl-p-phenylenediamine) as substrate, this herbicidal and anti-inflammatory agent at 100 microM concentration caused a 5-fold stimulation of oligomycin-inhibited respiration. Higher concentrations of the herbicide (greater than or equal to 120 microM) gave lower stimulatory effects. Similar stimulatory effects were obtained with 1 microM FCCP (carbonylcyanide p-trifluoromethyoxyphenyl-hydrazone), a classical protonophore. Our results also show an enhanced oligomycin-sensitive ATPase action in intact mitochondria incubated with ATP and varying concentrations of perfluidone. Maximum enhancement effect (111.3%) was obtained at 120 microM perfluidone. FCCP (1 microM) stimulated this ATPase action by 130%. An initial inhibition of respiration by oligomycin is due to an interaction with the proton well of FOF1-ATP synthetase (Lardy, H.A. et al., Arch. Biochem. Biophys., 78 (1953) 587). Perfluidone probably increases the proton conductance of mitochondrial inner membrane in the same manner as FCCP and thus causes an increase in mitochondrial respiratory rate. As protons move into the matrix, delta mu H+, the proton electrochemical potential gradient becomes very small and the F0F1-ATP synthetase functions in the direction of hydrolysis of ATP rather than its shnthesis (Mitchell, P., Eur. J. Biochem., 95 (1979) 1). These findings therefore indicate that perfluidone acts in a way similar to FCCP, a classical uncoupler and protonophore.

Topics: Adenosine Triphosphatases; Animals; Ascorbic Acid; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Drug Interactions; Electrodes; Enzyme Activation; Herbicides; Malates; Mitochondria, Liver; Oligomycins; Oxygen Consumption; Proteins; Pyruvates; Rats; Rats, Inbred Strains; Succinates; Succinic Acid; Sulfones; Tetramethylphenylenediamine

An evaluation of the efficiency of the L-alanine and L-malate transport systems was undertaken with the photosynthetic bacterium Rhodospirillum rubrum grown on the amino acid whose uptake was measured. An all-glass apparatus was constructed for measuring transport activity under anaerobic conditions. L-Alanine transport activity decreased under conditions of Mg2+ depletion. When cells were allowed to become inactive by suspending them in the dark in Mg2+-free buffer, full activity could be restored with a few minutes by adding 20 mM Mg2+ and illuminating the cells. The transport activity was completely inhibited by carbonyl cyanide m-trifluoromethoxyphenylhydrazone and by ammonia. The quantum yield for the uptake of either L-alanine or L-malate was 0.015 molecules per photon. The results are discussed in relation to the expected efficiencies for metabolite transport and regulation by Mg2+.

Topics: Alanine; Antimycin A; Biological Transport, Active; Dicyclohexylcarbodiimide; Electron Transport; Kinetics; Light; Magnesium; Malates; Oligomycins; Oxygen; Rhodospirillum rubrum

Topics: Adenosine Triphosphate; Ammonia; Amobarbital; Anti-Bacterial Agents; Aspartic Acid; Dinitrophenols; Enzyme Inhibitors; Glutamates; Glutamic Acid; Hydrogen; Ketoglutaric Acids; Liver; Malates; Mitochondria; Mitochondria, Liver; NAD; Oligomycins; Pharmacology; Rats; Research