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1.
Biokhimiia ; 56(8): 1420-8, 1991 Aug.
Article in Russian | MEDLINE | ID: mdl-1782265

ABSTRACT

Regulation of respiration at all rates between State 4 and State 3 was studied in heart mitochondria oxidizing FAD- and NAD-dependent substrates (succinate, pyruvate + + malate and palmitoylcarnitine). The creatine phosphokinase ADP-regenerating system was used which allows to fix the concentrations of extramitochondrial adenine nucleotides in such a way that the rate of respiration is controlled by mitochondrial processes alone. It was shown that respiration is controlled by delta mu(H+)-utilizing system within the respiration rate interval from State 4 till 70-80% of the maximal rate in State 3 (corresponding to physiological rates) both for NAD- and FAD-dependent substrates. The main step in the control of respiration near State 4 is proton leakage through the inner mitochondrial membrane, whereas in all the other parts of the mentioned interval this role is assigned to the adenine nucleotide translocator (ANT). The control coefficient for ANT is higher, while that of proton leakage is lower at the same relative rates of respiration with NAD-dependent substrates compared with succinate. These differences were found to be related to much higher values of the membrane potential generated at the same relative rates of succinate oxidation in comparison with the case with pyruvate + + malate. The contribution of delta mu(H+)-utilizing system to respiration control sharply decreases, whereas that of the delta mu(H+)-generating system increases at maximal rates of respiration near State 3. This phenomenon in more characteristic of succinate. In this case the control coefficient of ANT drops to zero, while that of succinate dehydrogenase rises to 0.7.


Subject(s)
Mitochondria, Heart/metabolism , NAD/metabolism , Oxygen/metabolism , Succinates/metabolism , Adenine Nucleotides/metabolism , Animals , Creatine Kinase/metabolism , Flavin-Adenine Dinucleotide/metabolism , Mitochondria, Heart/enzymology , Oxidation-Reduction , Rabbits , Substrate Specificity , Succinic Acid
2.
Biokhimiia ; 54(12): 1947-51, 1989 Dec.
Article in Russian | MEDLINE | ID: mdl-2633800

ABSTRACT

The effect of intramitochondrial acyl-CoA on the respiration of rabbit heart mitochondria in different metabolic states was studied. Acyl-CoA inhibited O2 consumption by 11% in State 4 and by 6% in State 3. However, the effect of acyl-CoA was more pronounced (20%) in the intermediate state of respiration between State 4 and State 3. The data obtained suggest that acyl-CoA can regulate oxidative phosphorylation in heart mitochondria in vivo.


Subject(s)
Acyl Coenzyme A/metabolism , Mitochondria, Heart/metabolism , Myocardium/metabolism , Oxidative Phosphorylation , Adenosine Diphosphate/metabolism , Animals , Creatine Kinase/metabolism , Kinetics , Mitochondria, Heart/enzymology , Myocardium/enzymology , Oxygen Consumption , Rabbits
3.
Biokhimiia ; 53(6): 1009-12, 1988 Jun.
Article in Russian | MEDLINE | ID: mdl-2846076

ABSTRACT

The regulatory role of adenine nucleotide translocase in oxidative phosphorylation was determined by titration of respiration of isolated rabbit heart mitochondria with carboxyatractyloside in the creatine phosphokinase ADP-regenerating system, which is not rate-limiting. It was found that the respiration rate is not controlled by adenine nucleotide translocase in states 3 and 4. Within the physiological region of respiration (30-70% of the maximal rate), the control coefficient for ADP/ATP translocase is 0.62-0.75. Thus, translocase plays a key role in the regulation of oxidative phosphorylation.


Subject(s)
Mitochondria, Heart/metabolism , Mitochondrial ADP, ATP Translocases/metabolism , Nucleotidyltransferases/metabolism , Oxidative Phosphorylation , Animals , Kinetics , Mitochondria, Heart/enzymology , Oxidation-Reduction , Phosphocreatine/metabolism , Rabbits , Succinates/metabolism
4.
Biull Eksp Biol Med ; 105(5): 540-2, 1988 May.
Article in Russian | MEDLINE | ID: mdl-3382729

ABSTRACT

A regulatory role of adenine nucleotide translocator (ANT) was determined by titration of mitochondrial respiration (state 3) with carboxyatractyloside. It was shown that ANT regulates pyruvate oxidation: the control strength is more pronounced after depletion of endogenous substrates or after the increase in extramitochondrial ATP/ADP. The rate of succinate oxidation is controlled mainly by succinate dehydrogenase, while ANT does not participate in its regulation.


Subject(s)
Adenine Nucleotides/metabolism , Mitochondria, Heart/metabolism , Pyruvates/metabolism , Adenosine Diphosphate/metabolism , Adenosine Triphosphate/metabolism , Animals , Atractyloside/analogs & derivatives , Atractyloside/analysis , Oxidative Phosphorylation , Rabbits , Succinate Dehydrogenase/metabolism
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