Chance 1961 J Biol Chem-VI: Difference between revisions
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{{Publication | {{Publication | ||
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria VI. The efficiency of the reaction. J Biol Chem 236: 1577- | |title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria VI. The efficiency of the reaction. J Biol Chem 236:1577-84. | ||
|info=[http://www.jbc.org/content/236/5/1577.full.pdf+html PMID: 13692280 Open Access] | |info=[http://www.jbc.org/content/236/5/1577.full.pdf+html PMID: 13692280 Open Access] | ||
|authors=Chance B, Hollunger G | |authors=Chance B, Hollunger G | ||
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|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=The stoichiometry and efficiency of the interaction of adenosine 5’-triphosphate with the respiratory carriers has been evaluated. From oxidative recovery data, the adenosine 5’-triphosphate-electron ratio is about 1. Values from 1.0 to 1.5 are obtained from the direct effects of adenosine 5’-triphosphate in both the reduction of pyridine nucleotide and the oxidation of cytochrome, although the computations indicating a low stoichiometric ratio for oxidizing equivalents are based upon more assumptions than in the case of reducing equivalents. There is rough agreement in the number of oxidizing equivalents found in cytochrome and the number of reducing equivalents found in pyridine nucleotide, provided succinate is absent. The reversal of electron transfer occurs with the expenditure of a remarkably small amount of energy (fifteen thousand calories) in cytochrome oxidation and pyridine nucleotide reduction in the respiratory chain. An interpretation of such data suggests that the principal point of entry of adenosine 5’-triphosphate may be at the pyridine nucleotide-flavin couple, but the entry of adenosine 5’-triphosphate simultaneously at other points is also consistent with these data. | |abstract=The stoichiometry and efficiency of the interaction of adenosine 5’-triphosphate with the respiratory carriers has been evaluated. From oxidative recovery data, the adenosine 5’-triphosphate-electron ratio is about 1. Values from 1.0 to 1.5 are obtained from the direct effects of adenosine 5’-triphosphate in both the reduction of pyridine nucleotide and the oxidation of cytochrome, although the computations indicating a low stoichiometric ratio for oxidizing equivalents are based upon more assumptions than in the case of reducing equivalents. There is rough agreement in the number of oxidizing equivalents found in cytochrome and the number of reducing equivalents found in pyridine nucleotide, provided succinate is absent. The reversal of electron transfer occurs with the expenditure of a remarkably small amount of energy (fifteen thousand calories) in cytochrome oxidation and pyridine nucleotide reduction in the respiratory chain. An interpretation of such data suggests that the principal point of entry of adenosine 5’-triphosphate may be at the pyridine nucleotide-flavin couple, but the entry of adenosine 5’-triphosphate simultaneously at other points is also consistent with these data. | ||
|keywords=ATP, | |keywords=ATP, Pyridine nucleotide, Cytochrome oxidation, Electron transfer, Energy efficiency | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism= | |organism=Guinea pig, Birds | ||
|tissues= | |tissues=Heart, Liver, Kidney | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex II; | |enzymes=Complex II;succinate dehydrogenase, Complex V;ATP synthase | ||
| | |topics=ADP, Coupling efficiency;uncoupling | ||
| | |couplingstates=OXPHOS | ||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 09:54, 9 November 2016
| Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria VI. The efficiency of the reaction. J Biol Chem 236:1577-84. |
Chance B, Hollunger G (1961) J Biol Chem
Abstract: The stoichiometry and efficiency of the interaction of adenosine 5’-triphosphate with the respiratory carriers has been evaluated. From oxidative recovery data, the adenosine 5’-triphosphate-electron ratio is about 1. Values from 1.0 to 1.5 are obtained from the direct effects of adenosine 5’-triphosphate in both the reduction of pyridine nucleotide and the oxidation of cytochrome, although the computations indicating a low stoichiometric ratio for oxidizing equivalents are based upon more assumptions than in the case of reducing equivalents. There is rough agreement in the number of oxidizing equivalents found in cytochrome and the number of reducing equivalents found in pyridine nucleotide, provided succinate is absent. The reversal of electron transfer occurs with the expenditure of a remarkably small amount of energy (fifteen thousand calories) in cytochrome oxidation and pyridine nucleotide reduction in the respiratory chain. An interpretation of such data suggests that the principal point of entry of adenosine 5’-triphosphate may be at the pyridine nucleotide-flavin couple, but the entry of adenosine 5’-triphosphate simultaneously at other points is also consistent with these data. • Keywords: ATP, Pyridine nucleotide, Cytochrome oxidation, Electron transfer, Energy efficiency
Labels:
Organism: Guinea pig, Birds
Tissue;cell: Heart, Liver, Kidney
Preparation: Isolated mitochondria
Enzyme: Complex II;succinate dehydrogenase, Complex V;ATP synthase
Regulation: ADP, Coupling efficiency;uncoupling
Coupling state: OXPHOS
Made history
