Chance 1961 J Biol Chem-VI: Difference between revisions
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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=Mammals, Other Non-Mammal | ||
|tissues=Cardiac muscle, Hepatocyte; Liver, Kidney | |tissues=Cardiac muscle, Hepatocyte; Liver, Kidney | ||
|preparations=Isolated Mitochondria | |preparations=Isolated Mitochondria | ||
Revision as of 17:34, 12 February 2013
| 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: 1577-1584. |
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: Mammals"Mammals" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property., Other Non-Mammal"Other Non-Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property., Hepatocyte; Liver"Hepatocyte; Liver" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property., Kidney
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property., Complex V; ATP Synthase"Complex V; ATP Synthase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
Coupling state: OXPHOS
Made history
