Difference between revisions of "Hatefi 1962 J Biol Chem-XLI"
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|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=The preparation from beef heart mitochondria and the properties, of a highly active and stable enzyme system, capable of catalyzing the reduction of cytochrome c by reduced coenzyme Q2 are described. The enzyme complex contains cytochrome b and cytochrome c1 in high concentration, and is free of cytochrome c oxidase, cytochrome c, flavoproteins, and the citric acid cycle dehydrogenases. The activity of the enzyme corresponds to a QO2, of about 320,000 at 38°. This activity is strongly inhibited by antimycin A, 2-nonyl-4-hydroxy-quinoline-N-oxide, and 2-alkyl-3-hydroxynaphthoquinone. Amytal, thenoyltrifluoroacetone, and a number of specific metal-chelating compounds are ineffective as inhibitors. | |abstract=The preparation from beef heart mitochondria and the properties, of a highly active and stable enzyme system, capable of catalyzing the reduction of cytochrome c by reduced coenzyme Q2 are described. The enzyme complex contains cytochrome b and cytochrome c1 in high concentration, and is free of cytochrome c oxidase, cytochrome c, flavoproteins, and the citric acid cycle dehydrogenases. The activity of the enzyme corresponds to a QO2, of about 320,000 at 38°. This activity is strongly inhibited by antimycin A, 2-nonyl-4-hydroxy-quinoline-N-oxide, and 2-alkyl-3-hydroxynaphthoquinone. Amytal, thenoyltrifluoroacetone, and a number of specific metal-chelating compounds are ineffective as inhibitors. | ||
|keywords=Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart | |keywords=[[Q-junction]], Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart | ||
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Revision as of 22:40, 31 May 2014
| Hatefi Y, Haavik AG, Griffiths DE (1962) Studies on the electron transfer system XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237: 1681-1685. |
Hatefi Y, Haavik AG, Griffiths DE (1962) J Biol Chem
Abstract: The preparation from beef heart mitochondria and the properties, of a highly active and stable enzyme system, capable of catalyzing the reduction of cytochrome c by reduced coenzyme Q2 are described. The enzyme complex contains cytochrome b and cytochrome c1 in high concentration, and is free of cytochrome c oxidase, cytochrome c, flavoproteins, and the citric acid cycle dehydrogenases. The activity of the enzyme corresponds to a QO2, of about 320,000 at 38°. This activity is strongly inhibited by antimycin A, 2-nonyl-4-hydroxy-quinoline-N-oxide, and 2-alkyl-3-hydroxynaphthoquinone. Amytal, thenoyltrifluoroacetone, and a number of specific metal-chelating compounds are ineffective as inhibitors. • Keywords: Q-junction, Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart
Labels:
Organism: Bovines
Tissue;cell: Heart
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 IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" 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: Substrate
Coupling state: ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.
Made history
