Hatefi 1962 J Biol Chem-XLI: Difference between revisions
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{{Publication | {{Publication | ||
|title=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. | |title=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. | ||
|info= | |info=[http://www.jbc.org/content/237/5/1681.long PMID: 13905328 Open Access] | ||
|authors=Hatefi Y, Haavik AG, Griffiths DE | |authors=Hatefi Y, Haavik AG, Griffiths DE | ||
|year=1962 | |year=1962 | ||
|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= | |keywords=Coenzyme Q, reduced coenzyme Q (QH2), cytochrome c reductase | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
Revision as of 12:46, 12 June 2012
| 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: Coenzyme Q, reduced coenzyme Q (QH2), cytochrome c reductase
Labels:
Organism: Other Mammal"Other 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.
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.
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