Hatefi 1962 J Biol Chem-XLI: Difference between revisions
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|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- | |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 237:1681-5. | ||
|info=[http://www.jbc.org/content/237/5/1681.long | |info=[http://www.ncbi.nlm.nih.gov/pubmed/13905328 PMID: 13905328 Open Access]; [http://www.jbc.org/content/237/5/1681.long PDF] | ||
|authors=Hatefi Y, Haavik AG, Griffiths DE | |authors=Hatefi Y, Haavik AG, Griffiths DE | ||
|year=1962 | |year=1962 |
Revision as of 11:33, 28 May 2015
Hatefi Y, Haavik AG, Griffiths DE (1962) Studies on the electron transfer system XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237:1681-5. |
ยป PMID: 13905328 Open Access; PDF
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 38ยฐ. 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. โข Keywords: Q-junction, Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex IV;cytochrome c oxidase
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