Difference between revisions of "Hatefi 1962 J Biol Chem-XLI"
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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- | |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 | ||
|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=[[Q-junction]], Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart | |keywords=[[Electron transfer-pathway]], [[Q-junction]], Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart | ||
}} | }} | ||
== Cited by == | |||
{{Template:Cited by Gnaiger 2020 BEC MitoPathways}} | |||
{{Labeling | {{Labeling | ||
|organism=Bovines | |organism=Bovines | ||
| Line 14: | Line 17: | ||
|enzymes=Complex IV;cytochrome c oxidase | |enzymes=Complex IV;cytochrome c oxidase | ||
|topics=Substrate | |topics=Substrate | ||
|couplingstates= | |couplingstates=ET | ||
|additional=Made history | |additional=Made history, BEC 2020.2 | ||
}} | }} | ||
Latest revision as of 17:16, 16 January 2021
| 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. |
» 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 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: Electron transfer-pathway, Q-junction, Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart
Cited by
- Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex IV;cytochrome c oxidase
Regulation: Substrate
Coupling state: ET
Made history, BEC 2020.2
