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Literature DB >> 720604

Is mitochondrial cytochrome b-566/558 a single hemoprotein or two individual components? A magnetic circular dichroism study.

A M Arutjunjan, Y A Kamensky, E Milgröm, S Surkov, A A Konstantinov, Y A Sharonov.

Abstract

Entities: Gene

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Year: 1978 PMID： 720604 DOI： 10.1016/0014-5793(78)80047-7

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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2 in total

1. The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Q_o site of bacterial cytochrome bc₁.

Authors: Francesco Francia; Marco Malferrari; Pascal Lanciano; Stefan Steimle; Fevzi Daldal; Giovanni Venturoli
Journal: Biochim Biophys Acta Date: 2016-09-05

2. The pathway of electron flow through ubiquinol:cytochrome c oxidoreductase in the respiratory chain. Evidence from inhibition studies for a modified 'Q cycle'.

Authors: A P Halestrap
Journal: Biochem J Date: 1982-04-15 Impact factor: 3.857

2 in total

Is mitochondrial cytochrome b-566/558 a single hemoprotein or two individual components? A magnetic circular dichroism study.

1. The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1.

2. The pathway of electron flow through ubiquinol:cytochrome c oxidoreductase in the respiratory chain. Evidence from inhibition studies for a modified 'Q cycle'.

1. The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Q_o site of bacterial cytochrome bc₁.