Reaction of thionitrobenzoate‐modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase

FEBS Letters

Georgevich, Gradimir¹  Capaldi, Roderick A.¹  Darley-Usmar, Victor M.¹ 

[1] Institute of Molecular Biology, University of Oregon, Eugene OR, USA

关键词: Cytochrome c;    Cytochrome c oxidase;    Thionitrobenzoate;    Electron transfer;   

DOI  :  10.1016/0014-5793(84)80058-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thionitrobenzoate-modified yeast cytochrome c was shown to react with both monomeric and dimeric forms of beef heart cytochrome c oxidase through subunit III. This cytochrome c derivative was found to inhibit electron transfer in the dimer but not in the monomer. These results are interpreted to show that the high affinity binding site for cytochrome c is a cleft at the interface between monomers in the cytochrome c oxidase dimer.

【 授权许可】

Unknown