The nature of CuA in cytochrome c oxidase

FEBS Letters

Li, Peter Mark¹  Chan, Sunney I.¹  Malmström, Bo G.¹ 

[1] Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA

关键词: Cytochrome-c oxidase;    Copper A;    Nitrous oxide reductase;    Mixed-valence binuclear center;    EPR;   

DOI  :  10.1016/0014-5793(89)80463-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Kroneek et al. [(1988) FEBS Lett. 242, 70–74] have recently suggested, on the basis of a comparison with the EPR properties of nitrous oxide reductase, that cytochrome c oxidase contains a mixed-valence binuclear copper site, and that this is responsible for the EPR spectrum generally ascribed to Cu_A. Here we question this hypothesis in view of a multitude of analytical and spectroscopic data available. We maintain that a mononuclear Cu site with two cysteine sulfur and two imidazole nitrogen atoms as ligands is consistent with the current experimental information on the Cu_A site.

【 授权许可】

Unknown