The reduction of cytochrome c oxidase by carbon monoxide

FEBS Letters

Brzezinski, Peter¹  Malmström, Bo G.¹ 

[1] Department of Biochemistry and Biophysics, University of Göteborg and Chalmers University of Technology, S-412 96 Göteborg, Sweden

关键词: Cytochrome c oxidase Cytochrome a3 Carbon monoxide Reduction kinetics Heme pocket Mixed-valence state;   

DOI  :  10.1016/0014-5793(85)81224-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The rate of formation of the mixed-valence state of cytochrome c oxidase on incubation with carbon monoxide is strongly dependent on pH, supporting the concept that CO itself is the reducing agent. The reaction is biphasic due to the presence of two different enzyme forms in the resting oxidase. The kinetics of the reaction with the major enzyme form suggests an initial rapid binding of CO in a heme pocket of the oxidized enzyme and a subsequent slow intramolecular electron transfer to the cytochrome a ₃-Cu_B site. Cytochrome a and Cu_A are not reduced even on prolonged incubation.

【 授权许可】

Unknown