Activity of proteoliposomes containing cytochrome oxidase in the submitochondrial orientation

FEBS Letters

Cooper, C.E.¹  Nicholls, P.¹ 

[1] Department of Biological Sciences, Brock University, St. Catharines, Ontario L2S 3A1, Canada

关键词: Cytochrome oxidase;    Proteoliposome;    N;    N;    N′;    N′-Tetramethyl-p-phenylenediamine;    Cytochrome c;    Fatty acid;    COV;    cytochrome-c oxidase reconstituted proteoliposomes;    c-loaded COV;    COV containing entrapped cytochrome c;    TMPD;    N;    N;    N′;    N′-tetramethyl-p-phenylenediamine;    DAD;    2;    3;    5;    6-tetramethyl-p-phenylenediamine;    PMS;    phenazine methosulphate;    FCCP;    carbonylcyanide p-trifluoromethoxyphenylhydrazone;   

DOI  :  10.1016/0014-5793(87)80527-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cytochrome-c oxidase proteoliposomes containing internally trapped cytochrome c can turn over on internal or external cytochrome c. At low TMPD levels the internal activity is significantly lower than the external activity as the functional internal cytochrome c is not fully reduced in the steady state. Increasing TMPD concentration increases the internal rate to equal that of the external enzyme. Internal activity results in the accumulation of TMPD⁺. Valinomycin increases this accumulation and subsequently FCCP decreases it. In the presence of excess external cytochrome c, the effects of these ionophores are reversed. The internally-facing enzyme is thus capable of generating a ΔμH⁺ in proteoliposomes as well as in submitochondrial particles.

【 授权许可】

Unknown