The allosteric ATP-inhibition of cytochrome c oxidase activity is reversibly switched on by cAMP-dependent phosphorylation

被引：158

作者：

Bender, E ^{[1
]}

Kadenbach, B ^{[1
]}

机构：

[1] Univ Marburg, Fachbereich Chem, D-35032 Marburg, Germany

来源：

FEBS LETTERS | 2000年 / 466卷 / 01期

关键词：

cytochrome c oxidase; cAMP-dependent phosphorylation; respiratory control; allosteric effector; protein kinase A; Ca2+-activated protein phosphatase;

D O I：

10.1016/S0014-5793(99)01773-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In previous studies the allosteric inhibition of cytochrome c oxidase at high intramitochondrial ATP/ADP-ratios via binding of the nucleotides to the matrix domain of subunit IV was demonstrated. Here me show that the allosteric ATP-inhibition of the isolated bovine heart enzyme is switched on by cAMP-dependent phosphorylation with protein kinase A of subunits II (and/or III) and Vb, and switched off by subsequent incubation with protein phosphatase 1. It is suggested that after cAMP-dependent phosphorylation of cytochrome c oxidase mitochondrial respiration is controlled by the ATP/ADP-ratio keeping the proton motive force Delta p low, and the efficiency of energy transduction high. After Ca2+-induced dephosphorylation this control is lost, accompanied by increase of Delta p, slip of proton pumping (decreased H(+/)e(-) stoichiometry), and increase of the rate of respiration and ATP-synthesis at a decreased efficiency of energy transduction. (C) 2000 Federation of European Biochemical Societies.

引用

页码：130 / 134

页数：5

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