Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side

被引：11

作者：

Martino, Pietro Luca ^{[1
]}

Capitanio, Giuseppe ^{[1
]}

Capitanio, Nazzareno ^{[2
]}

Papa, Sergio ^{[1
,3
]}

机构：

[1] Univ Bari, Dept Med Biochem Biol & Phys, I-70124 Bari, Italy

[2] Univ Foggia, Dept Biomed Sci, Foggia, Italy

[3] CNR, Inst Bioenerget & Biomembranes, I-70126 Bari, Italy

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2011年 / 1807卷 / 09期

关键词：

Cytochrome c oxidase; Proton pumping; Redox Bohr effect; Allosteric cooperativity; Zinc inhibition; OXYGEN-REDUCTION SITE; HEME-COPPER OXIDASES; PARACOCCUS-DENITRIFICANS; ELECTRON-TRANSFER; CATALYTIC CYCLE; ENERGY TRANSDUCTION; TRANSLOCATION; STOICHIOMETRY; COMPLEXES; MECHANISM;

D O I：

10.1016/j.bbabio.2011.05.015

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：

A study is presented on the effect of zinc binding at the matrix side, on the proton pump of purified liposome reconstituted bovine heart cytochrome c oxidase (COV). Internally trapped Zn2+ resulted in 50% decoupling of the proton pump at level flow. Analysis of the pH dependence of inhibition by internal Zn2+ of proton release in the oxidative and reductive phases of the catalytic cycle of cytochrome c oxidase indicates that Zn2+ suppresses two of the four proton pumping steps in the cycle, those taking place when the 2 OH- produced in the reduction of O-2 at the binuclear center are protonated to 2 H2O. This decoupling effect could be associated with Zn2+ induced conformational alteration of an acid/base cluster linked to heme a(3). (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：1075 / 1082

页数：8

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