Transmembrane proton translocation by cytochrome c oxidase

被引:102
作者
Branden, Gisela
Gennis, Robert B. [1 ]
Brzezinski, Peter
机构
[1] Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs Nat Sci, SE-10691 Stockholm, Sweden
[2] Univ Illinois, Sch Chem Sci, Urbana, IL 61801 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2006年 / 1757卷 / 08期
关键词
cytochrome aa(3); quinol oxidase; electron transfer; proton transfer; electrochemical proton gradient;
D O I
10.1016/j.bbabio.2006.05.020
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
Respiratory heme-copper oxidases are integral membrane proteins that catalyze the reduction of molecular oxygen to water using electrons donated by either quinol (quinol oxidases) or cytochrome c (cytochrome c oxidases, CcOs). Even though the X-ray crystal structures of several heme-copper oxidases and results from functional studies have provided significant insights into the mechanisms of O-2-reduction and, electron and proton transfer, the design of the proton-pumping machinery is not known. Here, we summarize the current knowledge on the identity of the structural elements involved in proton transfer in CcO. Furthermore, we discuss the order and timing of electron-transfer reactions in CcO during 02 reduction and how these reactions might be energetically coupled to proton pumping across the membrane. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1052 / 1063
页数:12
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