Observations concerning the quinol oxidation site of the cytochrome bc1 complex

被引：57

作者：

Berry, EA ^{[1
]}

Huang, LS ^{[1
]}

机构：

[1] Lawrence Berkeley Lab, Berkeley, CA 94720 USA

来源：

FEBS LETTERS | 2003年 / 555卷 / 01期

关键词：

ubiquinone; cytochrome c; oxidoreductase; membrane protein complex; respiratory enzyme; protein crystal; X-ray; structure; mechanism; tautomerisrn; resonance;

D O I：

10.1016/S0014-5793(03)01099-8

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 direct hydrogen bond between ubiquinone/quinol bound at the Q(O) site and a cluster-ligand histidine of the iron-sulfur protein (ISP) is described as a major determining factor explaining much experimental data on position of the ISP ectodomain, electron paramagnetic resonance (EPR) lineshape and midpoint potential of the iron-sulfur cluster, and the mechanism of the bifurcated electron transfer from ubiquinol to the high and low potential chains of the be, complex. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：13 / 20

页数：8

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