Observations concerning the quinol oxidation site of the cytochrome bc1 complex

被引：58

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.

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页码：13 / 20

页数：8

相关论文

共 38 条

[1] Structure and function of cytochrome bc complexes [J].

Berry, EA ;

Guergova-Kuras, M ;

Huang, LS ;

Crofts, AR .

ANNUAL REVIEW OF BIOCHEMISTRY, 2000, 69 :1005-1075

[2]

BOWYER JR, 1982, J BIOL CHEM, V257, P8321

[3] ELECTRON-SPIN ECHO ENVELOPE MODULATION SPECTROSCOPY SUPPORTS THE SUGGESTED COORDINATION OF 2 HISTIDINE LIGANDS TO THE RIESKE FE-S CENTERS OF THE CYTOCHROME-B6F COMPLEX OF SPINACH AND THE CYTOCHROME-BC1 COMPLEXES OF RHODOSPIRILLUM-RUBRUM, RHODOBACTER-SPHAEROIDES R-26, AND BOVINE HEART-MITOCHONDRIA [J].

BRITT, RD ;

SAUER, K ;

KLEIN, MP ;

KNAFF, DB ;

KRIAUCIUNAS, A ;

YU, CA ;

YU, L ;

MALKIN, R .

BIOCHEMISTRY, 1991, 30 (07) :1892-1901

[4] A spectroscopic method for observing the domain movement of the Rieske iron-sulfur protein [J].

Brugna, M ;

Rodgers, S ;

Schricker, A ;

Montoya, G ;

Kazmeier, M ;

Nitschke, W ;

Sinning, I .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (05) :2069-2074

[5] INTERACTION OF 2,5-DIBROMO-3-METHYL-6-ISOPROPYLBENZOQUINONE (DBMIB) WITH BOUND ELECTRON CARRIERS IN SPINACH-CHLOROPLASTS [J].

CHAIN, RK ;

MALKIN, R .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1979, 197 (01) :52-56

[6] LOW-BARRIER HYDROGEN-BONDS AND ENZYMATIC CATALYSIS [J].

CLELAND, WW ;

KREEVOY, MM .

SCIENCE, 1994, 264 (5167) :1887-1890

[7] Physicochemical aspects of the movement of the rieske iron sulfur protein during quinol oxidation by the bc1 complex from mitochondria and photosynthetic bacteria [J].

Crofts, AR ;

Hong, SJ ;

Zhang, ZL ;

Berry, EA .

BIOCHEMISTRY, 1999, 38 (48) :15827-15839

[8] Interactions of quinone with the iron-sulfur protein of the bc1 complex:: is the mechanism spring-loaded? [J].

Crofts, AR ;

Shinkarev, VP ;

Dikanov, SA ;

Samoilova, RI ;

Kolling, D .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2002, 1555 (1-3) :48-53

[9] HOW RAPID ARE THE INTERNAL REACTIONS OF THE UBIQUINOL-CYTOCHROME-C2 OXIDOREDUCTASE [J].

CROFTS, AR ;

WANG, ZG .

PHOTOSYNTHESIS RESEARCH, 1989, 22 (01) :69-87

[10] Uncovering the [2Fe2S] domain movement in cytochrome bc1 and its implications for energy conversion [J].

Darrouzet, E ;

Valkova-Valchanova, M ;

Moser, CC ;

Dutton, PL ;

Daldal, F .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (09) :4567-4572

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