Insights from the structure of the yeast cytochrome bc1 complex:: crystallization of membrane proteins with antibody fragments

被引:25
作者
Hunte, C [1 ]
机构
[1] Max Planck Inst Biophys, Abt Mol Membranbiol, D-60528 Frankfurt, Germany
来源
FEBS LETTERS | 2001年 / 504卷 / 03期
关键词
oxidoreductase; complex III; antibody fragment; crystallization; Q cycle; quinol;
D O I
10.1016/S0014-5793(01)02744-2
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
The ubiquinol:cytochrome c oxidoreductase (EC 1.20.2.2, QCR or cytochrome be, complex) is a component of respiratory and photosynthetic electron transfer chains in mitochondria and bacteria. The complex transfers electrons from quinol to cytochrome c. Electron transfer is coupled to proton translocation across the lipid bilayer, thereby generating an electrochemical proton gradient, which conserves the free energy of the redox reaction. The yeast complex was crystallized with antibody Fv fragments, a promising technique to obtain well-ordered crystals from membrane proteins. The high-resolution structure of the yeast protein reveals details of the catalytic sites of the complex, which are important for electron and proton transfer. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:126 / 132
页数:7
相关论文
共 44 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]   THE PROTONMOTIVE Q-CYCLE IN MITOCHONDRIA AND BACTERIA [J].
BRANDT, U ;
TRUMPOWER, B .
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1994, 29 (03) :165-197
[3]   A compilation of mutations located in the cytochrome b subunit of the bacterial and mitochondrial bc(1) complex [J].
Brasseur, G ;
Saribas, AS ;
Daldal, F .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1996, 1275 (1-2) :61-69
[4]   ARE THE CORE PROTEINS OF THE MITOCHONDRIAL BC(1) COMPLEX EVOLUTIONARY RELICS OF A PROCESSING PROTEASE [J].
BRAUN, HP ;
SCHMITZ, UK .
TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (05) :171-175
[5]   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
[6]   Mechanism of ubiquinol oxidation by the bc1 complex:: Different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors [J].
Crofts, AR ;
Barquera, B ;
Gennis, RB ;
Kuras, R ;
Guergova-Kuras, M ;
Berry, EA .
BIOCHEMISTRY, 1999, 38 (48) :15807-15826
[7]   Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria [J].
Crofts, AR ;
Berry, EA .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1998, 8 (04) :501-509
[8]   A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage [J].
Demartis, S ;
Huber, A ;
Viti, F ;
Lozzi, L ;
Giovannoni, L ;
Neri, P ;
Winter, G ;
Neri, D .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 286 (02) :617-633
[9]   Activation of a matrix processing peptidase from the crystalline cytochrome bc1 complex of bovine heart mitochondria [J].
Deng, KP ;
Zhang, L ;
Kachurin, AM ;
Yu, L ;
Xia, D ;
Kim, H ;
Deisenhofer, J ;
Yu, CA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (33) :20752-20757
[10]  
DEVRIES S, 1981, J BIOL CHEM, V256, P1996