Synthase (H+ ATPase):: coupling between catalysis, mechanical work, and proton translocation

被引：39

作者：

Futai, M ^{[1
]}

Omote, H ^{[1
]}

Sambongi, Y ^{[1
]}

Wada, Y ^{[1
]}

机构：

[1] Osaka Univ, Inst Sci & Ind Res, Div Biol Sci, Japan Sci & Technol Corp,CREST, Osaka 5670047, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2000年 / 1458卷 / 2-3期

关键词：

F0F1; catalytic site; ATP synthesis; proton transport; HC ATPase; rotational catalysis;

D O I：

10.1016/S0005-2728(00)00080-3

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：

Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the beta subunit of F-1 sector and roles of the gamma subunit in energy coupling. The gamma-subunit rotation during catalysis is also discussed. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

收藏

页码：276 / 288

页数：13

相关论文

共 73 条

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].

ABRAHAMS, JP ;

LESLIE, AGW ;

LUTTER, R ;

WALKER, JE .

NATURE, 1994, 370 (6491) :621-628

[2]

AGGELER R, 1993, J BIOL CHEM, V268, P20831

[3] DISULFIDE BOND FORMATION BETWEEN THE COOH-TERMINAL DOMAIN OF THE BETA-SUBUNITS AND THE GAMMA-SUBUNITS AND EPSILON-SUBUNITS OF THE ESCHERICHIA-COLI F1-ATPASE - STRUCTURAL IMPLICATIONS AND FUNCTIONAL CONSEQUENCES [J].

AGGELER, R ;

HAUGHTON, MA ;

CAPALDI, RA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (16) :9185-9191

[4]

AlShawi MK, 1997, J BIOL CHEM, V272, P2300

[5] Mechanism of energy coupling in the F0F1-ATP synthase: The uncoupling mutation, gamma M23K, disrupts the use of binding energy to drive catalysis [J].

AlShawi, MK ;

Nakamoto, RK .

BIOCHEMISTRY, 1997, 36 (42) :12954-12960

[6] The Escherichia coli F0F1 gamma M23K uncoupling mutant has a higher K-0.5 for P-i. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway [J].

AlShawi, MK ;

Ketchum, CJ ;

Nakamoto, RK .

BIOCHEMISTRY, 1997, 36 (42) :12961-12969

[7]

BIRKENHAGER R, 1995, EUR J BIOCHEM, V230, P58, DOI 10.1111/j.1432-1033.1995.0058i.x

[8]

Boyer P.D., 1979, MEMBRANE BIOENERGETI, P461

[9] The ATP synthase - A splendid molecular machine [J].

Boyer, PD .

ANNUAL REVIEW OF BIOCHEMISTRY, 1997, 66 :717-749

[10] ADENINE-NUCLEOTIDE BINDING-SITES ON BEEF-HEART F1 ATPASE - PHOTOAFFINITY-LABELING OF BETA-SUBUNIT TYR-368 AT A NONCATALYTIC SITE AND BETA-TYR-345 AT A CATALYTIC SITE [J].

CROSS, RL ;

CUNNINGHAM, D ;

MILLER, CG ;

XUE, ZX ;

ZHOU, JM ;

BOYER, PD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (16) :5715-5719

← 1 2 3 4 5 6 7 8 →