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

被引：40

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

页码：276 / 288

页数：13

共 73 条

[71] ATP synthase's second stalk comes into focus [J].