The rotary binding change mechanism of ATP synthases

被引：59

作者：

Cross, RL ^{[1
]}

机构：

[1] SUNY Hlth Sci Ctr, Dept Biochem & Mol Biol, Syracuse, NY 13210 USA

来源：

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

关键词：

F0F1 ATP synthase; binding change mechanism; rotational catalysis; oxidative phosphorylation;

D O I：

10.1016/S0005-2728(00)00079-7

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 F0F1 ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F-0 drives the binding changes in F-1 that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：270 / 275

页数：6

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