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
收藏
页码：270 / 275
页数：6
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