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
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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