Catalytic robustness and torque generation of the F1-ATPase

被引:38
|
作者
Noji H. [1 ]
Ueno H. [1 ]
McMillan D.G.G. [1 ]
机构
[1] Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, Tokyo
基金
日本学术振兴会; 日本科学技术振兴机构;
关键词
ATP synthase; F[!sub]1[!/sub]-ATPase; Molecular motor; Single-molecule techniques;
D O I
10.1007/s12551-017-0262-x
中图分类号
学科分类号
摘要
The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines. © 2017, The Author(s).
引用
收藏
页码:103 / 118
页数:15
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