Notes on the mechanism of ATP synthesis

被引：16

作者：

Bianchet, MA

Pedersen, PL

Amzel, LM ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA

[2] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA

来源：

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 2000年 / 32卷 / 05期

关键词：

F-1-ATPase; ATP synthesis; conformational changes;

D O I：

10.1023/A:1005673209883

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and P-i assumes that all states of the FI portion of the ATP synthase have beta subunits in "tight," " loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional beta subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

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页码：517 / 521

页数：5

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