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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