期刊
FEBS LETTERS
卷 494, 期 1-2, 页码 1-5出版社
WILEY
DOI: 10.1016/S0014-5793(01)02300-6
关键词
ATP synthase; subunit c; proton stoichiometry; sequence alignment
In recent years, structural information on the Fl sector of the ATP synthase has provided an insight into the molecular mechanism of ATP catalysis, The structure strongly supports the proposal that the ATP synthase works as a rotary molecular motor. Insights into the membrane domain have just started to emerge but more detailed structural information is needed if the molecular mechanism of proton translocation coupled to ATP synthesis is to be understood. This review will focus mainly on the ion translocating rotor in the membrane domain of the F-type ATPase, and the related vacuolar and archaeal relatives. (C) 2001 Published by Elsevier Science B,V, on behalf of the Federation of European Biochemical Societies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据