4.5 Review

The ε subunit of bacterial and chloroplast F1F0 ATPases -: Structure, arrangement, and role of the ε subunit in energy coupling within the complex

期刊

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1458, 期 2-3, 页码 263-269

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/S0005-2728(00)00078-5

关键词

F1F0 ATPase; epsilon subunit; rotary motor; cross linking

资金

  1. NHLBI NIH HHS [HL 24526] Funding Source: Medline

向作者/读者索取更多资源

Recent studies show that the epsilon subunit of bacterial and chloroplast F1F0 ATPases is a component of the central stalk that links the F-1 and F-0 parts. This subunit interacts with alpha, beta and gamma subunits of F-1 and the c subunit ring of F-0. Along with the gamma subunit, epsilon is a part of the rotor that couples events at the three catalytic sites sequentially with proton translocation through the F-0 part. Structural data on the epsilon subunit when separated from the complex and in situ are reviewed, and the functioning of this polypeptide in coupling within the ATP synthase is considered. (C) 2000 Elsevier Science B.V. All rights reserved.

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。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据