4.5 Article

Interactions of the Escherichia coli hydrogenase biosynthetic proteins:: HybG complex formation

期刊

FEBS LETTERS
卷 580, 期 2, 页码 677-681

出版社

WILEY
DOI: 10.1016/j.febslet.2005.12.063

关键词

hydrogenase; metallocenter assembly; accessory protein interactions; nickel

向作者/读者索取更多资源

Assembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway and the coordinated activity of many accessory proteins. To analyze complex formation between these factors in Escherichia coli, they were genomically tagged and native multi-protein complexes were isolated. This method validated multiple interactions reported in separate studies from several organisms and defined a new complex containing the putative chaperone HybG and the large subunit of hydrogenase 1 or 2. The complex also includes HypE and HypD, which interact with each other before joining the larger complex. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier 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