期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 19, 期 6, 页码 747-757出版社
SPRINGER
DOI: 10.1007/s00775-014-1168-8
关键词
Hydrogenase; Radical SAM; Metal cluster assembly; HydE; HydG; HydF; Carbon monoxide; Cyanide
The organometallic H-cluster at the active site of the [FeFe]-hydrogenase serves as the site of reversible binding and reduction of protons to produce H-2. The H-cluster is unique in biology, and consists of a 2Fe subcluster tethered to a typical [4Fe-4S] cluster by a single cysteine ligand. The remaining ligands to the 2Fe subcluster include three carbon monoxides, two cyanides, and a dithiomethylamine. This mini-review will focus on the significant advances in recent years in understanding the pathway for H-cluster biosynthesis, as well as the structures, roles, and mechanisms of the three enzymes directly involved.
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