氢化酶
固氮酶
铁硫簇
活动站点
化学
星团(航天器)
催化作用
辅因子
酶
生物化学
组合化学
固氮
有机化学
计算机科学
程序设计语言
氮气
作者
R. David Britt,Guodong Rao,Lizhi Tao
标识
DOI:10.1038/s41570-020-0208-x
摘要
Nature uses multinuclear metal clusters to catalyse a number of important multielectron redox reactions. Examples that employ complex Fe-S clusters in catalysis include the Fe-Mo cofactor (FeMoco) of nitrogenase and its V and all-Fe variants, and the [FeFe] and [NiFe] hydrogenases. This Perspective begins with a focus on the catalytic H-cluster of [FeFe] hydrogenase, which is highly active in producing molecular H2. There has been much recent progress in characterizing the enzyme-catalysed assembly of the H-cluster, including information gleaned from spectroscopy combined with in vitro isotopic labelling of this cluster using chemical synthesis. We then compare the lessons learned from H-cluster biosynthesis to what is known about the bioassembly of the binuclear active site of [NiFe] hydrogenase and the nitrogenase active site cluster FeMoco.
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