Britt R David, Rao Guodong, Tao Lizhi
Department of Chemistry, University of California, Davis, Davis, CA, USA.
Nat Rev Chem. 2020 Oct;4(10):542-549. Epub 2020 Jul 22.
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 H. 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.
自然界利用多核金属簇催化许多重要的多电子氧化还原反应。在催化过程中使用复杂铁硫簇的例子包括固氮酶的铁钼辅因子（FeMoco）及其钒和全铁变体，以及[FeFe]和[NiFe]氢化酶。本综述首先聚焦于[FeFe]氢化酶的催化H簇，它在产生分子氢方面具有很高的活性。最近在表征该酶催化的H簇组装方面取得了很大进展，包括从光谱学以及结合使用化学合成对该簇进行体外同位素标记所获得的信息。然后，我们将从H簇生物合成中学到的经验与关于[NiFe]氢化酶双核活性位点和固氮酶活性位点簇FeMoco生物组装的已知信息进行比较。
