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.

大自然使用多核金属簇来催化许多重要的多电子氧化还原反应。在催化中采用复杂的Fe-S簇的例子包括固氮酶的Fe-Mo辅因子（FeMoco）及其V和全Fe变体，以及[FeFe]和[NiFe]氢化酶。该观点开始于[FeFe]氢化酶的催化H簇，该簇在产生分子H _2方面非常活跃。在表征H簇的酶催化组装方面已有许多新进展，包括从光谱学中收集的信息以及使用化学合成方法对该簇的体外同位素标记。然后，我们将从H簇生物合成中吸取的教训与[NiFe]氢化酶双核活性位点和固氮酶活性位点簇FeMoco的生物组装知识相比较。