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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Fast and selective reduction of nitroarenes under visible light with an earth-abundant plasmonic photocatalyst
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This work is funded by the National Institutes of Health (1R35GM126961 to R.D.B.).
The authors declare no competing interests.
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Britt, R.D., Rao, G. & Tao, L. Bioassembly of complex iron–sulfur enzymes: hydrogenases and nitrogenases. Nat Rev Chem 4, 542–549 (2020). https://doi.org/10.1038/s41570-020-0208-x
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