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Significance [FeFe]-hydrogenases catalyze H2 evolution at extraordinary rates at low overpotential using base metal (not platinum). In the field of renewable energy, the biosynthesis of these enzymes’ active sites, the H-cluster, is of intense interest. Among its many cofactors, the azadithiolate is unique, and its biosynthesis remains enigmatic. Three Fe–S proteins, HydE, HydF, and HydG, are essential for the H-cluster bioassembly. This paper describes an in vitro assembly approach where a synthetic [Fe(cysteine)(CO)2 (CN)] complex, “syn-B,” allows HydG-free biosynthesis of the active enzyme. Using isotopic and S/Se labeling, syn-B is shown to contribute Fe(CO)2 (CN)S to the biosynthesis. This work sets the stage for further investigation of the H-cluster bioassembly.

The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO) 2 (CN)] organometallic precursor

The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO) ₂ (CN)] organometallic precursor