[FeFe]-hydrogenase reduces hydrogen protons and produces diatomic hydrogen at a complex metallo-cofactor, known as the H-cluster. This H-cluster is comprised of a [4Fe-4S] cluster linked to a decorated 2Fe subcluster via a thiolate of a protein-derived cysteine ligand. This 2Fe subcluster is the location of proton reduction and includes biologically toxic carbon monoxide and cyanide ligands in addition to a bridging dithiomethylamine. The details of the assembly of this decorated 2Fe subcluster remain unresolved; however, four proteins have been deemed essential in the construction and housing of the H-cluster: HydA, HydE, HydF and HydG. HydA houses the H-cluster during catalysis. The carbon monoxide, cyanide, and bridging dithiomethylamine ligands are expected to be delivered by the radical SAM enzymes, HydE and HydG. HydF is expected to be a scaffold protein on which the 2Fe subcluster of the H-cluster is built prior to delivery to HydA. By examining the cluster content on the maturase HydF through biochemical analysis and various forms of spectroscopy, this study probes the construction of the decorated 2Fe subcluster.

Insights into the biochemical characterization of [FeFe]-hydrogenase Maturase HydF

249th National Meeting (2015)

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