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• W2974037107 abstract "The radical SAM enzyme HydG generates CO- and CN--containing Fe complexes that are involved in the bioassembly of the [FeFe] hydrogenase active cofactor, the H-cluster. HydG contains a unique 5Fe-4S cluster in which the fifth dangler Fe and the coordinating cysteine molecule have both been shown to be essential for its function. Here, we demonstrate that this dangler Fe can be replaced with Ni2+ or Co2+ and that the cysteine can be replaced with selenocysteine. The resulting HydG variants were characterized by electron paramagnetic resonance and X-ray absorption spectroscopy, as well as subjected to a Tyr cleavage assay. Both Ni2+ and Co2+ are shown to be exchange-coupled to the 4Fe-4S cluster, and selenocysteine substitution does not alter the electronic structure significantly. XAS data provide details of the coordination environments near the Ni, Co, and Se atoms and support a close interaction of the dangler metal with the FeS cluster via an asymmetric SeCys bridge. Finally, while we were unable to observe the formation of novel organometallic species for the Ni2+ and Co2+ variants, the selenocysteine variant retains the activity of wild type HydG in forming [Fe(CO)x(CN)y] species. Our results provide more insights into the unique auxiliary cluster in HydG and expand the scope of artificially generated Fe-S clusters with heteroatoms." @default.
• W2974037107 created "2019-09-26" @default.
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• W2974037107 date "2019-09-20" @default.
• W2974037107 modified "2023-10-17" @default.
• W2974037107 title "Incorporation of Ni²⁺, Co²⁺, and Selenocysteine into the Auxiliary Fe-S Cluster of the Radical SAM Enzyme HydG" @default.
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• W2974037107 doi "https://doi.org/10.1021/acs.inorgchem.9b01293" @default.
• W2974037107 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6984664" @default.
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