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- W2009080760 abstract "Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen. Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen." @default.
- W2009080760 created "2016-06-24" @default.
- W2009080760 creator A5015990767 @default.
- W2009080760 creator A5030590912 @default.
- W2009080760 date "2012-04-01" @default.
- W2009080760 modified "2023-09-30" @default.
- W2009080760 title "Structure-Function Relationships in [FeFe]-Hydrogenase Active Site Maturation" @default.
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- W2009080760 doi "https://doi.org/10.1074/jbc.r111.310797" @default.
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