期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 17, 页码 13532-13540出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R111.310797
关键词
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资金
- Agence Nationale de la Recherche [ANR-08-BLAN-0224-01]
- Commissariat a l'Energie Atomique et aux Energies Alternatives
- CNRS
- Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0224] Funding Source: Agence Nationale de la Recherche (ANR)
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.
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