期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 13, 页码 4533-4540出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja711187e
关键词
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资金
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [0755676] Funding Source: National Science Foundation
An X-ray crystallographic refinement of the H-cluster of [FeFe]-hydrogenase from Clostridium pasteurianum has been carried out to close-to atomic resolution and is the highest resolution [FeFe]-hydrogenase presented to date. The 1.39 angstrom, anisotropically refined [FeFe]-hydrogenase structure provides a basis for examining the outstanding issue of the composition of the unique nonprotein dithiolate ligand of the H-cluster. In addition to influencing the electronic structure of the H-cluster, the composition of the ligand has mechanistic implications due to the potential of the bridge-head gamma-group participating in proton transfer during catalysis. In this work, sequential density functional theory optimizations of the dithiolate ligand embedded in a 3.5-3.9 angstrom protein environment provide an unbiased approach to examining the most likely composition of the ligand. Structural, conformational, and energetic considerations indicate a preference for dithiomethylether as an H-cluster ligand and strongly disfavor the dithiomethylammonium as a catalytic base for hydrogen production.
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