期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 13, 期 36, 页码 16146-16149出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1cp21045a
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资金
- DFG (Cluster of Excellence UniCat'')
Structural models for the Ni-B state of the wild-type and C81S protein variant of the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha H16 were derived by applying the homology model technique combined with molecular simulations and a hybrid quantum mechanical/molecular mechanical approach. The active site structure was assessed by comparing calculated and experimental IR spectra, confirming the view that the active site structure is very similar to those of anaerobic standard hydrogenases. In addition, the data suggest the presence of a water molecule in the second coordination sphere of the active centre.
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