期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 11, 期 1, 页码 41-51出版社
SPRINGER
DOI: 10.1007/s00775-005-0048-7
关键词
electron-nuclear double resonance; hydrogenase; single crystal
The catalytic center of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F in the oxidized states was investigated by electron paramagnetic resonance and electron-nuclear double resonance spectroscopy applied to single crystals of the enzyme. The experimental results were compared with density functional theory (DFT) calculations. For the Ni-B state, three hyperfine tensors could be determined. Two tensors have large isotropic hyperfine coupling constants and are assigned to the beta-CH2 protons of the Cys-549 that provides one of the bridging sulfur ligands between Ni and Fe in the active center. From a comparison of the orientation of the third hyperfine tensor with the tensor obtained from DFT calculations an OH- bridging ligand has been identified in the Ni-B state. For the Ni-A state broader signals were observed. The signals of the third proton, as observed for the ready state Ni-B, were not observed at the same spectral position for Ni-A, confirming a structural difference involving the bridging ligand in the unready state of the enzyme.
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