A Single-crystal Endor and Density Functional Theory Study of the Oxidized States of the [Nife] Hydrogenase from Desulfovibrio Vulgaris Miyazaki F.
From: Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
- Publish Date: Jan 2006
- ISSN: 0949-8257
- Volume: 11
- Issue: 1
- Pages: 41-51
- Medium: Print
- Language: English
- Citation (JAMA): van Gastel Maurice, Stein Matthias, Brecht Marc, et al. A Single-crystal Endor and Density Functional Theory Study of the Oxidized States of the [Nife] Hydrogenase from Desulfovibrio Vulgaris Miyazaki F.. J. Biol. Inorg. Chem. Jan 2006;11:41-51
Abstract
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.
Mesh Headings (Keywords): Binding Sites, Crystallization, Cysteine, Desulfovibrio vulgaris, Electron Spin Resonance Spectroscopy, Hydrogenase, Ligands, Oxidation-Reduction, Protein Conformation, Protons, Sulfur
Check for Full Text / PubMed Unique Identifier (PMID): 16292669
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