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https://hdl.handle.net/2440/65883
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Type: | Journal article |
Title: | Structure of the active site of sulfite dehydrogenase from Starkeya novella |
Author: | Doonan, C. Kappler, U. George, G. |
Citation: | Inorganic Chemistry: including bioinorganic chemistry, 2006; 45(18):7488-7492 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2006 |
ISSN: | 0020-1669 1520-510X |
Statement of Responsibility: | Christian J. Doonan, Ulrike Kappler and Graham N. George |
Abstract: | In this paper, we report the results of molybdenum K-edge X-ray absorption studies performed on the oxidized and reduced active sites of the sulfite dehydrogenase from Starkeya novella. Our results provide the first direct structural information on the active site of the oxidized form of this enzyme and confirm the conclusions derived from protein crystallography that the molybdenum coordination is analogous to that of the sulfite oxidases. The molybdenum atom of the oxidized enzyme is bound by two Mo=O ligands at 1.73 A and three thiolate Mo-S ligands at 2.42 A, whereas the reduced enzyme has one oxo at 1.74 A, one long oxygen at 2.19 A (characteristic of Mo-OH2), and three Mo-S ligands at 2.40 A. |
Keywords: | Alphaproteobacteria Molybdenum Ligands Spectrum Analysis Electron Spin Resonance Spectroscopy Sensitivity and Specificity Binding Sites Molecular Structure Oxidation-Reduction X-Rays Sulfite Dehydrogenase |
Rights: | Copyright © 2006 American Chemical Society |
DOI: | 10.1021/ic0607944 |
Published version: | http://dx.doi.org/10.1021/ic0607944 |
Appears in Collections: | Aurora harvest 5 Chemistry and Physics publications Environment Institute publications |
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