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https://hdl.handle.net/2440/47130
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Type: | Journal article |
Title: | Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase |
Author: | George, G. Nelson, K. Harris, H. Doonan, C. Rajagopalan, K. |
Citation: | Inorganic Chemistry: including bioinorganic chemistry, 2007; 46(8):3097-3104 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2007 |
ISSN: | 0020-1669 1520-510X |
Statement of Responsibility: | Graham N. George , Kimberly Johnson Nelson , Hugh H. Harris , Christian J. Doonan , and K. V. Rajagopalan |
Abstract: | We report a structural characterization using X-ray absorption spectroscopy of Rhodobacter sphaeroides dimethylsulfoxide (DMSO) reductase reduced with trimethylarsine, and show that this is structurally analogous to the physiologically relevant dimethylsulfide-reduced DMSO reductase. Our data unambiguously indicate that these species should be regarded as formal MoIV species, and indicate a classical coordination complex of trimethylarsine oxide, with no special structural distortions. The similarity of the trimethylarsine and dimethylsulfide complexes suggests in turn that the dimethylsulfide reduced enzyme possesses a classical coordination of DMSO with no special elongation of the S—O bond, as previously suggested. |
Keywords: | Rhodobacter sphaeroides Arsenicals Oxidoreductases Iron-Sulfur Proteins Spectrum Analysis Sensitivity and Specificity Binding Sites Structure-Activity Relationship X-Rays Models, Chemical Models, Molecular |
Description: | Copyright © 2007 American Chemical Society |
DOI: | 10.1021/ic0619052 |
Published version: | http://pubs.acs.org/cgi-bin/abstract.cgi/inocaj/2007/46/i08/abs/ic0619052.html |
Appears in Collections: | Aurora harvest 6 Chemistry and Physics publications Environment Institute publications |
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