Please use this identifier to cite or link to this item: http://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, 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
RMID: 0020081340
DOI: 10.1021/ic0619052
Published version: http://pubs.acs.org/cgi-bin/abstract.cgi/inocaj/2007/46/i08/abs/ic0619052.html
Appears in Collections:Chemistry and Physics publications
Environment Institute publications

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