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|Title:||Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase|
|Citation:||Inorganic Chemistry, 2007; 46(8):3097-3104|
|Publisher:||Amer Chemical Soc|
|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|
|Appears in Collections:||Chemistry and Physics publications|
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