Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase
Date
2007
Authors
George, G.
Nelson, K.
Harris, H.
Doonan, C.
Rajagopalan, K.
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Advisors
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Journal article
Citation
Inorganic Chemistry: including bioinorganic chemistry, 2007; 46(8):3097-3104
Statement of Responsibility
Graham N. George , Kimberly Johnson Nelson , Hugh H. Harris , Christian J. Doonan , and K. V. Rajagopalan
Conference Name
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.
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Copyright © 2007 American Chemical Society