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Title: Interaction of Product Analogues With the Active Site of Rhodobacter Sphaeroides Dimethyl Sulfoxide Reductase

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.
Authors:
; ; ; ; ;
Publication Date:
OSTI Identifier:
909800
Report Number(s):
SLAC-REPRINT-2007-094
Journal ID: ISSN 0020-1669; INOCAJ; TRN: US200723%%193
DOE Contract Number:
AC02-76SF00515
Resource Type:
Journal Article
Resource Relation:
Journal Name: Inorg. Chem 46:3097,2007; Journal Volume: 46
Research Org:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ABSORPTION SPECTROSCOPY; DIMETHYL SULFIDE; DMSO; ELONGATION; ENZYMES; OXIDOREDUCTASES Other,OTHER