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 dimethyl sulfoxide (DMSO) reductase reduced with trimethylarsine and show that this is structurally analogous to the physiologically relevant dimethyl sulfide 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 dimethyl sulfide complexes suggests, in turn, that the dimethyl sulfide reduced enzyme possesses a classical coordination of DMSO with no special elongation of the S-O bond, as previously suggested.
George
Graham N
GN
Department of Geological Sciences, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada. g.george@usask.ca
Nelson
Kimberly Johnson
KJ
Harris
Hugh H
HH
Doonan
Christian J
CJ
Rajagopalan
K V
KV
D001152:Arsenicals / Q000737:chemistry*; D001665:Binding Sites; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D012680:Sensitivity and Specificity; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship; D014965:X-Rays
D001152:Arsenicals; D007506:Iron-Sulfur Proteins; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase; C009572:trimethylarsine