Enantioselective deoxygenation of alkyl aryl sulfoxides by DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans.
The substrate specificity and enantioselectivity of DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans were studied on a series of alkyl aryl sulfoxides as substrate. The enzyme was found to catalyze deoxygenation of (S)-sulfoxides predominantly. (R)-Sulfoxides were recovered with a high enantiomeric excess.
Abo
M
M
Department of Applied Biological Chemistry, University of Tokyo, Japan.
Tachibana
M
M
Okubo
A
A
Yamazaki
S
S
D007506:Iron-Sulfur Proteins; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013454:Sulfoxides / Q000378:metabolism*
D007506:Iron-Sulfur Proteins; D013454:Sulfoxides; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase