title: Enantioselective deoxygenation of alkyl aryl sulfoxides by DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans.
abstract: 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.
authors.affiliation: Department of Applied Biological Chemistry, University of Tokyo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Abo
authors.forename: M
authors.initials: M
authors.lastname: Tachibana
authors.forename: A
authors.initials: A
authors.lastname: Okubo
authors.forename: S
authors.initials: S
authors.lastname: Yamazaki
mesh_terms: 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*
chemical_list: D007506:Iron-Sulfur Proteins; D013454:Sulfoxides; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase