title: Asymmetric thiosulfinations catalyzed by bovine serum albumin and horseradish peroxidase.
abstract: Bovine serum albumin (BSA) and horseradish peroxidase (HRP) catalyzed the monooxidation of organic disulfides with peroxides to optically active thiosulfinates. With BSA, a hydrophobic disulfide was oxidized in a stereoselective manner, and the nature of the oxidant (H2O2 or tert-butyl hydroperoxide) controlled the absolute configuration of the product. The rates of HRP-catalyzed thiosulfination in methanol were several times faster than in water but the enzyme was less stereoselective.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Sergei V
authors.initials: SV
authors.lastname: Dzyuba
authors.forename: Alexander M
authors.initials: AM
authors.lastname: Klibanov
mesh_terms: D000818:Animals; D002384:Catalysis; D002417:Cattle; D004220:Disulfides / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D010084:Oxidation-Reduction; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013237:Stereoisomerism; D013886:Thiosulfonic Acids / Q000138:chemical synthesis*; D014867:Water / Q000737:chemistry*; D020122:tert-Butylhydroperoxide / Q000737:chemistry*
chemical_list: D004220:Disulfides; D013886:Thiosulfonic Acids; D014867:Water; D012710:Serum Albumin, Bovine; D020122:tert-Butylhydroperoxide; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase