Asymmetric thiosulfinations catalyzed by bovine serum albumin and horseradish peroxidase.
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.
Dzyuba
Sergei V
SV
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Klibanov
Alexander M
AM
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*
D004220:Disulfides; D013886:Thiosulfonic Acids; D014867:Water; D012710:Serum Albumin, Bovine; D020122:tert-Butylhydroperoxide; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase