Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases

Org Biomol Chem. 2009 Mar 21;7(6):1115-9. doi: 10.1039/b819057g. Epub 2009 Jan 26.

Abstract

Three FMN-dependent oxidoreductases, YcnD and YhdA from Bacillus subtilis and Lot6p from Saccharomyces cerevisiae, oxidised alpha,beta-unsaturated carbonyl compounds and a thioether, respectively, to furnish the corresponding racemic epoxides or sulfoxide, respectively. The mechanism of this enzyme-mediated (rather than enzyme-catalysed) oxidation was shown to proceed via the NADH-dependent reduction of O(2), forming H(2)O(2), which acted as oxidant in a spontaneous (non-enzymatic) fashion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / enzymology
  • Epoxy Compounds / chemistry
  • Epoxy Compounds / metabolism*
  • FMN Reductase / metabolism*
  • Molecular Structure
  • Oxidation-Reduction
  • Saccharomyces cerevisiae / enzymology
  • Stereoisomerism
  • Sulfhydryl Compounds / chemistry
  • Sulfhydryl Compounds / metabolism*
  • Sulfides / chemistry
  • Sulfides / metabolism*

Substances

  • Epoxy Compounds
  • Sulfhydryl Compounds
  • Sulfides
  • FMN Reductase