Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases.
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.
Mueller
Nicole Jasmin
NJ
Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, Austria.
Stueckler
Clemens
C
Hall
Melanie
M
Macheroux
Peter
P
Faber
Kurt
K
D001412:Bacillus subtilis / Q000201:enzymology; D004852:Epoxy Compounds / Q000737:chemistry / Q000378:metabolism*; D038181:FMN Reductase / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013237:Stereoisomerism; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*; D013440:Sulfides / Q000737:chemistry / Q000378:metabolism*
D004852:Epoxy Compounds; D013438:Sulfhydryl Compounds; D013440:Sulfides; D038181:FMN Reductase