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Issue 6, 2009
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Epoxidation of conjugated C[double bond, length as m-dash]C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases

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Abstract

Three FMN-dependent oxidoreductases, YcnD and YhdA from Bacillus subtilis and Lot6p from Saccharomyces cerevisiae, oxidised α,β-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 O2, forming H2O2, which acted as oxidant in a spontaneous (non-enzymatic) fashion.

Graphical abstract: Epoxidation of conjugated C [[double bond, length as m-dash]] C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases

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Publication details

The article was received on 27 Oct 2008, accepted on 28 Nov 2008 and first published on 26 Jan 2009


Article type: Paper
DOI: 10.1039/B819057G
Citation: Org. Biomol. Chem., 2009,7, 1115-1119
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    Epoxidation of conjugated C[double bond, length as m-dash]C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases

    N. J. Mueller, C. Stueckler, M. Hall, P. Macheroux and K. Faber, Org. Biomol. Chem., 2009, 7, 1115
    DOI: 10.1039/B819057G

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