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Issue 9, 2011
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Reductive biotransformation of nitroalkenesvianitroso-intermediates to oxazetes catalyzed by xenobiotic reductase A (XenA)

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Abstract

A novel reductive biotransformation pathway for β,β-disubstituted nitroalkenes catalyzed by flavoproteins from the Old Yellow Enzyme (OYE) family was elucidated. It was shown to proceed via enzymatic reduction of the nitro-moiety to furnish the corresponding nitroso-alkene, which underwent spontaneous (non-enzymatic) electrocyclization to form highly strained 1,2-oxazete derivatives. At elevated temperatures the latter lost HCN via a retro-[2 + 2]-cycloaddition to form the corresponding ketones. This pathway was particularly dominant using xenobiotic reductase A, while pentaerythritol tetranitrate-reductase predominantly catalyzed the biodegradation via the Nef-pathway.

Graphical abstract: Reductive biotransformation of nitroalkenes via nitroso-intermediates to oxazetes catalyzed by xenobiotic reductase A (XenA)

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Supplementary files

Article information


Submitted
22 Nov 2010
Accepted
21 Feb 2011
First published
22 Feb 2011

Org. Biomol. Chem., 2011,9, 3364-3369
Article type
Paper

Reductive biotransformation of nitroalkenes via nitroso-intermediates to oxazetes catalyzed by xenobiotic reductase A (XenA)

K. Durchschein, W. M. F. Fabian, P. Macheroux, K. Zangger, G. Trimmel and K. Faber, Org. Biomol. Chem., 2011, 9, 3364
DOI: 10.1039/C0OB01216E

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