Jump to main content
Jump to site search

Issue 9, 2011
Previous Article Next Article

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

Author affiliations

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)

Back to tab navigation

Supplementary files

Publication details

The article was received on 22 Nov 2010, accepted on 21 Feb 2011 and first published on 22 Feb 2011


Article type: Paper
DOI: 10.1039/C0OB01216E
Citation: Org. Biomol. Chem., 2011,9, 3364-3369
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements