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

Org Biomol Chem. 2011 May 7;9(9):3364-9. doi: 10.1039/c0ob01216e. Epub 2011 Mar 15.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkenes / chemistry*
  • Alkenes / metabolism
  • Azetidines / chemistry*
  • Bacterial Proteins / metabolism*
  • Biocatalysis*
  • Flavoproteins / metabolism*
  • Molecular Structure
  • Nitro Compounds / chemistry*
  • Nitro Compounds / metabolism
  • Nitroso Compounds / chemistry*
  • Nitroso Compounds / metabolism
  • Oxidation-Reduction
  • Oxidoreductases / metabolism*
  • Pseudomonas putida / enzymology*

Substances

  • Alkenes
  • Azetidines
  • Bacterial Proteins
  • Flavoproteins
  • Nitro Compounds
  • Nitroso Compounds
  • XenA protein, Pseudomonas putida
  • Oxidoreductases