Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita

FEBS Lett. 2008 Dec 10;582(29):4100-6. doi: 10.1016/j.febslet.2008.11.006. Epub 2008 Nov 18.


Agrocybe aegerita peroxidase (AaP) is a versatile extracellular biocatalyst that can oxygenate aromatic compounds. Here, we report on the selective oxidation of pyridine (PY) yielding pyridine N-oxide as sole product. Using H(2)(18)O(2) as co-substrate, the origin of oxygen was confirmed to be the peroxide. Therefore, AaP can be regarded as a true peroxygenase transferring one oxygen atom from peroxide to the substrate. To our best knowledge, there are only two types of enzymes oxidizing PY at the nitrogen: bacterial methane monooxygenase and a few P450 monooxygenases. AaP is the first extracellular enzyme and the first peroxidase that catalyzes this reaction, and it converted also substituted PYs into the corresponding N-oxides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agrocybe / enzymology*
  • Catalysis
  • Hydrocarbons, Aromatic / metabolism*
  • Hydrogen Peroxide / metabolism
  • Mixed Function Oxygenases / metabolism*
  • Oxidation-Reduction
  • Oxygen / metabolism*
  • Pyridines / metabolism*
  • Substrate Specificity


  • Hydrocarbons, Aromatic
  • Pyridines
  • Hydrogen Peroxide
  • Mixed Function Oxygenases
  • peroxygenase
  • pyridine
  • Oxygen