Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita.
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.
Ullrich
René
R
Unit of Environmental Biotechnology, International Graduate School of Zittau, Markt 23, 02763 Zittau, Germany. ullrich@ihi-zittau.de
Dolge
Christoph
C
Kluge
Martin
M
Hofrichter
Martin
M
D055362:Agrocybe / Q000201:enzymology*; D002384:Catalysis; D006841:Hydrocarbons, Aromatic / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D011725:Pyridines / Q000378:metabolism*; D013379:Substrate Specificity
D006841:Hydrocarbons, Aromatic; D011725:Pyridines; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; C022333:peroxygenase; C023666:pyridine; D010100:Oxygen