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Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita
Author(s) -
Ullrich René,
Dolge Christoph,
Kluge Martin,
Hofrichter Martin
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.11.006
Subject(s) - chemistry , biocatalysis , substrate (aquarium) , monooxygenase , peroxide , pyridine , peroxidase , oxidizing agent , combinatorial chemistry , horseradish peroxidase , organic chemistry , stereochemistry , enzyme , catalysis , cytochrome p450 , reaction mechanism , oceanography , geology
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.