Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita was written by Ullrich, Rene;Dolge, Christoph;Kluge, Martin;Hofrichter, Martin. And the article was included in FEBS Letters in 2008.Computed Properties of C7H9NO This article mentions the following:
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 H2 18O2 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 P 450 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. In the experiment, the researchers used many compounds, for example, 3,5-Dimethylpyridine 1-oxide (cas: 3718-65-8Computed Properties of C7H9NO).
3,5-Dimethylpyridine 1-oxide (cas: 3718-65-8) belongs to pyridine derivatives. The pyridine ring occurs in many important compounds, including agrochemicals, pharmaceuticals, and vitamins. Pyridine, its benzo and pyridine-based compounds play diverse roles in organic chemistry. Pyridine-based materials are valued for their optical and physical properties as well as their medical potential. Computed Properties of C7H9NO