TITLE

Aromatic C–H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig’s blue formation

AUTHOR(S)
Shoji, Osami; Wiese, Christian; Fujishiro, Takashi; Shirataki, Chikako; Wünsch, Bernhard; Watanabe, Yoshihito
PUB. DATE
September 2010
SOURCE
Journal of Biological Inorganic Chemistry;Sep2010, Vol. 15 Issue 7, p1109
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
omatic C–H bond hydroxylation of 1-methoxynaphthalene was efficiently catalyzed by the substrate misrecognition system of the hydrogen peroxide dependent cytochrome P450 (CYP152A1), which usually catalyzes hydroxylation of long-alkyl-chain fatty acids. Very importantly, the hydroxylation of 1-methoxynaphthalene can be monitored by a color change since the formation of 4-methoxy-1-naphthol was immediately followed by its further oxidation to yield Russig’s blue. Russig’s blue formation allows us to estimate the peroxygenation activity of enzymes without the use of high performance liquid chromatography, gas chromatography, and nuclear magnetic resonance measurements.
ACCESSION #
53443528

 

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