Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 15, Issue 7, Pages 1109-1115Publisher
SPRINGER
DOI: 10.1007/s00775-010-0671-9
Keywords
Cytochrome P450; Hydroxylation; Hydrogen peroxide; Colorimetric assay; Enzyme catalysis
Funding
- Ministry of Education, Culture, Sports, Science, and Technology (Japan)
- International Research Training Group (DFG)
- International Research Training Group (JSPS)
- JSPS
- Grants-in-Aid for Scientific Research [19105004, 21685018] Funding Source: KAKEN
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Aromatic C-H bond hydroxylation of 1-methoxynaphthalene was efficiently catalyzed by the substrate misrecognition system of the hydrogen peroxide dependent cytochrome P450(BS beta) (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.
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