Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 34, 2015
Previous Article Next Article

Acetate anion-triggered peroxygenation of non-native substrates by wild-type cytochrome P450s

Author affiliations

Abstract

Cytochrome P450SPα (P450SPα) and cytochrome P450BSβ (P450BSβ) belonging to the CYP152 family of enzymes (CYP152s) can utilize H2O2 efficiently as an oxidant for the generation of compound I. Although P450SPα and P450BSβ have very high substrate specificity and catalyse hydroxylation of long-chain fatty acids exclusively, we found that they can oxidize non-native substrates such as styrene simply by including medium chain length n-alkyl carboxylic acids as “decoy molecules.” Although we had assumed that acetic acid did not serve as a decoy molecule, P450SPα and P450BSβ efficiently catalysed oxidation of non-native substrates when the reaction was carried out at a high concentration of acetate anion. The turnover rate for epoxidation of styrene catalysed by P450BSβ in the presence of 1 M acetate anion reached 590 ± 30 min−1.

Graphical abstract: Acetate anion-triggered peroxygenation of non-native substrates by wild-type cytochrome P450s

Back to tab navigation

Supplementary files

Article information


Submitted
24 Feb 2015
Accepted
29 May 2015
First published
09 Jun 2015

Dalton Trans., 2015,44, 15316-15323
Article type
Paper

Acetate anion-triggered peroxygenation of non-native substrates by wild-type cytochrome P450s

H. Onoda, O. Shoji and Y. Watanabe, Dalton Trans., 2015, 44, 15316
DOI: 10.1039/C5DT00797F

Social activity

Search articles by author

Spotlight

Advertisements