Jump to main content
Jump to site search

Issue 4, 2011
Previous Article Next Article

Design of H2O2-dependent oxidation catalyzed by hemoproteins

Author affiliations

Abstract

The monooxygenese activity of cytochrome P450 is successfully introduced into myoglobin by rational design of its active site. Introduction of an aromatic ring, tryptophan, near the heme by site-directed mutagenesis resulted in the hydroxylation of tryptophan at the C6 position by using an almost stoichiometric amount of H2O2. We also altered the substrate specificity of H2O2-dependent P450 by employing a simple substrate trick. Although P450BSβ exclusively catalyzes peroxygenation of long-alkyl-chain fatty acids, oxidation of non-natural substrates such as styrene, ethylbenzene, and 1-methoxynaphthalen are catalyzed by P450BSβ in the presence of decoy molecules having a carboxyl group. Advantageously, the substrate specificity of P450BSβ can be altered by simply adding the decoy molecule without replacing any amino acid residues. Moreover, the stereoselectivity can be controlled by changing the structure of the decoy molecule. The crystal structure analysis of the decoy molecule bound-form of P450BSβ shows that P450BSβ accepts the decoy molecule, whose carboxylate is located at the same position to that of long-alkyl-chain fatty acid.

Graphical abstract: Design of H2O2-dependent oxidation catalyzed by hemoproteins

  • This article is part of the themed collection: Cytochromes
Back to tab navigation

Publication details

The article was received on 26 Nov 2010, accepted on 21 Jan 2011 and first published on 10 Feb 2011


Article type: Paper
DOI: 10.1039/C0MT00090F
Citation: Metallomics, 2011,3, 379-388
  •   Request permissions

    Design of H2O2-dependent oxidation catalyzed by hemoproteins

    O. Shoji and Y. Watanabe, Metallomics, 2011, 3, 379
    DOI: 10.1039/C0MT00090F

Search articles by author

Spotlight

Advertisements