Issue 16, 2005
From the journal:

Organic & Biomolecular Chemistry

Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from Actinomycetes

Ayhan Çelik,a   Sabine L. Flitscha  and  Nicholas J. Turner*a  

* Corresponding authors

a School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, UK
E-mail: n.j.turner@ed.ac.uk
Fax: +44 (0) 131 650 4719
Tel: +44 (0) 131 650 4719

Abstract

The hydroxylation of α-ionone 1 and β-ionone 2 to their corresponding mono-hydroxylated derivatives has been examined using a recombinant E. coli whole cell system, in which cytochromes P450 SU1 and SU2, and P450 SOY were over-expressed with their cognate ferrodoxins. Both substrates are hydroxylated with a high degree of regioselectivity and for α-ionone 1 the reaction is highly diastereoselective yielding the anti-isomer.

Graphical abstract: Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from Actinomycetes

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Article information

DOI
https://doi.org/10.1039/B506159H
Article type
Paper
Submitted
04 May 2005
Accepted
13 Jun 2005
First published
07 Jul 2005

Org. Biomol. Chem., 2005,3, 2930-2934

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Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from Actinomycetes

A. Çelik, S. L. Flitsch and N. J. Turner, Org. Biomol. Chem., 2005, 3, 2930 DOI: 10.1039/B506159H

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