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Issue 16, 2005
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Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from Actinomycetes

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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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Publication details

The article was received on 04 May 2005, accepted on 13 Jun 2005 and first published on 07 Jul 2005


Article type: Paper
DOI: 10.1039/B506159H
Citation: 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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