Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from actinomycetes.

The hydroxylation of alpha-ionone 1 and beta-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 alpha-ionone 1 the reaction is highly diastereoselective yielding the anti-isomer.