Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450†
Alecia R.
Gee, 
a
Isobella S. J.
Stone,
a
Tegan P.
Stockdale,
b
Tara L.
Pukala,
a
James J.
De Voss
b
and
Stephen G.
Bell
*a
a
Isobella S. J.
Stone,
a
Tegan P.
Stockdale,
b
Tara L.
Pukala,
a
James J.
De Voss
b
and
Stephen G.
Bell
*a
Abstract
A highly sought after reaction in chemical synthesis is the activation of unactivated carbon–hydrogen bonds. We demonstrate the hydroxylation of fatty acids using an engineered thermostable archaeal cytochrome P450 enzyme. By replacing a seven amino acid section of the I-helix, the nicotinamide cofactor-dependent monooxygenase was converted into a hydrogen peroxide using peroxygenase, enabling the efficient biocatalytic oxidation of C–H bonds at room temperature to 90 °C.
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