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Updated: Jul 12, 2025

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Efficient biocatalytic C-H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome
Alecia R Gee1, Isobella S J Stone1, Tegan P Stockdale2
1School of Physics, Chemistry and Earth Sciences, University of Adelaide, Adelaide, SA 5005, Australia. stephen.bell@adelaide.edu.au.
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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