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Biotechnol Appl Biochem. 2013 Jan-Feb;60(1):111-8. doi: 10.1002/bab.1063. Epub 2013 Jan 25.

Light-driven biocatalysis with cytochrome P450 peroxygenases.

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Institute of Biochemistry, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.


The cytochrome P450 peroxygenases P450(Bsβ) (CYP152A1) from Bacillus subtilis and P450(Cla) (CYP152A2) from Clostridium acetobutylicum belong to a unique group of P450s with high synthetic potential. They consume hydrogen peroxide via the peroxide shunt and therefore do not require additional electron transfer proteins for biocatalytic activity. Their high synthetic potential is, however, impaired by their rather poor operational stability in the presence of hydrogen peroxide. Herein, we report the use of a light-driven approach utilizing light-excited flavins (riboflavin, flavin mononucleotide, or flavin adenine dinucleotide) and the electron donor ethylenediaminetetraacetate as the electron source for the in situ generation of hydrogen peroxide. This approach represents a simple and easily applicable way to promote oxyfunctionalization reactions catalyzed by P450 peroxygenases and is useful for biocatalysis with these enzymes.

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