Journal
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Volume 60, Issue 1, Pages 111-118Publisher
WILEY-BLACKWELL
DOI: 10.1002/bab.1063
Keywords
cytochrome P450; peroxygenase; CYP152; light-driven biocatalysis; flavin; hydrogen peroxide
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The cytochrome P450 peroxygenases P450Bs (CYP152A1) from Bacillus subtilis and P450Cla (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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