Thespecific and selective oxidation of an unactivated C-H bond remains one of themost challenging reactions in organic chemistry. Cytochrome P450, heme-thiolateenzymes, catalyze the insertion of an oxygen atom, derived from moleculardioxygen, into a C-H bond of a variety of substrates, often with high degreesof regio- and stereoselectivity. Recent interests in these proteins arise fromthe desire to harness their synthetic potential for biotechnologicalapplications. The main challenge in utilizing P450s asbiocatalysts has been in the control of the electron delivery to the buriedactive site of the enzymes while preventing protein deactivation by reactiveoxygen species. We have developed hybrid enzymes constituted ofa photosensitizer covalently attached to the heme domain of P450 BM3 mutants. Theseenzymes have been characterized by UV-Vis and fluorescence spectroscopies, and massspectrometry. Our preliminary results in hydroxylating lauric acid under constantvisible light irradiation will be presented.

Engineered P450
BM3 enzymes towards specific C-H bond oxidation using light activation

241st National Meeting (2011)

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