The high regio- and stereoselectivity offered by P450 enzymes in the functionalization of C-H bonds has rendered them of high interest for industrial and synthetic applications. These heme-thiolate enzymes catalyze a number of selective oxidation reactions utilizing molecular dioxygen and two reducing equivalents typically delivered by the electron carrier, reductase. Our laboratory has utilized the photochemical properties of Ru(II) based photosensitizer covalently attached to P450 BM3 heme domain mutants in order to harness the synthetic potential upon light activation. As recently reported, the optimization of this system has led to some of the highest catalytic activities for the hydroxylation of lauric acid with P450 BM3. To further capitalize on their synthetic potential, we have generated a library of light-driven P450 heme domain mutants able to accommodate a wide range of non-natural substrates. We will present our current efforts toward the oxidation of non-natural substrates and the production of synthetically valuable synthons.

Expanding the synthetic scope of light-driven hybrid P450 enzymes

248th National Meeting (2014)

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