Golden Gate BridgeAbstract Imagehttp://www.asbmb.org/assets/0/366/418/428/116556/116557/116558/63774bcb-ae9d-43ab-9c67-cb05dd5bb1fd.pngDr. Cheruzel with Ngoc Han TranCheruzel Research PictureChem 1A studentChristmas 2012 Potluck

The specific and selective oxidation of an unactivated C-H bond remains one of the most challenging reactions in organic chemistry. Cytochrome P450 is a unique superfamily of heme-thiolate enzymes that catalyze the insertion of an oxygen atom, derived from molecular dioxygen, into a C-H bond of a variety of organic substrates, often with high degrees of regio- and stereoselectivity. Recent interests in these proteins arise from the desire to harness their synthetic potential for biotechnological applications.

Our laboratory focuses on developing hybrid P450 biocatalysts capable of the selective oxidation of organic substrate C-H bonds upon light activation. The hybrid enzymes consist of a photosensitizer covalently attached to P450 heme domains.