Cytochrome P450 monooxygenases are ubiquitous in nature, catalyzing a variety of oxidative transformations.  Recent work has shown that PikC, a P450 isolated from the bacteria <i>Streptomyces venezuelae</i>, can catalyze the regioselective hydroxylation of both small molecule and larger macrolactone ring systems via a unique anchoring mechanism.  The catalytic versatility of PikC, however, remains limited primarily to hydroxylation reactions.  Further research into the activity of mixed function P450s could therefore expand upon the use of enzymes as biocatalysts. This work focuses on the synthesis of an analog of tirandamycin, the natural substrate of the multi-functional P450 TamI, to access novel oxidation products using either PikC or TamI.  Investigation into these biocatalytic systems explores whether PikC can install multiple types of oxidative functionality within the bicyclic core of tirandamycin as well as probes the utility of TamI as a new biocatalyst for site-selective C-H functionalization of unnatural substrates.<br/>

Exploring biosynthetic P450s as biocatalysts for multi-functional C-H oxidation

254th National Meeting (2017)

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