Multi-engineering of Microbial Cytochrome P450 Enzymes

Conference Dates

September 15-19, 2019


Selective oxidation of unactivated C–H bonds remains a central challenge in synthetic chemistry. Cytochrome P450 enzymes, a superfamily of ubiquitous hemoproteins, represent the nature’s primary solutions to overcome this challenge. As promising biocatalysts for practical applications in pharmaceutical, biotechnological and chemical industries, P450 enzymes have attracted a wealth of attention due to their great versatility in catalyzing diverse oxidative reactions (e.g., the sp3 C–H hydroxylation and the sp2 C=C epoxidation) on structurally complex and heavily functionalized substrates in regio- and/or stereoselective manners. However, wild type P450 enzymes usually show suboptimal activity, low stability, and narrow substrate spectra, which have significantly limited their broader applications. A typical P450 reaction system includes a P450 enzyme as the central catalyst, a substrate to be oxidized, redox partner proteins for electron transfer, NAD(P)H as the electron donor, and O2 as the oxidant. In the past five years, we have made significant progresses on enzyme engineering, substrate engineering, redox partner engineering, and electron donor engineering for a number of microbial P450 enzymes. These multi-engineering efforts have generated useful engineered P450 catalytic systems for bio-production of pharmaceuticals, chemical intermediates, and biofuel molecules.

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