Bringing new catalytic functions to naturally occurring enzymes can dramatically expand the repertoire of enzymology and generate novel biocatalysts. Inspired by the innate redox properties of first-row transition-metal cofactor, our group has recently begun to repurpose metalloproteins to catalyze stereoselective radical reactions triggered by single electron transfer. Due to the lack of exploitable stereocontrol elements in synthetic systems, steering the absolute and relative stereochemistry of these free radical processes is notoriously difficult in asymmetric catalysis. We engineered a set of metalloenzymes to impose excellent stereocontrol over the bond forming events in these unnatural processes, allowing stereodivergent radical catalysis to be easily carried out. These metalloenzymes are fully genetically encoded and readily function in bacterial cells, displaying excellent activities at room temperature . Collectively, this evolvable metalloenzyme platform represents a promising solution to tame fleeting radical intermediates for asymmetric catalysis.

New-to-nature metalloredox biocatalysis for stereoselective radical transformations

ACS Spring 2022

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