The past several years have witnessed exciting developments in the field of stereoselective radical biocatalysis. Guided by the fundamental principles of organic and transition-metal chemistry, various organic cofactor and metallocofactor -dependent enzymes were repurposed to catalyze free radical-mediated asymmetric transformations previously unknown in enzymology, allowing the achievement of challenging stereocontrol over free radical intermediates, many of which had previously eluded small-molecule catalyst systems. In the early stages of this effort, the central doctrine in biocatalytic radical reaction design emphasized that the key radical intermediate must be generated within the enzyme's active site, often through the involvement of a redox-active cofactor and/or substrate-cofactor charge transfer complex. In these processes, the binding and activation of the radical precursor with the enzyme precede radical initiation. While this strategy has proven tremendously successful and culminated in an astonishing array of useful biocatalytic radical reactions, 2 it poses limitations for the types of enzymes that could be used for rational radical reaction design.