Site-Selective Enzymatic C–H Amidation for Synthesis of Diverse Lactams

Frances Arnold presents a site-selective enzymatic C–H amidation to synthesize diverse lactams.

A paramount challenge in carbon–hydrogen (C–H) functionalization is to control the site selectivity of the reaction. Current methods use directing groups and/or substrate control to pick out a particular C–H bond, which limits the breadth of potential substrates. Recently, an enzymatic strategy to address this challenge was reported by Professor Frances H. Arnold and her co-workers from the California Institute of Technology (USA). They used directed evolution to tune the site selectivity of C–H amidation catalyzed by heme enzymes. The Arnold group’s study uses an iron-heme cytochrome ‘P411’ to perform a C–H amidation transformation not found in nature. With directed evolution, the researchers fine-tuned the site selectivity of intramolecular amidation to deliver lactam products of various sizes.

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