Pedro S. Coelho

TL;DR: E engineered variants of cytochrome P450BM3 that catalyze highly diastereo- and enantioselective cyclopropanation of styrenes from diazoester reagents via putative carbene transfer are reported, highlighting the capacity to adapt existing enzymes for the catalysis of synthetically important reactions not previously observed in nature.

TL;DR: The most prevalent mechanistic strategies used by enzymes to functionalize non-acidic C-H bonds are discussed, the application and evolution of these enzymes for chemical synthesis, and a number of potential biosynthetic capabilities uniquely enabled by these powerful catalysts are discussed.

TL;DR: A unique serine-heme ligated cytochrome “P411” that catalyzes efficient and selective carbene transfers from diazoesters to olefins in intact Escherichia coli cells is designed.

TL;DR: Engineered variants of cytochrome P450_(BM3) have now been found to catalyze intramolecular C-H aminations in azide substrates, with mutations to two highly conserved residues significantly increased this activity.

TL;DR: A highly active His-ligated variant of P450-BM3 that can be employed for the enantioselective synthesis of the levomilnacipran core was engineered and catalyzes the cyclopropanation of N,N-diethyl-2-phenylacrylamide with an estimated initial rate of over 1000 turnovers per minute.