An Artificial Metalloenzyme Based on a Copper Heteroscorpionate Enables sp<sup>3</sup> C–H Functionalization via Intramolecular Carbene Insertion
Corentin Rumo, Alina Stein, Juliane Klehr, Ryo Tachibana, Alessandro Prescimone, Daniel Häußinger, Thomas R. Ward
Abstract
C-H bonds. Target residues for genetic optimization of the artificial metalloenzyme were identified by quantum mechanics/molecular mechanics simulations. Double-saturation mutagenesis yielded detailed insight on the contribution of individual amino acids on the activity and the selectivity of the artificial metalloenzyme. Mutagenesis at a third position afforded a set of artificial metalloenzymes that catalyze the enantio- and regioselective formation of β- and γ-lactams with high turnovers and promising enantioselectivities.
Topics & Concepts
ChemistryIntramolecular forceCarbeneSaturated mutagenesisSurface modificationStereochemistryRegioselectivityCombinatorial chemistryCatalysisOrganic chemistryMutantBiochemistryPhysical chemistryGeneCyclopropane Reaction MechanismsCatalytic C–H Functionalization MethodsSynthesis and Catalytic Reactions