Oriented (Local) Electric Fields Drive the Millionfold Enhancement of the H-Abstraction Catalysis Observed for Synthetic Metalloenzyme Analogues

This contribution follows the recent remarkable catalysis observed by Groves et al. in hydrogen-abstraction reactions by a) an oxoferryl porphyrin radical-cation complex [Por^⋅+Fe^IV(O)L_ax] and b) a hydroxoiron porphyrazine ferric complex [PyPzFe^III(OH)L_ax], both of which involve positively charged substituents on the outer circumference of the respective macrocyclic ligands. These charge-coronated complexes are analogues of the biologically important Compound I (Cpd I) and synthetic hydroxoferric species, respectively. We demonstrate that the observed enhancement of the H-abstraction catalysis for these systems is a purely electrostatic effect, elicited by the local charges embedded on the peripheries of the respective macrocyclic ligands. Our findings provide new insights into how electrostatics can be employed to tune the catalytic activity of metalloenzymes and can thus contribute to the future design of new and highly efficient hydrogen-abstraction catalysts.