Abstract 1357 Design of a biotinylated [Cp*Co(III)Cl2]2-Streptavidin Artificial Metalloenzyme for C-H bond activation

Transitions metals donate electrons easily and have multiple coordination sites, making them prime candidates for bond activation, while enzymes have catalytic rates many times faster than typically produced in a laboratory setting. Engineering artificial metalloenzymes to incorporate transition metal complexes can create systems with higher substrate selectivity and/or enhanced catalytic efficiency in comparison to the isolated metal complex. Previous studies have shown that a biotinylated [Cp*Rh(III)Cl2]2 complex docked to a tailored streptavidin protein can increase the asymmetric carbon-hydrogen bond activation properties of the rhodium complex by 100 fold.