Antibody-Metalloporphyrin Catalytic Assembly Mimics Natural Oxidation Enzymes
An antibody−metalloporphyrin assembly that catalyzes the enantioselective oxidation of aromatic sulfides to sulfoxides is presented. Antibody SN37.4 was elicited against a water-soluble tin(IV) porphyrin containing an axial α-naphthoxy ligand. The catalytic assembly comprising antibody SN37.4 and a ruthenium(II) porphyrin cofactor exhibited typical enzyme characteristics, such as predetermined oxidant and substrate selectivity, enantioselective delivery of oxygen to the substrate, and Michaelis−Menten saturation kinetics. This assembly, which promotes a complex, multistep catalytic event, represents a close model of natural heme-dependent oxidation enzymes.