Abstract
An antibody elicited to a distorted N -methyl porphyrin catalyzed metal ion chelation by the planar porphyrin. At fixed Zn 2+ and Cu 2+ concentrations, the antibody-catalyzed reaction showed saturation kinetics with respect to the substrate mesoporphyrin IX (2) and was inhibited by the hapten, N -methylmesoporphyrin IX (1). The turnover number of 80 hour -1 for antibody-catalyzed metallation of 2 with Zn 2+ compares with an estimated value of 800 hour -1 for ferrochelatase. The antibody also catalyzed the insertion of Co 2+ and Mn 2+ into 2, but it did not catalyze the metallation of protoporphyrin IX (3) or deuteroporphyrin IX (4). The antibody has high affinity for several metalloporphyrins, suggesting an approach to developing antibody-heme catalysts for redox or electron transfer reactions.

This publication has 16 references indexed in Scilit: