Proton-Directed Redox Control of O-O Bond Activation by Heme Hydroperoxidase Models

摘要

Hangman metalloporphyrin complexes poise an acid-base group over a redox-active metal center and in doing so allow the "pull" effect of the secondary coordination environment of the heme cofactor of hydroperoxidase enzymes to be modeled. Stopped-flow investigations have been performed to decipher the influence of a proton-donor group on O-O bond activation. Low-temperature reactions of tetramesi-tylporphyrin (IMP) and Hangman iron complexes containing acid (HPX-CO_2H) and methyl ester (HPX-CO_2Me) functional groups with peroxyacids generate high-valent Fe=O active sites. Reactions of peroxyacids with (TMP)Fe~Ⅲ(OH) and methyl ester Hangman (HPX-CO_2Me)Fe~Ⅲ(OH) give both O-O heterolysis and homolysis products, Compound Ⅰ (Cpd Ⅰ) and Compound Ⅱ (Cpd Ⅱ), respectively. However, only the former is observed when the hanging group is the acid, (HPX-CO_2H)Fe~ⅢOH), because odd-electron homolytic O-O bond cleavage is inhibited. This proton-controlled, 2e~- (heterolysis) vs 1e~-(homolysis) redox specificity sheds light on the exceptional catalytic performance of the Hangman metalloporphyrin complexes and provides tangible benchmarks for using proton-coupled multielectron reactions to catalyze O-O bond-breaking and bond-making reactions.