期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 129, 期 16, 页码 5069-5075出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja0683032
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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 tetramesitylporphyrin (TMP) and Hangman iron complexes containing acid (HPX-CO2H) and methyl ester (HPX-CO2Me) functional groups with peroxyacids generate high-valent FeO active sites. Reactions of peroxyacids with (TMP)Fe-III(OH) and methyl ester Hangman (HPX-CO2Me)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-CO2H)Fe-III(OH), 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.
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