A designed second-sphere hydrogen-bond interaction that critically influences the O-O bond activation for heterolytic cleavage in ferric iron-porphyrin complexes.

ABSTRACT: Heme hydroperoxidases catalyze the oxidation of substrates by H₂O₂. The catalytic cycle involves the formation of a highly oxidizing species known as Compound I, resulting from the two-electron oxidation of the ferric heme in the active site of the resting enzyme. This high-valent intermediate is formed upon facile heterolysis of the O-O bond in the initial Fe^III-OOH complex. Heterolysis is assisted by the histidine and arginine residues present in the heme distal cavity. This chemistry has not been successfully modeled in synthetic systems up to now. In this work, we have used a series of iron(iii) porphyrin complexes (Fe^IIIL2(Br), Fe^IIIL3(Br) and Fe^IIIMPh(Br)) with covalently attached pendent basic groups (pyridine

SUBMITTER: Bhunia S 

PROVIDER: S-EPMC8157560 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature