Functional models of nonheme diiron enzymes: kinetic and computational evidence for the formation of oxoiron(iv) species from peroxo-diiron(iii) complexes, and their reactivity towards phenols and H2O2

Miklós István Szávuly; Mihai Surducan; Emőke Nagy; Mátyás Surányi; Gábor Speier; Radu Silaghi-Dumitrescu; József Kaizer

doi:10.1039/c6dt01598k

Functional models of nonheme diiron enzymes: kinetic and computational evidence for the formation of oxoiron(iv) species from peroxo-diiron(iii) complexes, and their reactivity towards phenols and H2O2

Dalton Trans. 2016 Oct 7;45(37):14709-18. doi: 10.1039/c6dt01598k. Epub 2016 Jun 10.

Authors

Miklós István Szávuly¹, Mihai Surducan, Emőke Nagy, Mátyás Surányi, Gábor Speier, Radu Silaghi-Dumitrescu, József Kaizer

Affiliation

¹ Department of Chemistry, University of Pannonia, 8201 Veszprém, Wartha Vince u. 1., Hungary. kaizer@almos.vein.hu.

PMID: 27283752
DOI: 10.1039/c6dt01598k

Abstract

The reactivity of the previously reported peroxo adducts [Fe2(μ-O2)(L(1))4(CH3CN)2](2+), and [Fe2(μ-O2)(L(2))4(CH3CN)2](2+), (L(1) = 2-(2'-pyridyl)benzimidazole and L(2) = 2-(2'-pyridyl)-N-methylbenzimidazole) towards H2O2 as catalase mimics, and towards various phenols as functional RNR-R2 mimics, is described. Kinetic, mechanistic and computational studies gave direct evidence for the involvement of the (μ-1,2-peroxo)diiron(iii) intermediate in the O-H activation process via formation of low-spin oxoiron(iv) species.