Issue 37, 2016

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

Abstract

The reactivity of the previously reported peroxo adducts [Fe2(μ-O2)(L1)4(CH3CN)2]2+, and [Fe2(μ-O2)(L2)4(CH3CN)2]2+, (L1 = 2-(2′-pyridyl)benzimidazole and L2 = 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.

Graphical abstract: 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

Supplementary files

Article information

Article type
Paper
Submitted
25 ኤፕሪ 2016
Accepted
05 ጁን 2016
First published
06 ጁን 2016

Dalton Trans., 2016,45, 14709-14718

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

M. I. Szávuly, M. Surducan, E. Nagy, M. Surányi, G. Speier, R. Silaghi-Dumitrescu and J. Kaizer, Dalton Trans., 2016, 45, 14709 DOI: 10.1039/C6DT01598K

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