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.
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.
Department of Chemistry, University of Pannonia, 8201 Veszprém, Wartha Vince u. 1., Hungary. kaizer@almos.vein.hu.
Miklós István
MI
Szávuly
Mihai
M
Surducan
Emőke
E
Nagy
Mátyás
M
Surányi
Gábor
G
Speier
Radu
R
Silaghi-Dumitrescu
József
J
Kaizer