Isolation and characterization of a dihydroxo-bridged iron(III,III)(μ-OH)2 diamond core derived from dioxygen.

ABSTRACT: Dioxygen addition to coordinatively unsaturated [Fe(II)(O(Me2)N4(6-Me-DPEN))](PF6) (1) is shown to afford a complex containing a dihydroxo-bridged Fe(III)2(μ-OH)2 diamond core, [Fe(III)(O(Me2)N4(6-Me-DPEN))]2(μ-OH)2(PF6)2·(CH3CH2CN)2 (2). The diamond core of 2 resembles the oxidized methane monooxygenase (MMOox) resting state, as well as the active site product formed following H-atom abstraction from Tyr-OH by ribonucleotide reductase (RNR). The Fe-OH bond lengths of 2 are comparable with those of the MMOHox suggesting that MMOHox contains a Fe(III)2(μ-OH)2 as opposed to Fe(III)2(μ-OH)(μ-OH2) diamond core as had been suggested. Isotopic labeling experiments with (18)O2 and CD3CN indicate that the oxygen and proton of the μ-OH bridges of 2 are derived from dioxygen and acetonitrile. Deuter

SUBMITTER: Coggins MK 

PROVIDER: S-EPMC3885352 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature