Unknown

Dataset Information

0

Sc3+-Promoted O-O Bond Cleavage of a (?-1,2-Peroxo)diiron(III) Species Formed from an Iron(II) Precursor and O2 to Generate a Complex with an FeIV2(?-O)2 Core.


ABSTRACT: Soluble methane monooxygenase (sMMO) carries out methane oxidation at 4 °C and under ambient pressure in a catalytic cycle involving the formation of a peroxodiiron(III) intermediate (P) from the oxygenation of the diiron(II) enzyme and its subsequent conversion to Q, the diiron(IV) oxidant that hydroxylates methane. Synthetic diiron(IV) complexes that can serve as models for Q are rare and have not been generated by a reaction sequence analogous to that of sMMO. In this work, we show that [FeII(Me3NTB)(CH3CN)](CF3SO3)2 (Me3NTB = tris((1-methyl-1H-benzo[d]imidazol-2-yl)methyl)amine) (1) reacts with O2 in the presence of base, generating a (?-1,2-peroxo)diiron(III) adduct with a low O-O stretching frequency of 825 cm-1 and a short Fe···Fe distance of 3.07 Å. Even more interesting is the observation that the peroxodiiron(III) complex undergoes O-O bond cleavage upon treatment with the Lewis acid Sc3+ and transforms into a bis(?-oxo)diiron(IV) complex, thus providing a synthetic precedent for the analogous conversion of P to Q in the catalytic cycle of sMMO.

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC7136037 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Sc<sup>3+</sup>-Promoted O-O Bond Cleavage of a (μ-1,2-Peroxo)diiron(III) Species Formed from an Iron(II) Precursor and O<sub>2</sub> to Generate a Complex with an Fe<sup>IV</sup><sub>2</sub>(μ-O)<sub>2</sub> Core.

Banerjee Saikat S   Draksharapu Apparao A   Crossland Patrick M PM   Fan Ruixi R   Guo Yisong Y   Swart Marcel M   Que Lawrence L  

Journal of the American Chemical Society 20200219 9


Soluble methane monooxygenase (sMMO) carries out methane oxidation at 4 °C and under ambient pressure in a catalytic cycle involving the formation of a peroxodiiron(III) intermediate (<b>P</b>) from the oxygenation of the diiron(II) enzyme and its subsequent conversion to <b>Q</b>, the diiron(IV) oxidant that hydroxylates methane. Synthetic diiron(IV) complexes that can serve as models for <b>Q</b> are rare and have not been generated by a reaction sequence analogous to that of sMMO. In this wor  ...[more]

Similar Datasets

| S-EPMC3760346 | biostudies-literature
| S-EPMC2736334 | biostudies-literature
| S-EPMC2787896 | biostudies-literature
| S-EPMC2765497 | biostudies-literature
| S-EPMC5765857 | biostudies-literature
| S-EPMC2812653 | biostudies-literature
| S-EPMC5605297 | biostudies-literature
| S-EPMC8251627 | biostudies-literature
| S-EPMC8168641 | biostudies-literature
| S-EPMC4063178 | biostudies-literature