most citedStructure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction

90 citations · 182 across the 14 of their papers we have counts for

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physics.chem-ph2015

Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii

Christelle Mathé, Tony A Mattioli, Olivier Horner +4

The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here…

physics.chem-ph20151 cited

Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis

M. Lombard, C. Houée-Levin, D. Touati +2

Superoxide reductase (SOR) is a small metalloenzyme that catalyzes reduction of O(2)(*)(-) to H(2)O(2) and thus provides an antioxidant mechanism against superoxide radicals. Its a…

physics.chem-ph201529 cited

Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide

Fernando P Molina-Heredia, Chantal Houée-Levin, Catherine Berthomieu +5

The superoxide radical O(2)(-.) is a toxic by-product of oxygen metabolism. Two O(2)(-.) detoxifying enzymes have been described so far, superoxide dismutase and superoxide reducta…

physics.chem-ph2014

M{ö}ssbauer characterization of an unusual high-spin side-on peroxo-Fe3+ species in the active site of superoxide reductase from Desulfoarculus Baarsii. Density functional calculations on related models

Olivier Horner, Jean-Marie Mouesca, Jean-Louis Oddou +9

Superoxide reductase (SOR) is an Fe protein that catalyzes the reduction of superoxide to give H(2)O(2). Recently, the mutation of the Glu47 residue into alanine (E47A) in the acti…