output
20062025
most citedImprovement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients

457 citations

Showing 2015Show all

8 papers · 1 filter

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…

q-bio.BM2015★ 59 cited

A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor

Julien Valton, Laurent Filisetti, Marc Fontecave +1

The two-component flavin-dependent monooxygenases belong to an emerging class of enzymes involved in oxidation reactions in a number of metabolic and biosynthetic pathways in micro…

q-bio.BM2015★ 16 cited

The flavin reductase ActVB from Streptomyces coelicolor: characterization of the electron transferase activity of the flavoprotein form

Laurent Filisetti, Julien Valton, Marc Fontecave +1

The flavin reductase ActVB is involved in the last step of actinorhodin biosynthesis in Streptomyces coelicolor. Although ActVB can be isolated with some FMN bound, this form was n…

physics.chem-ph2015★ 48 cited

Pulse radiolysis studies on superoxide reductase from Treponema pallidum

V Nivière, M. Lombard, M. Fontecave +1

Superoxide reductases (SORs) are small metalloenzymes, which catalyze reduction of O2*- to H2O2. The reaction of the enzyme from Treponema pallidum with superoxide was studied by p…

physics.chem-ph2015★ 1 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…

q-bio.BM2015

The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides

V. Nivière, F. Fieschi, J. L. Dećout +1

The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The…

q-bio.BM2015★ 16 cited

Hydrogen bonding to the cysteine ligand of superoxide reductase: acid--base control of the reaction intermediates

Emilie Tremey, Florence Bonnot, Yohann Moreau +6

Superoxide reductase SOR is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [Hi…

q-bio.BM2015

Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii

Christelle Mathé, Vincent Nivière, Chantal Houée-Levin +1

Superoxide reductases (SORs) are superoxide (O2-)-detoxifying enzymes that catalyse the reduction of O2- into hydrogen peroxide. Three different classes of SOR have been reported o…