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

457 citations

researchers with a paper here

Counting papers with at most 25 authors, so collaboration author lists do not stand in for the people here.

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11 papers · 1 filter

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…

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…

q-bio.BM2014

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme

Gergely Katona, Philippe Carpentier, Vincent Nivière +5

Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (…

q-bio.BM2014

Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates

V Nivière, M. A. Vanoni, G. Zanetti +1

Flavin reductase catalyzes the reduction of free flavins by NAD(P)H. As isolated, Escherichia coli flavin reductase does not contain any flavin prosthetic group but accommodates bo…

q-bio.BM2014

Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity

M Lombard, M Fontecave, D Touati +1

Desulfoferrodoxin is a small protein found in sulfate-reducing bacteria that contains two independent mononuclear iron centers, one ferric and one ferrous. Expression of desulfofer…

q-bio.BM2014

Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes

Christelle Mathé, Vincent Nivière, Tony A Mattioli

Superoxide reductase (SOR) catalyzes the reduction of O2*- to H2O2. Its active site consists of a non-heme Fe2+ center in an unusual square-pyramidal [His4 Cys] coordination. Like…

q-bio.BM2014

Superoxide reductase from Desulfoarculus baarsii

Vincent Nivière, Murielle Lombard

Superoxide radical (O2.-) is the univalent reduction product of molecular oxygen and belongs to the group of the so-called toxic oxygen derivatives. For years the only enzymatic sy…

q-bio.BM2014★ 63 cited

Discovery of superoxide reductase: an historical perspective

Vincent Nivière, Marc Fontecave

For more than 30 years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living i…