457 citations
Counting papers with at most 25 authors, so collaboration author lists do not stand in for the people here.
- Centre National de la Recherche ScientifiqueFR24 papers
- CEA GrenobleFR22 papers
- Commissariat à l'Énergie Atomique et aux Énergies AlternativesFR22 papers
- Université Joseph FourierFR12 papers
- Université Grenoble AlpesFR7 papers
- CEA Paris-SaclayFR3 papers
- InsermFR3 papers
- Institut de Chimie PhysiqueFR3 papers
- Institut Pluridisciplinaire Hubert CurienFR3 papers
- Université Paris-SudFR3 papers
- Institut de Biologie StructuraleFR2 papers
- Institut de Recherches en Technologies et Sciences pour le VivantFR2 papers
9 papers · 1 filter
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 (…
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…
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…
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…
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…
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…
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…
Paleoproteomics explained to youngsters: how did the wedding of two-dimensional electrophoresis and protein sequencing spark proteomics on: Let there be light
Thierry Rabilloud
Taking the opportunity of the 20th anniversary of the word "proteomics", this young adult age is a good time to remember how proteomics came from enormous progress in protein separ…
The proteomic to biology inference, a frequently overlooked concern in the interpretation of proteomic data: A plea for functional validation
Thierry Rabilloud, Pierre Lescuyer
Proteomics will celebrate its 20th year in 2014. In this relatively short period of time, it has invaded most areas of biology and its use will probably continue to spread in the f…