V. Nivière

发表

NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.

J. Covès, M. Fontecave, M. Eschenbrenner, 1993, The Journal of biological chemistry.

The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals.

D. Touati, M. Fontecave, P. Gaudu, 1994, The Journal of biological chemistry.

Kinetic studies of electron transfer between hydrogenase and cytochrome c3 from Desulfovibrio gigas. Electrochemical properties of cytochrome c3

E. Hatchikian, P. Bianco, J. Haladjian, 1988 .

Assessing the Role of the Active-site Cysteine Ligand in the Superoxide Reductase from Desulfoarculus baarsii*

C. Houée-Lévin, T. Mattioli, C. Weill, 2007, Journal of Biological Chemistry.

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

D. Touati, V. Adam, C. Houée-Lévin, 2006, Proceedings of the National Academy of Sciences.

Novel Mn-SOD Mimetics Offer Superior Protection Against Oxidative Damages in Hek293 Kidney Cells

S. Padhye, Z. Afrasiabi, M. Khetmalas, 2014 .

Distribution of Hydrogenase Genes in Desulfovibrio spp. and Their Use in Identification of Species from the Oil Field Environment

D. Westlake, P. Fedorak, F. G. Ferris, 1990, Applied and environmental microbiology.

A Two-component Flavin-dependent Monooxygenase Involved in Actinorhodin Biosynthesis in Streptomyces coelicolor*

M. Fontecave, V. Nivière, Julien Valton, 2004, Journal of Biological Chemistry.

Isolation, amino acid analysis and N-terminal sequence determination of the two subunits of the nickel-containing hydrogenase of Desulfovibrio gigas.

C. Hatchikian, J. Bonicel, G. Bovier-Lapierre, 1988, Biochimie.

Mössbauer 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.

P. Maldivi, M. Fontecave, T. Mattioli, 2004, Biochemistry.

Physicochemical Properties of Nanoparticles in Relation with Toxicity

O. Proux, J. Rose, J. Bottero, 2012 .

Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in Escherichia coli.

B. Guigliarelli, F. Fieschi, Corinne Vivès, 2021, ACS chemical biology.

Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study.

M. Fontecave, A. Verméglio, C. Berthomieu, 2002, Biochemistry.

Crystallization, preliminary X-ray study and crystal activity of the hydrogenase from Desulfovibrio gigas.

C. Cambillau, C. Hatchikian, V. Nivière, 1987, Journal of molecular biology.

Localization of hydrogenase in Desulfovibrio gigas cells

A. Bernadac, C. Hatchikian, V. Nivière, 1991, Archives of Microbiology.

Kinetic studies of electron transfer between hydrogenase and cytochrome c3 by electrochemistry

F. Guerlesquin, M. Bruschi, P. Bianco, 1990 .

An Aromatic Hydroxylation Reaction Catalyzed by a Two-component FMN-dependent Monooxygenase

T. Douki, M. Fontecave, S. Kendrew, 2006, Journal of Biological Chemistry.

Biological sources of reduced oxygen species

M. Fontecave, V. Nivière, 1995 .

Desulfovibrio alcoholovorans sp. nov., a sulfate-reducing bacterium able to grow on glycerol, 1,2- and 1,3-propanediol

J. García, V. Nivière, A. Qatibi, 1991, Archives of Microbiology.

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

T. Mattioli, V. Nivière, C. Mathé, 2015, Biophysical chemistry.

Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.

S. Ramaswamy, H. Eklund, M. Fontecave, 1999, Biochemistry.

Formation of high-valent iron-oxo species in superoxide reductase: characterization by resonance Raman spectroscopy.

D. von Stetten, P. Carpentier, S. Duval, 2014, Angewandte Chemie.

Reaction of the Desulfoferrodoxin from Desulfoarculus baarsii with Superoxide Anion

D. Touati, M. Fontecave, V. Nivière, 2000, The Journal of Biological Chemistry.

Conformational H-bonding modulation of the iron active site cysteine ligand of superoxide reductase: absorption and resonance Raman studies.

S. Torelli, A. Desbois, V. Nivière, 2021, Physical chemistry chemical physics : PCCP.

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

V. Favaudon, G. Blondin, C. Berthomieu, 2013, JBIC Journal of Biological Inorganic Chemistry.

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

M. Fontecave, G. Zanetti, M. Vanoni, 1998, Biochemistry.

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

M. Fontecave, T. Mattioli, O. Horner, 2002, Journal of the American Chemical Society.

The NAD(P)H:Flavin Oxidoreductase from Escherichia coli

M. Fontecave, F. Fieschi, J. Décout, 1999, The Journal of Biological Chemistry.

The Mechanism and Substrate Specificity of the NADPH:Flavin Oxidoreductase from Escherichia coli(*)

M. Fontecave, F. Fieschi, J. Décout, 1995, The Journal of Biological Chemistry.

Mechanism and Regulation of the Two-component FMN-dependent Monooxygenase ActVA-ActVB from Streptomyces coelicolor*

M. Fontecave, D. Ballou, V. Nivière, 2008, Journal of Biological Chemistry.

A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP*

J. Dupuy, F. Fieschi, Corinne Vivès, 2016, The Journal of Biological Chemistry.

Mechanism and Substrate Specificity of the Flavin Reductase ActVB from Streptomyces coelicolor *

M. Fontecave, V. Nivière, Laurent Filisetti, 2003, The Journal of Biological Chemistry.

Discovery of superoxide reductase: an historical perspective

M. Fontecave, V. Nivière, 2004, JBIC Journal of Biological Inorganic Chemistry.

Cys5 and Cys214 of NAD(P)H:flavin oxidoreductase from Escherichia coli are located in the active site.

M. Fontecave, F. Fieschi, V. Nivière, 1996, European journal of biochemistry.

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

V. Adam, D. Bourgeois, A. Royant, 2004, Structure.

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

V. Adam, D. Bourgeois, A. Royant, 2004 .

Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein.

G. Voordouw, S. Wong, V. Nivière, 1992, Journal of general microbiology.

Interference between nanoparticles and metal homeostasis

N. Herlin‐Boime, T. Douki, J. Ravanat, 2011 .

Characterization of the soluble hydrogenase from Desulfovibrio africanus.

E. Hatchikian, V. Nivière, J. Gayda, 1986, Biochemical and biophysical research communications.

An original electroenzymatic system: Flavin reductase-riboflavin for the improvement of dehydrogenase-based biosensors. Application to the amperometric detection of lactate

S. Cosnier, M. Fontecave, C. Innocent, 1997 .

Raman-Assisted Crystallography Reveals End-On Peroxide Intermediates in a Nonheme Iron Enzyme

Nikolay Tsanov, Patricia Amara, Philippe Carpentier, 2007, Science.

Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum.

D. Touati, M. Fontecave, V. Nivière, 2000, The Journal of biological chemistry.

Superoxide reductase from Desulfoarculus baarsii.

V. Nivière, M. Lombard, 2014, Methods in enzymology.

Photochemical processes observed during the reaction of superoxide reductase from Desulfoarculus baarsii with superoxide: re-evaluation of the reaction mechanism.

V. Favaudon, V. Nivière, C. Houée-Levin, 2010, Biochimica et biophysica acta.

Pulse radiolysis studies on superoxide reductase from Treponema pallidum

M. Fontecave, V. Nivière, M. Lombard, 2001, FEBS letters.

Photonic Crystal Nanobeam Cavities

Sergei V. Kalinin, L. Valdevit, Seajin Oh, 2012 .

The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals

M. Fontecave, Y. Pétillot, P. Gaudu, 1996, FEBS letters.

Iron Hydroperoxide Intermediate in Superoxide Reductase: Protonation or Dissociation First? MM Dynamics and QM/MM Metadynamics Study.

A. Milet, V. Nivière, Yohann Moreau, 2017, Journal of chemical theory and computation.

Control of the evolution of iron peroxide intermediate in superoxide reductase from Desulfoarculus baarsii. Involvement of lysine 48 in protonation.

V. Favaudon, S. Duval, S. Ménage, 2012, Journal of the American Chemical Society.

Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site

S. Duval, V. Nivière, M. Lombard, 2011, JBIC Journal of Biological Inorganic Chemistry.

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

D. Touati, M. Fontecave, V. Nivière, 2001, Biochemistry.

Desulfovibrio Gigas Hydrogenase: Crystallographic Studies

C. Cambillau, C. Hatchikian, V. Nivière, 1990 .

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

T. Mattioli, V. Nivière, C. Mathé, 2005, Journal of the American Chemical Society.

Is the NAD(P)H:Flavin Oxidoreductase from Escherichia coli a Member of the Ferredoxin-NADP+ Reductase Family?

M. Fontecave, F. Fieschi, J. Décout, 1996, The Journal of Biological Chemistry.

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

V. Favaudon, G. Blondin, C. Berthomieu, 2013, JBIC Journal of Biological Inorganic Chemistry.

Non-heme iron hydroperoxo species in superoxide reductase as a catalyst for oxidation reactions.

F. Thomas, S. Rat, S. Ménage, 2014, Chemical communications.