J. Gaillard

发表

A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus.

C. Châtelet, J. Gaillard, Y. Pétillot, 1999, Biochemical and biophysical research communications.

Characterization of a naphthalene dioxygenase endowed with an exceptionally broad substrate specificity toward polycyclic aromatic hydrocarbons.

V. Stojanoff, J. Gaillard, Y. Jouanneau, 2006, Biochemistry.

Molecular mechanism of pyruvate‐ferredoxin oxidoreductases based on data obtained with the Clostridium pasteurianum enzyme

J. Gaillard, J. Meyer, J. Moulis, 1996, FEBS letters.

Purification and properties of a catalase from potato tubers (Solanum tuberosum)

J. Gaillard, J. Gagnon, F. Beaumont, 1990 .

Effect of (5'S)-5',8-cyclo-2'-deoxyadenosine on the conformation of di and trinucleotides. A NMR and DFT study.

J. Cadet, J. Gaillard, B. Karwowski, 2008, Organic & biomolecular chemistry.

Rapid inactivation of plant aconitase by hydrogen peroxide.

J. Gaillard, R. Douce, M. Neuburger, 1991, The Biochemical journal.

Crystallographic and spectroscopic evidence for high affinity binding of FeEDTA(H2O)- to the periplasmic nickel transporter NikA.

J. Fontecilla-Camps, J. Gaillard, L. Jacquamet, 2005, Journal of the American Chemical Society.

Assembly of a [2Fe-2S]2+ cluster in a molecular variant of Clostridium pasteurianum rubredoxin.

C. Colangelo, J. Gaillard, Y. Pétillot, 1997, Biochemistry.

Dioxygenase Reactivation Evidence for Their Involvement in Catechol Catabolism of Cresols or Naphthalene : [ 2 Fe2 S ] Ferredoxins Associated with Characterization of Three XylT-Like

K. Timmis, J. Armengaud, J. Gaillard, 2000 .

A Novel [2Fe-2S] Ferredoxin from Pseudomonas putidamt2 Promotes the Reductive Reactivation of Catechol 2,3-Dioxygenase*

K. Timmis, J. Armengaud, J. Gaillard, 1998, The Journal of Biological Chemistry.

Interaction between pyridine adenine dinucleotides and bovine liver catalase: a chromatographic and spectral study.

J. Gaillard, J. Pelmont, H. Jouve, 1986, Archives of biochemistry and biophysics.

Biochemical characterization of the HydE and HydG iron‐only hydrogenase maturation enzymes from Thermatoga maritima

M. Fontecave, J. Gaillard, J. K. Rubach, 2005, FEBS letters.

Purification and characterization of a novel dimeric ferredoxin (FdIII) from Rhodobacter capsulatus.

J. Gaillard, Y. Jouanneau, C. Meyer, 1993, The Journal of biological chemistry.

Inhibition by iodoacetamide and acetylene of the H-D-exchange reaction catalyzed by Thiocapsa roseopersicina hydrogenase.

J. Gaillard, P. Carrier, P. Vignais, 1996, European journal of biochemistry.

Hydrogen-1 nuclear magnetic resonance of the nitrogenase iron protein (Cp2) from Clostridium pasteurianum.

J. Gaillard, J. Meyer, J. Moulis, 1988, Biochemistry.

Human iron regulatory protein 2 is easily cleaved in its specific domain: consequences for the haem binding properties of the protein.

C. Bougault, J. Gaillard, K. Pantopoulos, 2007, The Biochemical journal.

On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin.

J. Gaillard, J. Moulis, V. Davasse, 1994, Protein engineering.

Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4S] ferredoxin.

J. Gaillard, J. Moulis, I. Quinkal, 1993, Biochemistry.

Replacement Of Sulfur By Selenium In Iron—Sulfur Proteins

J. Gaillard, J. Moulis, Jacques Meyer, 1992 .

Characterization of [4Fe-4Se]2+/3+ high-potential iron−sulfur protein from Chromatium vinosum

J. Gaillard, J. Moulis, Louis Noodleman, 1988 .

Analysis of the high-spin states of the 2[4Fe-4Se]+ ferredoxin from Clostridium pasteurianum by Mössbauer spectroscopy.

J. Gaillard, J. Meyer, J. Moulis, 1987, The Biochemical journal.

Hydrogen-1 nuclear magnetic resonance of selenium-substituted clostridial ferredoxins

J. Gaillard, J. Moulis, Jacques Meyer, 1987 .

High-multiplicity spin states of 2[4Fe-4Se]+ clostridial ferredoxins.

J. Gaillard, J. Meyer, J. Moulis, 1986, Biochemistry.

Unusual features in EPR and Mössbauer spectra of the 2[4Fe-4Se]+ ferredoxin from Clostridium pasteurianum.

J. Gaillard, J. Meyer, J. Moulis, 1984, The Journal of biological chemistry.

Identification of residues of Rhodobacter capsulatus ferredoxin I important for its interaction with nitrogenase.

J. Gaillard, Y. Jouanneau, C. Meyer, 1996, European journal of biochemistry.

Characterization of a 2[4Fe-4S] ferredoxin obtained by chemical insertion of the Fe-S clusters into the apoferredoxin II from Rhodobacter capsulatus.

J. Armengaud, J. Gaillard, Y. Jouanneau, 1995, European journal of biochemistry.

Role of HiPIP as electron donor to the RC-bound cytochrome in photosynthetic purple bacteria

J. Gaillard, A. Verméglio, L. Menin, 1998, Photosynthesis Research.

Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxin.

B. Guigliarelli, J. Gaillard, P. Kyritsis, 1999, Biochemistry.

Site-directed mutagenesis of rubredoxin reveals the molecular basis of its electron transfer properties.

J. Gaillard, J. Moulis, R. Kümmerle, 1997, Biochemistry.

Intramolecular electron transfer between [4Fe-4S] clusters studied by proton magnetic resonance spectroscopy.

J. Gaillard, P. Kyritsis, J. Moulis, 1997, Biochemistry.

Nuclear-magnetic-resonance determination of the electron self-exchange rate constant of Clostridium pasteurianum rubredoxin.

J. Gaillard, J. Moulis, H. Zhuang-Jackson, 1996, European journal of biochemistry.

In vivo participation of a high potential iron-sulfur protein as electron donor to the photochemical reaction center of Rubrivivax gelatinosus.

J. Gaillard, A. Verméglio, L. Menin, 1995, Biochemistry.

Sequence-specific assignments of the 1H nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum.

D. Wemmer, J. Gaillard, J. Moulis, 1992, Biochemistry.

Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster.

J. Gaillard, J. Meyer, Jacques Meyer, 1994, Biochemistry.

Kinetic study of the activation of the neutrophil NADPH oxidase by arachidonic acid. Antagonistic effects of arachidonic acid and phenylarsine oxide.

J. Gaillard, P. Vignais, A. Poinas, 1999, Biochemistry.

Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.

T. Bergman, M. Fontecave, J. Gaillard, 1997, The Journal of biological chemistry.

Purification and characterization of a 7Fe-ferredoxin from Rhodobacter capsulatus.

J. Gaillard, Y. Jouanneau, C. Meyer, 1990, Biochemical and biophysical research communications.

The heme component of the neutrophil NADPH oxidase complex is a target for aryliodonium compounds.

J. Gaillard, P. Vignais, J. Doussière, 1999, Biochemistry.

Expression in Escherichia coli and characterization of a recombinant 7Fe ferredoxin of Rhodobacter capsulatus.

C. Duport, J. Gaillard, Y. Jouanneau, 1992, The Biochemical journal.

Magnetic studies of E. coli ribonucleotide reductase: First evidence of the mixed valence Fe(II)Fe(III) state

M. Fontecave, J. Gaillard, M. Atta, 1991 .

Structural and magnetic properties of a novel pentacopper(II) cluster involving a trinucleating catechol ligand

J. Gaillard, J. Latour, J. Laugier, 1987 .

Synthesis and structural characterization of [Fe4(.mu.3-S)3(.mu.3-S2)Cp4][MoOCl4(THF)]. A new iron-sulfur cluster with different modes of coordination at the iron sites

J. Gaillard, J. Jordanov, P. Auric, 1984 .

Mutated forms of a [2Fe-2S] ferredoxin with serine ligands to the iron-sulfur cluster.

J. Gaillard, J. Meyer, J. Fujinaga, 1993, Biochemical and biophysical research communications.

An Isc-type extremely thermostable [2Fe-2S] ferredoxin from Aquifex aeolicus. Biochemical, spectroscopic, and unfolding studies.

P. Wittung-Stafshede, Catherine L. Higgins, J. Gaillard, 2003, Biochemistry.

Human Cytoplasmic Aconitase (Iron Regulatory Protein 1) Is Converted into Its [3Fe-4S] Form by Hydrogen Peroxide in Vitro but Is Not Activated for Iron-responsive Element Binding*

M. Hentze, J. Gaillard, K. Pantopoulos, 1999, The Journal of Biological Chemistry.

Purification and properties of a halophilic catalase-peroxidase from Haloarcula marismortui.

P. Thibault, G. Zaccai, J. Gaillard, 1994, Biochimica et biophysica acta.

Excretion of laccase by sycamore (Acer pseudoplatanus L.) cells. Effects of a copper deficiency.

J. Gaillard, R. Bligny, R. Douce, 1986, The Biochemical journal.

The possible role of an [FeFe]-hydrogenase-like protein in the plant responses to changing atmospheric oxygen levels.

J. Fontecilla-Camps, J. Gaillard, P. Ratet, 2008, Journal of inorganic biochemistry.

Exploration of the diaphorase activity of neutrophil NADPH oxidase.

J. Gaillard, P. Vignais, A. Poinas, 2002, European journal of biochemistry.

Electron transfer across the O2- generating flavocytochrome b of neutrophils. Evidence for a transition from a low-spin state to a high-spin state of the heme iron component.

J. Gaillard, P. Vignais, P V Vignais, 1996, Biochemistry.

An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli.

M. Fontecave, J. Gaillard, P. Reichard, 1993, The Journal of biological chemistry.

EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: formation of porphyrin and tyrosyl radical intermediates.

J. Gaillard, A. Ivancich, H M Jouve, 1997, Biochemistry.

The [Fe-Fe]-Hydrogenase Maturation Protein HydF from Thermotoga maritima Is a GTPase with an Iron-Sulfur Cluster*

Serge Gambarelli, Marc Fontecave, Jacques Gaillard, 2006, Journal of Biological Chemistry.

Characterization and spectral properties of Proteus mirabilis PR catalase.

J. Gaillard, J. Pelmont, H. Jouve, 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire.

Electron transfer properties of iron-sulfur proteins.

J. Gaillard, P. Kyritsis, J. Moulis, 2000, Journal of inorganic biochemistry.

Characterization of a cytosolic aconitase in higher plant cells.

J. Gaillard, M. Nishimura, R. Douce, 1987, Plant physiology.

Electron paramagnetic resonance characterization of membrane bound iron-sulfur clusters and aconitase in plant mitochondria.

J. Gaillard, R. Douce, R. Brouquisse, 1986, Plant physiology.

Reduction of the Small Subunit of Ribonucleotide Reductase by Diimide: Evidence for the Formation of the Mixed‐Valence FeIIFeIII center

M. Fontecave, J. Gaillard, J. Latour, 1991 .

Assembly of 2Fe-2S and 4Fe-4S Clusters in the Anaerobic Ribonucleotide Reductase from Escherichia coli

M. Fontecave, J. Gaillard, T. Mattioli, 1999 .

NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters.

J. Gaillard, J. Moulis, J. Huber, 1995, Biochemistry.

Characterization ofaCytosolic Aconitase inHigher Plant Cells

J. Gaillard, Cellulaire Vegetale, 1987 .

J. Gaillard, J. Meyer, R. Kümmerle, 1999, Biochemistry.

Heterologous biosynthesis and characterization of the [2Fe-2S]-containing N-terminal domain of Clostridium pasteurianum hydrogenase.

J. Gaillard, J. Meyer, M. Lafferty, 1998, Biochemistry.

EPR EVIDENCE FOR A TYROSYL RADICAL INTERMEDIATE IN BOVINE LIVER CATALASE

J. Gaillard, A. Ivancich, H. Jouve, 1996 .

Electron Paramagnetic Resonance Characterization ofMembrane BoundIron-Sulfur Clusters andAconitase inPlant Mitochondria

J. Gaillard, 1986 .

A Second [2Fe-2S] Ferredoxin from Sphingomonas sp. Strain RW1 Can Function as an Electron Donor for the Dioxin Dioxygenase

K. Timmis, J. Armengaud, J. Gaillard, 2000, Journal of bacteriology.

Drosophila nuclear receptor E75 is a thiolate hemoprotein.

J. Fontecilla-Camps, J. Gaillard, F. Borel, 2006, Biochemistry.

Sequential assignments by 1H 2D NMR of oxidized ferredoxins from Clostridium pasteurianum and Clostridium acidurici

J. Gaillard, J. Moulis, Jacques Meyer, 1993 .

Characterization of a mutated rubredoxin with a cysteine ligand of the iron replaced by serine.

J. Gaillard, J. Meyer, M. Lutz, 1995, Biochemical and biophysical research communications.