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Fontecave M.
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http://hub.abes.fr/acs/periodical/jacsat/1995/volume_117/issue_43/101021ja00148a013/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_16/101021bi00016a012/authorship/4
http://hub.abes.fr/acs/periodical/inocaj/1993/volume_32/issue_22/101021ic00074a019/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_27/101021bi0498151/authorship/8
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_14/101021bi992090u/authorship/7
http://hub.abes.fr/acs/periodical/inocaj/2008/volume_47/issue_14/101021ic800534v/authorship/7
http://hub.abes.fr/acs/periodical/joceah/2005/volume_70/issue_1/101021jo048380k/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2002/volume_124/issue_18/101021ja025707v/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_12/101021bi001746c/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_23/101021bi002936q/authorship/5
http://hub.abes.fr/acs/periodical/inocaj/2003/volume_42/issue_16/101021ic0341338/authorship/6
http://hub.abes.fr/acs/periodical/inocaj/2007/volume_46/issue_13/101021ic7005502/authorship/4
http://hub.abes.fr/acs/periodical/joceah/2000/volume_65/issue_1/101021jo9908492/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_1/101021ja026690j/authorship/5
http://hub.abes.fr/acs/periodical/inocaj/2005/volume_44/issue_13/101021ic050167z/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2007/volume_46/issue_17/101021bi7000449/authorship/7
http://hub.abes.fr/acs/periodical/inocaj/2007/volume_46/issue_5/101021ic061625m/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_50/101021ja805032r/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_16/101021bi0023908/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_29/101021bi0122011/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_32/101021bi020344x/authorship/3
http://hub.abes.fr/acs/periodical/inocaj/2003/volume_42/issue_2/101021ic025866f/authorship/3
http://hub.abes.fr/acs/periodical/chreay/2003/volume_103/issue_6/101021cr020427j/authorship/1
http://hub.abes.fr/acs/periodical/inocaj/2006/volume_45/issue_11/101021ic060510f/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_3/101021bi00118a020/authorship/2
http://hub.abes.fr/springer/periodical/10534/1991/volume_4/issue_3/B943381937025DE1E053120B220A297A/authorship/1
http://hub.abes.fr/acs/periodical/joceah/1994/volume_59/issue_23/101021jo00102a028/authorship/3
http://hub.abes.fr/springer/periodical/10534/1994/volume_7/issue_1/B943381937F25DE1E053120B220A297A/authorship/1
http://hub.abes.fr/cairn/periodical/pes/2021/issue_pes386/D33BF7C3D9183F33E053120B220A1712/authorship/1
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New Thionitrites: Synthesis, Stability, and Nitric Oxide Generation
Alkane oxidation catalyzed by .mu.-oxo-bridged diferric complexes: a structure/reactivity correlation study
Biological Radical Sulfur Insertion Reactions
[Ni(xbsms)Ru(CO)2Cl2]: A Bioinspired Nickel−Ruthenium FunctionalModel of [NiFe] Hydrogenase
Very High-Field EPR Study of Glycyl Radical Enzymes
Hydrolysis of Phosphodiesters by Diiron Complexes: Design ofNonequivalent Iron Sites in Purple Acid Phosphatase Models
Proton Electroreduction Catalyzed by Cobaloximes: Functional Modelsfor Hydrogenases
Activation of Oxaziridines by Lewis Acids: Application inEnantioselective Sulfoxidation
“Chiral-at-Metal” Octahedral Ruthenium(II) Complexes with AchiralLigands: A New Type of Enantioselective Catalyst
Superoxide Reductase from Desulfoarculus baarsii: Reaction Mechanism and Roleof Glutamate 47 and Lysine 48 in Catalysis†
New Polydentate Ligand and Catalytic Properties of the Corresponding Ruthenium Complex During Sulfoxidation and Alkene Epoxidation
Redox-Dependent Structural Changes in the Superoxide Reductase fromDesulfoarculus baarsii and Treponema pallidum: A FTIR Study
2-(Trimethylsilyl)ethanethiol in NucleosideChemistry. A Short Route for PreparingThionucleosides and Their MethylDisulfides
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
Iron-Sulfur Center of Biotin Synthase and Lipoate Synthase
Activation of Class III Ribonucleotide Reductase by Flavodoxin: A ProteinRadical-Driven Electron Transfer to the Iron−Sulfur Center
Biotin Synthase Is a Pyridoxal Phosphate-Dependent Cysteine Desulfurase
MiaB, a Bifunctional Radical-S-Adenosylmethionine Enzyme Involved in theThiolation and Methylation of tRNA, Contains Two Essential [4Fe-4S] Clusters
Cobaloximes as Functional Models for Hydrogenases. 2. ProtonElectroreduction Catalyzed byDifluoroborylbis(dimethylglyoximato)cobalt(II) Complexes in OrganicMedia
Combined NMR and DFT Studies for the Absolute Configuration Elucidation of the Spore Photoproduct, a UV-Induced DNA Lesion
Ferric reductases or flavin reductases?
Chiral-at-Metal Ruthenium Complex as a Metalloligand for AsymmetricCatalysis
Activation of Class III Ribonucleotide Reductase from E. coli. The ElectronTransfer from the Iron−Sulfur Center to S-Adenosylmethionine
Identification of Iron(III) Peroxo Species in the Active Site of the SuperoxideReductase SOR from Desulfoarculus baarsii
Iron metabolism: The low-molecular-mass iron pool
Inhibition of Ribonucleotide Reductase by Nitric Oxide Derived from Thionitrites: Reversible Modifications of Both Subunits
Reduction of the small subunit of Escherichia coli ribonucleotide reductase by hydrazines and hydroxylamines
g-Values as a Probe of the Local Protein Environment: High-Field EPR of Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II
http://hub.abes.fr/cairn/periodical/pes/2021/issue_pes386/D33BF7C3D9183F33E053120B220A1712/w
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