E. P. Skaar, D. M. Tobiason, J. Quick, R. C. Judd, H. Weissbach et al., The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species, Proc. Natl Acad. Sci. USA, pp.10108-10113, 2002.
DOI : 10.1016/0092-8674(85)90143-6

?. Delano and W. L. , The PyMOL Molecular Graphics System, 2002.

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, Is a Disulfide Reductase That Can Recycle Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.254, issue.13, pp.12344-12350, 2005.
DOI : 10.1128/JB.184.7.2005-2018.2002

URL : https://hal.archives-ouvertes.fr/hal-01690798

J. Tapsall, Current concepts in the management of gonorrhoea, Expert Opinion on Pharmacotherapy, vol.73, issue.82, pp.147-157, 2002.
DOI : 10.1136/sti.77.3.218

A. Antignac, M. Ducos-galand, A. Guiyoule, R. Pirès, J. Alonso et al., Neisseria meningitidis Strains Isolated from Invasive Infections in France (1999-2002): Phenotypes and Antibiotic Susceptibility Patterns, Clinical Infectious Diseases, vol.45, issue.12, pp.912-920, 1999.
DOI : 10.1128/AAC.45.12.3625-3628.2001

V. Kapatral, I. Anderson, N. Ivanova, G. Reznik, T. Los et al., Genome Sequence and Analysis of the Oral Bacterium Fusobacterium nucleatum Strain ATCC 25586, Journal of Bacteriology, vol.184, issue.7, 2002.
DOI : 10.1128/JB.184.7.2005-2018.2002

H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat et al., The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235

A. Crow, R. M. Acheson, N. E. Le-brun, and A. Oubrie, Biosynthesis Protein ResA, Journal of Biological Chemistry, vol.3, issue.22, pp.23654-23660, 2004.
DOI : 10.1002/prot.340110407

R. A. Laskowsky, M. W. Macarthur, D. S. Moss, and J. M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, 1993.
DOI : 10.1107/S0021889892009944

&. N. Crystallography, system: a new software suite for macromolecular structure determination, Acta Crystallog. sect. D, vol.54, pp.905-921

C. Ramakrishnan and G. N. Ramachandran, Stereochemical Criteria for Polypeptide and Protein Chain Conformations, Biophysical Journal, vol.5, issue.6, pp.909-933, 1965.
DOI : 10.1016/S0006-3495(65)86759-5

H. Eklund, F. K. Gleason, and A. Holmgren, Structural and functional relations among thioredoxins of different species, Proteins: Structure, Function, and Genetics, vol.29, issue.1, pp.13-28, 1991.
DOI : 10.1016/B978-0-12-721955-4.50047-6

L. Holm and C. Sander, Protein Structure Comparison by Alignment of Distance Matrices, Journal of Molecular Biology, vol.233, issue.1, 1993.
DOI : 10.1006/jmbi.1993.1489

J. F. Gibrat, T. Madej, and S. H. Bryant, Surprising similarities in structure comparison, Current Opinion in Structural Biology, vol.6, issue.3, pp.377-385, 1996.
DOI : 10.1016/S0959-440X(96)80058-3

M. A. Edeling, L. W. Guddat, R. A. Fabianek, L. Thony-meyer, and J. L. Martin, Structure of CcmG/DsbE at 1.14 ?? Resolution, Structure, vol.10, issue.7, pp.973-979, 2002.
DOI : 10.1016/S0969-2126(02)00794-3

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, M. G. Gruetter, R. Glockshuber et al., Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation, Structure, vol.13, issue.7, pp.985-993, 2005.
DOI : 10.1016/j.str.2005.04.014

M. F. Jeng, A. P. Campbell, T. Begley, A. Holmgren, D. A. Case et al., High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin, Structure, vol.2, issue.9, pp.853-868, 1994.
DOI : 10.1016/S0969-2126(94)00086-7

K. A. Kerr, J. P. Ashmore, and T. F. Koetzle, -cysteine, Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, vol.31, issue.8, pp.2022-2026, 1975.
DOI : 10.1107/S0567740875006772

L. M. Gregoret, S. D. Rader, R. J. Fletterick, and F. E. Cohen, Hydrogen bonds involving sulfur atoms in proteins, Proteins: Structure, Function, and Genetics, vol.91, issue.2, pp.99-107, 1991.
DOI : 10.1002/prot.340090204

Y. Qi and N. V. Grishin, Structural classification of thioredoxin-like fold proteins, Proteins: Structure, Function, and Bioinformatics, vol.5, issue.2, pp.376-388, 2005.
DOI : 10.1016/S0022-2836(05)80360-2

E. Mö-ssner, M. Huber-wunderlich, and R. Glockshuber, thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases, Protein Science, vol.34, issue.5, pp.1233-1244, 1998.
DOI : 10.1042/bj3151001

U. Grauschopf, J. R. Winther, P. Korber, T. Zander, P. Dallinger et al., Why is DsbA such an oxidizing disulfide catalyst? Cell, pp.947-955, 1995.
DOI : 10.1016/0092-8674(95)90210-4

URL : https://doi.org/10.1016/0092-8674(95)90210-4

M. Huber-wunderlich and R. Glockshuber, A single dipeptide sequence modulates the redox properties of a whole enzyme family, Folding and Design, vol.3, issue.3, pp.161-171, 1998.
DOI : 10.1016/S1359-0278(98)00024-8

Q. Li, H. Hu, and G. Xu, Biochemical Characterization of the Thioredoxin Domain of Escherichia coli DsbE Protein Reveals a Weak Reductant, Biochemical and Biophysical Research Communications, vol.283, issue.4, pp.849-853, 2001.
DOI : 10.1006/bbrc.2001.4876

R. A. Fabianek, M. Huber-wunderlich, R. Glockshuber, P. Kü-nzler, H. Hennecke et al., -Type Cytochromes, Journal of Biological Chemistry, vol.178, issue.7, pp.4467-4473, 1997.
DOI : 10.1128/jb.178.21.6166-6172.1996

H. Loferer, M. Wunderlich, H. Hennecke, and R. Glockshuber, A Bacterial Thioredoxin-like Protein That Is Exposed to the Periplasm Has Redox Properties Comparable with Those of Cytoplasmic Thioredoxins, Journal of Biological Chemistry, vol.268, issue.44, pp.26178-26183, 1995.
DOI : 10.1111/j.1365-2958.1990.tb00576.x

L. S. Erlendsson, R. M. Acheson, L. Hederstedt, and N. E. Le-brun, Synthesis, Journal of Biological Chemistry, vol.1504, issue.20, pp.17852-17858, 2003.
DOI : 10.1016/S0005-2728(00)00265-6

A. Jacobi, M. Huber-wunderlich, J. Hennecke, and R. Glockshuber, Elimination of All Charged Residues in the Vicinity of the Active-site Helix of the Disulfide Oxidoreductase DsbA, Influence of electrostatic interactions on stability and redox properties, 1997.
DOI : 10.1016/0263-7855(96)00009-4

E. Moutevelis and J. Warwicker, Prediction of pKa and redox properties in the thioredoxin superfamily, Protein Science, vol.4, issue.10, pp.2744-2752, 2004.
DOI : 10.1110/ps.8.2.418

J. Qin, G. M. Clore, W. M. Poindexter-kennedy, J. R. Huth, and A. M. Gronenborn, Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF??B, Structure, vol.3, issue.3, pp.289-297, 1995.
DOI : 10.1016/S0969-2126(01)00159-9

J. Qin, G. M. Clore, W. P. Kennedy, J. Kuszewski, and A. M. Gronenborn, The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal, Structure, vol.4, issue.5, pp.613-620, 1996.
DOI : 10.1016/S0969-2126(96)00065-2

B. W. Lennon, C. H. Williams, &. Jr, and M. L. Ludwig, Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase, Science, vol.289, issue.5482, pp.1190-1194, 2000.
DOI : 10.1126/science.289.5482.1190

S. F. Altschul, T. L. Madden, A. A. Schäffer, J. Zhang, Z. Zhang et al., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Research, vol.25, issue.17, pp.3389-3402, 1997.
DOI : 10.1093/nar/25.17.3389

A. Bairoch, R. Apweiler, C. H. Wu, W. C. Barker, B. Boeckmann et al., The Universal Protein Resource (UniProt), Nucleic Acids Research, vol.33, issue.Database issue, pp.154-159, 2005.
DOI : 10.1093/nar/gki070

I. N. Shindyalov and P. E. Bourne, Protein structure alignment by incremental combinatorial extension (CE) of the optimal path, Protein Engineering Design and Selection, vol.11, issue.9, pp.739-747, 1998.
DOI : 10.1093/protein/11.9.739

G. J. Kleywegt and T. A. Jones, [27] Detecting folding motifs and similarities in protein structures, Methods Enzymol, vol.277, pp.525-545, 1997.
DOI : 10.1016/S0076-6879(97)77029-0

V. Ramakrishnan, J. T. Finch, V. Graziano, P. L. Lee, and R. M. Sweet, Crystal structure of globular domain of histone H5 and its implications for nucleosome binding, Nature, vol.362, issue.6417, pp.219-223, 1993.
DOI : 10.1038/362219a0

Z. Otwinowski and W. Minor, [20] Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol, vol.276, pp.307-326, 1997.
DOI : 10.1016/S0076-6879(97)76066-X

S. Panjikar, V. Parthasarathy, V. S. Lamzin, M. S. Weiss, and P. A. Tucker, : an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment, Acta Crystallographica Section D Biological Crystallography, vol.61, issue.4, pp.61-449, 2005.
DOI : 10.1107/S0907444905001307

K. Cowtan, Dm: an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on protein crystallography, pp.34-38, 1994.

G. J. Kleywegt and T. A. Jones, Template Convolution to Enhance or Detect Structural Features in Macromolecular Electron-Density Maps, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.2, pp.179-185, 1997.
DOI : 10.1107/S0907444996012279

A. Perrakis, R. J. Morris, and V. S. Lamzin, Automated protein model building combined with iterative structure refinement, Nature Structural Biology, vol.6, issue.5, pp.458-463, 1999.
DOI : 10.1038/8263

A. Vagin and A. Teplyakov, : an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6, 1997.
DOI : 10.1107/S0021889897006766

A. Roussel and C. Cambillau, The TURBO- FRODO Graphics Package Silicon Graphics Geometry Partners Directory, Silicon Graphics, vol.81, p.86, 1991.

R. Koradi, M. Billeter, and K. Wü-thrich, MOLMOL: A program for display and analysis of macromolecular structures, Journal of Molecular Graphics, vol.14, issue.1, pp.51-55, 1996.
DOI : 10.1016/0263-7855(96)00009-4

M. S. Weiss and R. Hilgenfeld, On the use of the merging R factor as a quality indicator for X-Ray data, 1997.

R. 1. Moskovitz, J. Balta, B. Monard, G. Ruiz-lopez, M. F. Antoine et al., 39062-70. 15 Theoretical study of the reduction mechanism of sulfoxides by thiols, J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory, vol.110, pp.7628-7664, 2005.

W. T. Lowther, N. Brot, H. Weissbach, B. W. Matthews, N. Coudevylle et al., Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme Solution structure and backbone dynamics of the reduced form and an oxidized form of E. coli methionine sulfoxide reductase A (MsrA): structural insight of the MsrA catalytic cycle, Biochemistry J Mol Biol, vol.39, issue.366, pp.13307-13319, 2000.

F. Tete-favier, D. Cobessi, S. Boschi-muller, S. Azza, G. Branlant et al., Crystal Structure of the Escherichia coli Peptide Methionine Sulphoxide Reductase at 1.9 ?? Resolution, Structure, vol.8, issue.11, pp.1167-78, 2000.
DOI : 10.1016/S0969-2126(00)00526-8

URL : https://hal.archives-ouvertes.fr/hal-00151127

A. B. Taylor, D. M. Benglis, . Jr, S. Dhandayuthapani, and P. J. Hart, Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine, J Biol Chem J Bacteriol, vol.282, issue.185, pp.3367-78, 2003.

A. Gand, M. Antoine, S. Boschi-muller, G. Branlant, W. Kabsch et al., Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase a Processing of X-ray Diffraction Data Collected in Oscillation Mode Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants The TURBO-FRODO Graphics Package Crystallographic refinement of ligand complexes, Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Silicon Graphics Geometry Partners Directory, pp.20484-91, 1991.

P. Gouet, X. Robert, and E. Courcelle, ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins, Nucleic Acids Research, vol.31, issue.13, pp.3320-3323, 2003.
DOI : 10.1093/nar/gkg556

URL : https://hal.archives-ouvertes.fr/hal-00314281

J. P. Abrahams, A. G. Et, and . Leslie, Methods used in the structure determination of bovine mitochondrial F1 ATPase, Acta Crystallographica Section D Biological Crystallography, vol.52, issue.1, pp.30-42, 1996.
DOI : 10.1107/S0907444995008754

E. Adman, K. D. Watenpaugh, and L. H. Jensennh, NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein., Proceedings of the National Academy of Sciences, vol.72, issue.12, pp.4854-4858, 1975.
DOI : 10.1073/pnas.72.12.4854

M. Antoine, A. Gand, S. Boschi-muller, and G. Branlant, MsrA Involved in the Chemical Catalysis of the Methionine Sulfoxide Reduction Step, Journal of Biological Chemistry, vol.19, issue.51, pp.39062-70, 2006.
DOI : 10.1021/ja01497a003

URL : https://hal.archives-ouvertes.fr/hal-01690778

B. Balta, G. Monard, M. F. Ruiz-lopez, M. Antoine, A. Gand et al., Theoretical Study of the Reduction Mechanism of Sulfoxides by Thiols, The Journal of Physical Chemistry A, vol.110, issue.24, pp.7628-7664, 2006.
DOI : 10.1021/jp0573036

URL : https://hal.archives-ouvertes.fr/hal-01690787

B. S. Berlett, E. R. Et, and . Stadtman, Protein Oxidation in Aging, Disease, and Oxidative Stress, Journal of Biological Chemistry, vol.60, issue.33, pp.20313-20319, 1997.
DOI : 10.1016/B978-0-12-152828-7.50010-X

D. J. Bigelow, T. C. Et, and . Squier, Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.121-155, 2005.
DOI : 10.1016/j.bbapap.2004.09.012

B. Biteau, J. Labarre, and M. B. Toledano, ATP-dependent reduction of cysteine???sulphinic acid by S. cerevisiae sulphiredoxin, Nature, vol.19, issue.6961, pp.980-984, 2003.
DOI : 10.1093/emboj/19.19.5157

J. L. Bos, The ras gene family and human carcinogenesis, Mutation Research/Reviews in Genetic Toxicology, vol.195, issue.3, pp.255-71, 1988.
DOI : 10.1016/0165-1110(88)90004-8

S. Boschi-muller, S. Azza, and G. Branlant, E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide, Protein Science, vol.275, issue.11, pp.2272-2281, 2001.
DOI : 10.1074/jbc.M000690200

URL : https://hal.archives-ouvertes.fr/hal-00155884

S. Boschi-muller, A. Olry, M. Antoine, and G. Branlant, The enzymology and biochemistry of methionine sulfoxide reductases, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.231-239, 2005.
DOI : 10.1016/j.bbapap.2004.09.016

URL : https://hal.archives-ouvertes.fr/hal-01690795

G. Bricogne, C. Vonrhein, C. Flensburg, M. Schiltz, and W. Paciorek, 2.0, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.11, pp.2023-2030, 2003.
DOI : 10.1107/S0907444903017694

N. Brot, J. F. Collet, L. C. Johnson, T. J. Jonsson, H. Weissbach et al., The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, J Biol Chem, 2006.

N. Brot, L. Weissbach, J. Werth, and H. Weissbach, Enzymatic reduction of protein-bound methionine sulfoxide., Proceedings of the National Academy of Sciences, vol.78, issue.4, pp.2155-2163, 1981.
DOI : 10.1073/pnas.78.4.2155

A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros et al., Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, pp.905-921, 1998.
DOI : 10.1107/S0907444998003254

P. Caldwell, D. C. Luk, H. Weissbach, and N. Brot, Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity., Proceedings of the National Academy of Sciences, vol.75, issue.11, pp.75-5349, 1978.
DOI : 10.1073/pnas.75.11.5349

G. Capitani, R. Rossmann, D. F. Sargent, M. G. Grutter, T. J. Richmond et al., Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties11Edited by R. Huber, Journal of Molecular Biology, vol.311, issue.5, pp.1037-1085, 2001.
DOI : 10.1006/jmbi.2001.4913

K. C. Cheng, D. S. Cahill, H. Kasai, S. Nishimura, and L. A. Loeb, 8-Hydroxyguanine, an abundant form of oxidative DNA damage, The Journal of biological chemistry, vol.267, issue.1, pp.166-72, 1992.

M. A. Ciorba, S. H. Heinemann, H. Weissbach, N. Brot, and T. Hoshi, Modulation of potassium channel function by methionine oxidation and reduction, Proceedings of the National Academy of Sciences, vol.15, issue.4, pp.94-9932, 1997.
DOI : 10.1016/0160-5402(86)90010-0

J. Cioslowski, S. T. Et, and . Mixon, Rigorous interpretation of electronic wave functions. 2. Electronic structures of selected phosphorus, sulfur, and chlorine fluorides and oxides, Inorganic Chemistry, vol.32, issue.15, pp.3209-3216, 1993.
DOI : 10.1021/ic00067a004

N. Coudevylle, M. Antoine, S. Boschi-muller, G. Branlant, and M. T. Cung, )H, (13)C and (15)N Resonance Assignment of an Oxidized form (Cys(51)-Cys(198)) of Methionine Sulfoxide Reductase A from Escherichia Coli, J Biomol NMR, issue.1, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00128266

N. Coudevylle, M. Antoine, S. Bouguet-bonnet, P. Mutzenhardt, S. Boschi-muller et al., Solution Structure and Backbone Dynamics of the Reduced Form and an Oxidized Form of E. coli Methionine Sulfoxide Reductase A (MsrA): Structural Insight of the MsrA Catalytic Cycle, Journal of Molecular Biology, vol.366, issue.1, pp.193-206, 2007.
DOI : 10.1016/j.jmb.2006.11.042

URL : https://hal.archives-ouvertes.fr/hal-00155884

K. Cowtan, Dm: An automated procedure for phase improvement by density modification, Joint CCP4 and ESF-EACBM Newsletter on protein crystallography, vol.31, pp.34-38, 1994.

A. Crow, A. R. , N. E. Le-brun, and A. Oubrie, Biosynthesis Protein ResA, Journal of Biological Chemistry, vol.3, issue.22, pp.23654-23660, 2004.
DOI : 10.1002/prot.340110407

K. J. Davies, Degradation of oxidized proteins by the 20S proteasome, Biochimie, vol.83, issue.3-4, pp.301-310, 2001.
DOI : 10.1016/S0300-9084(01)01250-0

J. P. De-magalhaes, J. A. Cabral, and D. Magalhaes, The Influence of Genes on the Aging Process of Mice: A Statistical Assessment of the Genetics of Aging, Genetics, vol.169, issue.1, pp.265-74, 2005.
DOI : 10.1534/genetics.104.032292

A. Delaunay, D. Pflieger, M. B. Barrault, J. Vinh, and M. B. Toledano, A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation, Cell, vol.111, issue.4, pp.471-81, 2002.
DOI : 10.1016/S0092-8674(02)01048-6

URL : https://hal.archives-ouvertes.fr/hal-01637040

A. Denicola, B. A. Freeman, M. Trujillo, and R. Radi, Peroxynitrite Reaction with Carbon Dioxide/Bicarbonate: Kinetics and Influence on Peroxynitrite-Mediated Oxidations, Archives of Biochemistry and Biophysics, vol.333, issue.1, pp.49-58, 1996.
DOI : 10.1006/abbi.1996.0363

S. Dhandayuthapani, M. W. Blaylock, C. M. Bebear, W. G. Rasmussen, and J. B. Baseman, Peptide Methionine Sulfoxide Reductase (MsrA) Is a Virulence Determinant in Mycoplasma genitalium, Journal of Bacteriology, vol.183, issue.19, pp.5645-50, 2001.
DOI : 10.1128/JB.183.19.5645-5650.2001

C. Dherin, J. P. Radicella, M. Dizdaroglu, and S. Boiteux, Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations, Nucleic Acids Research, vol.27, issue.20, pp.27-4001, 1999.
DOI : 10.1093/nar/27.20.4001

D. A. Dixon, D. Feller, C. G. Zhan, and J. S. Francisco, Decomposition Pathways of Peroxynitrous Acid:?? Gas-Phase and Solution Energetics, The Journal of Physical Chemistry A, vol.106, issue.13, pp.3191-3196, 2002.
DOI : 10.1021/jp013783z

J. A. Dobado, H. Martinez-garcia, J. M. Molina, M. R. Sundbergy, =. et al., ; X = O, S, Se; Z = O, S) Compounds, Journal of the American Chemical Society, vol.121, issue.13, pp.3156-3164, 1999.
DOI : 10.1021/ja9828206

S. Doublie, S. Tabor, A. M. Long, C. C. Richardson, and T. Ellenberger, Crystal structure of a bacteriophage T7 DNA replication complex at 2.2?????resolution, Nature, vol.276, issue.6664, pp.251-259, 1998.
DOI : 10.1016/S0076-6879(97)77028-9

T. Douglas, D. S. Daniel, B. K. Parida, C. Jagannath, and S. Dhandayuthapani, Methionine Sulfoxide Reductase A (MsrA) Deficiency Affects the Survival of Mycobacterium smegmatis within Macrophages, Journal of Bacteriology, vol.186, issue.11, pp.3590-3598, 2004.
DOI : 10.1128/JB.186.11.3590-3598.2004

J. R. Durrant, L. B. Giorgi, J. Barber, D. R. Klug, and G. Porter, Characterisation of triplet states in isolated Photosystem II reaction centres: Oxygen quenching as a mechanism for photodamage, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1017, issue.2, pp.167-175, 1990.
DOI : 10.1016/0005-2728(90)90148-W

M. A. Edeling, L. W. Guddat, R. A. Fabianek, L. Tho-?-ny-meyer, and J. L. Martin, Structure of CcmG/DsbE at 1.14 ?? Resolution, Structure, vol.10, issue.7, pp.973-979, 2002.
DOI : 10.1016/S0969-2126(02)00794-3

P. Emsley, K. Et, and . Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

M. D. Evans, M. Dizdaroglu, and M. S. Cooke, Oxidative DNA damage and disease: induction, repair and significance, Mutation Research/Reviews in Mutation Research, vol.567, issue.1, pp.1-61, 2004.
DOI : 10.1016/j.mrrev.2003.11.001

B. Ezraty, L. Aussel, and F. Barras, Methionine sulfoxide reductases in prokaryotes, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.221-230, 2005.
DOI : 10.1016/j.bbapap.2004.08.017

B. Ezraty, R. Grimaud, M. Hassouni, D. Moinier, and F. Barras, Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli, The EMBO Journal, vol.13, issue.8, pp.1868-77, 2004.
DOI : 10.1038/sj.emboj.7600172

URL : https://hal.archives-ouvertes.fr/hal-01614790

R. A. Fabianek, M. Huber-wunderlich, R. Glockshuber, P. Künzler, H. Hennecke et al., -Type Cytochromes, Journal of Biological Chemistry, vol.178, issue.7, pp.4467-4473, 1997.
DOI : 10.1128/jb.178.21.6166-6172.1996

N. Fedoroff, Redox Regulatory Mechanisms in Cellular Stress Responses, Annals of Botany, vol.98, issue.2, pp.289-300, 2006.
DOI : 10.1242/jcs.01126

D. A. Ferrington, H. Sun, K. K. Murray, J. Costa, T. D. Williams et al., Selective Degradation of Oxidized Calmodulin by the 20 S Proteasome, Journal of Biological Chemistry, vol.266, issue.2, pp.937-980, 2001.
DOI : 10.1038/227680a0

R. A. Floyd, The role of 8-hydroxyguanine in carcinogenesis, Carcinogenesis, vol.11, issue.9, pp.1447-50, 1990.
DOI : 10.1093/carcin/11.9.1447

P. Fortini, E. Parlanti, O. M. Sidorkina, J. Laval, and E. Dogliotti, The Type of DNA Glycosylase Determines the Base Excision Repair Pathway in Mammalian Cells, Journal of Biological Chemistry, vol.76, issue.21, pp.15230-15236, 1999.
DOI : 10.1073/pnas.95.9.5061

B. Friguet, Oxidized protein degradation and repair in ageing and oxidative stress, FEBS Letters, vol.102, issue.12, pp.2910-2916, 2006.
DOI : 10.1073/pnas.0501519102

B. Friguet, E. R. Stadtman, and L. I. Szweda, Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease, J Biol Chem, vol.269, pp.21639-21643, 1994.

B. Friguet, L. I. Et, and . Szweda, Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein, FEBS Letters, vol.405, issue.1, pp.21-25, 1997.
DOI : 10.1016/S0014-5793(97)00148-8

M. Fuangthong, J. D. Et, and . Helmann, The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative, Proceedings of the National Academy of Sciences, vol.179, issue.23, pp.6690-6695, 2002.
DOI : 10.1128/jb.179.23.7420-7425.1997

S. P. Gabbita, M. Y. Aksenov, M. A. Lovell, and W. R. Markesbery, Decrease in Peptide Methionine Sulfoxide Reductase in Alzheimer's Disease Brain, Journal of Neurochemistry, vol.18, issue.4, pp.1660-1666, 1999.
DOI : 10.1016/0891-5849(94)00158-G

A. Gand, M. Antoine, S. Boschi-muller, and G. Branlant, Characterization of the Amino Acids Involved in Substrate Specificity of Methionine Sulfoxide Reductase A, Journal of Biological Chemistry, vol.7, issue.28, pp.20484-91, 2007.
DOI : 10.1016/j.jmb.2006.11.042

URL : https://hal.archives-ouvertes.fr/hal-01690658

J. Gao, Y. Yao, and T. C. Squier, Oxidatively Modified Calmodulin Binds to the Plasma Membrane Ca-ATPase in a Nonproductive and Conformationally Disordered Complex, Biophysical Journal, vol.80, issue.4, pp.1791-801, 2001.
DOI : 10.1016/S0006-3495(01)76149-8

J. F. Gibrat, T. Madej, and S. H. Bryant, Surprising similarities in structure comparison, Current Opinion in Structural Biology, vol.6, issue.3, pp.377-385, 1996.
DOI : 10.1016/S0959-440X(96)80058-3

C. B. Glaser, G. Yamin, V. N. Uversky, and A. L. Fink, Methionine oxidation, ??-synuclein and Parkinson's disease, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.157-69, 2005.
DOI : 10.1016/j.bbapap.2004.10.008

P. Gouet, X. Robert, and E. Courcelle, ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins, Nucleic Acids Research, vol.31, issue.13, pp.31-3320, 2003.
DOI : 10.1093/nar/gkg556

URL : https://hal.archives-ouvertes.fr/hal-00314281

C. W. Goulding, M. I. Apostol, S. Gleiter, A. Parseghian, J. Bardwell et al., Gram-positive DsbE Proteins Function Differently from Gram-negative DsbE Homologs, Journal of Biological Chemistry, vol.153, issue.5, pp.3516-3540, 2004.
DOI : 10.1016/S0923-2508(01)01278-5

U. Grauschopf, J. R. Winther, P. Korber, T. Zander, P. Dallinger et al., Why is DsbA such an oxidizing disulfide catalyst?, Cell, vol.83, issue.6, pp.947-955, 1995.
DOI : 10.1016/0092-8674(95)90210-4

L. M. Gregoret, S. D. Rader, R. J. Fletterick, and F. E. Cohen, Hydrogen bonds involving sulfur atoms in proteins, Proteins: Structure, Function, and Genetics, vol.91, issue.2, pp.99-107, 1991.
DOI : 10.1002/prot.340090204

R. Grimaud, B. Ezraty, J. K. Mitchell, D. Lafitte, C. Briand et al., Repair of Oxidized Proteins, Journal of Biological Chemistry, vol.180, issue.52, pp.48915-48935, 2001.
DOI : 10.1038/35051615

URL : https://hal.archives-ouvertes.fr/hal-01614791

I. C. Gunesekere, C. M. Kahler, C. S. Ryan, L. A. Snyder, N. J. Saunders et al., Ecf, an Alternative Sigma Factor from Neisseria gonorrhoeae, Controls Expression of msrAB, Which Encodes Methionine Sulfoxide Reductase, Journal of Bacteriology, vol.188, issue.10, pp.3463-3472, 2006.
DOI : 10.1128/JB.188.10.3463-3469.2006

K. Z. Guyton, T. W. Et, and . Kensler, Oxidative mechanisms in carcinogenesis, British Medical Bulletin, vol.49, issue.3, pp.523-567, 1993.
DOI : 10.1093/oxfordjournals.bmb.a072628

Q. Hao, : a program to determine absolute configuration and evaluate anomalous scatterer substructure, Journal of Applied Crystallography, vol.37, issue.3, pp.498-499, 2004.
DOI : 10.1107/S0021889804008696

M. E. Hassouni, J. P. Chambost, D. Expert, F. Van-gijsegem, and F. Barras, The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi, Proceedings of the National Academy of Sciences, vol.93, issue.19, pp.887-92, 1999.
DOI : 10.1073/pnas.93.19.10268

L. Holm, C. Et, and . Sander, Protein Structure Comparison by Alignment of Distance Matrices, Journal of Molecular Biology, vol.233, issue.1, pp.123-138, 1993.
DOI : 10.1006/jmbi.1993.1489

G. Hoppe, Y. C. Chai, J. W. Crabb, and J. Sears, Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone, Experimental Eye Research, vol.78, issue.6, pp.1085-1092, 2004.
DOI : 10.1016/j.exer.2004.02.001

I. C. Hsu, R. A. Metcalf, T. Sun, J. A. Welsh, N. J. Wang et al., Mutational hot spot in the p53 gene in human hepatocellular carcinomas, Nature, vol.350, issue.6317, pp.427-435, 1991.
DOI : 10.1038/350427a0

M. Huber-wunderlich, R. Et, and . Glockshuber, A single dipeptide sequence modulates the redox properties of a whole enzyme family, Folding and Design, vol.3, issue.3, pp.161-171, 1998.
DOI : 10.1016/S1359-0278(98)00024-8

A. Jacobi, M. Huber-wunderlich, J. Hennecke, and R. Glockshuber, Elimination of All Charged Residues in the Vicinity of the Active-site Helix of the Disulfide Oxidoreductase DsbA, Journal of Biological Chemistry, vol.15, issue.35, pp.21692-21699, 1997.
DOI : 10.1016/0263-7855(96)00009-4

M. F. Jeng, A. P. Campbell, T. Begley, A. Holmgren, D. A. Case et al., High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin, Structure, vol.2, issue.9, pp.853-868, 1994.
DOI : 10.1016/S0969-2126(94)00086-7

T. Jung, N. Bader, and T. Grune, Oxidized proteins: Intracellular distribution and recognition by the proteasome, Archives of Biochemistry and Biophysics, vol.462, issue.2, pp.231-238, 2007.
DOI : 10.1016/j.abb.2007.01.030

W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, Journal of Applied Crystallography, vol.26, issue.6, pp.795-800, 1993.
DOI : 10.1107/S0021889893005588

A. Kanayama, J. Inoue, Y. Sugita-konishi, M. Shimizu, and Y. Miyamoto, Oxidation of I??B?? at Methionine 45 Is One Cause of Taurine Chloramine-induced Inhibition of NF-??B Activation, Journal of Biological Chemistry, vol.72, issue.27, pp.24049-56, 2002.
DOI : 10.1074/jbc.272.42.26247

M. Kantorow, J. R. Hawse, T. L. Cowell, S. Benhamed, G. O. Pizarro et al., Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress, Proceedings of the National Academy of Sciences, vol.841, issue.3, pp.9654-9663, 2004.
DOI : 10.1016/0304-4165(85)90065-0

B. Kauffmann, F. Favier, A. Olry, S. Boschi-muller, P. Carpentier et al., PILB, Acta Crystallographica Section D Biological Crystallography, vol.58, issue.9, pp.1467-1476, 2002.
DOI : 10.1107/S0907444902010570

URL : https://hal.archives-ouvertes.fr/hal-00089617

B. Kauffmann, Etudes cristallographiques d'enzymes impliquées dans les mécanismes de défense contre le stress oxydant : les peptides méthionine sulfoxyde réductases et la NADH rubrédoxine oxydoréductase, Thèse, Biologie structurale moléculaire et cellulaire, 2003.

N. Keren, I. Ohad, A. W. Rutherford, F. Drepper, and A. Krieger-liszkay, Inhibition of Photosystem II activity by saturating single turnover flashes in calcium-depleted and active Photosystem II, Photosynthesis Research, vol.63, issue.3, pp.209-225, 2000.
DOI : 10.1023/A:1006435530817

K. A. Kerr, J. P. Ashmore, and T. F. Koetzle, -cysteine, Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, vol.31, issue.8, pp.2022-2026, 1975.
DOI : 10.1107/S0567740875006772

H. K. Khor, M. T. Fisher, and C. Schoneich, ), Journal of Biological Chemistry, vol.269, issue.19, pp.19486-93, 2004.
DOI : 10.1007/BF01888363

H. Y. Kim and V. N. Gladyshev, Different Catalytic Mechanisms in Mammalian Selenocysteine- and Cysteine-Containing Methionine-R-Sulfoxide Reductases, PLoS Biology, vol.50, issue.12, p.375, 2005.
DOI : 10.1371/journal.pbio.0030375.sg001

H. Y. Kim and V. N. Gladyshev, Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases, BMC Molecular Biology, vol.7, issue.1, p.11, 2006.
DOI : 10.1186/1471-2199-7-11

S. O. Kim, K. Merchant, R. Nudelman, W. F. Beyer, J. et al., OxyR, Cell, vol.109, issue.3, pp.383-96, 2002.
DOI : 10.1016/S0092-8674(02)00723-7

URL : https://doi.org/10.1016/s0092-8674(02)00723-7

Y. M. Kim, C. A. Bombeck, and T. R. Billiar, Nitric Oxide as a Bifunctional Regulator of Apoptosis, Circulation Research, vol.84, issue.3, pp.253-259, 1999.
DOI : 10.1161/01.RES.84.3.253

G. J. Kleywegt, Use of Non-crystallographic Symmetry in Protein Structure Refinement, Acta Crystallographica Section D Biological Crystallography, vol.52, issue.4, pp.842-57, 1996.
DOI : 10.1107/S0907444995016477

G. J. Kleywegt, Crystallographic refinement of ligand complexes, Acta Crystallographica Section D Biological Crystallography, vol.63, issue.1, pp.94-100, 2007.
DOI : 10.1107/S0907444906022657

G. J. Kleywegt, T. A. Et, and . Jones, Template Convolution to Enhance or Detect Structural Features in Macromolecular Electron-Density Maps, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.2, pp.179-85, 1997.
DOI : 10.1107/S0907444996012279

A. Koc, A. P. Gasch, J. C. Rutherford, H. Y. Kim, and V. N. Gladyshev, Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging, Proceedings of the National Academy of Sciences, vol.91, issue.7, pp.7999-8004, 2004.
DOI : 10.1016/S0092-8674(00)80493-6

P. V. Konarev, M. V. Petoukhov, V. V. Volkov, and D. I. Svergun, 2.1, a program package for small-angle scattering data analysis, Journal of Applied Crystallography, vol.39, issue.2, pp.277-286, 2006.
DOI : 10.1107/S0021889806004699

G. V. Kryukov, R. A. Kumar, A. Koc, Z. Sun, and V. N. Gladyshev, Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase, Proceedings of the National Academy of Sciences, vol.147, issue.11, pp.99-4245, 2002.
DOI : 10.1099/00221287-147-11-3037

Y. Kuchino, F. Mori, H. Kasai, H. Inoue, S. Iwai et al., Misreading of DNA templates containing 8-hydroxydeoxyguanosine at the modified base and at adjacent residues, Nature, vol.327, issue.6117, pp.77-86, 1987.
DOI : 10.1038/327077a0

R. A. Kumar, A. Koc, R. L. Cerny, and V. N. Gladyshev, -sulfoxide Reductase, Journal of Biological Chemistry, vol.9, issue.40, pp.37527-37562, 2002.
DOI : 10.1074/jbc.M112350200

H. M. Lander, An essential role for free radicals and derived species in signal transduction., The FASEB Journal, vol.11, issue.2, pp.118-142, 1997.
DOI : 10.1096/fasebj.11.2.9039953

G. N. Landis, J. Et, and . Tower, Superoxide dismutase evolution and life span regulation, Mechanisms of Ageing and Development, vol.126, issue.3, pp.365-79, 2005.
DOI : 10.1016/j.mad.2004.08.012

R. A. Laskowsky, M. W. Macarthur, D. S. Moss, and J. M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.282-291, 1993.
DOI : 10.1107/S0021889892009944

L. Page, F. , A. Guy, J. Cadet, A. Sarasin et al., Repair and mutagenic potency of 8-oxoG:A and 8-oxoG:C base pairs in mammalian cells, Nucleic Acids Research, vol.26, issue.5, pp.1276-81, 1998.
DOI : 10.1093/nar/26.5.1276

C. M. Lee, M. E. Lopez, R. Weindruch, and J. M. Aiken, Association of age-related mitochondrial abnormalities with skeletal muscle fiber atrophy, Free Radical Biology and Medicine, vol.25, issue.8, pp.964-72, 1998.
DOI : 10.1016/S0891-5849(98)00185-3

J. W. Lee, N. V. Gordiyenko, M. Marchetti, N. Tserentsoodol, D. Sagher et al., Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina, Experimental Eye Research, vol.82, issue.5, pp.816-843, 2006.
DOI : 10.1016/j.exer.2005.10.003

B. W. Lennon, C. H. Williams, J. Et, and M. L. Ludwig, Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase, Science, vol.289, issue.5482, pp.1190-1194, 2000.
DOI : 10.1126/science.289.5482.1190

R. L. Levine, L. Mosoni, B. S. Berlett, and E. R. Stadtman, Methionine residues as endogenous antioxidants in proteins, Proceedings of the National Academy of Sciences, vol.177, issue.3, pp.15036-15076, 1996.
DOI : 10.1016/0022-2836(84)90298-5

Q. Li, H. Y. Hu, and G. J. Xu, Biochemical Characterization of the Thioredoxin Domain of Escherichia coli DsbE Protein Reveals a Weak Reductant, Biochemical and Biophysical Research Communications, vol.283, issue.4, pp.849-853, 2001.
DOI : 10.1006/bbrc.2001.4876

H. Loferer, M. Wunderlich, H. Hennecke, and R. Glockshuber, A Bacterial Thioredoxin-like Protein That Is Exposed to the Periplasm Has Redox Properties Comparable with Those of Cytoplasmic Thioredoxins, Journal of Biological Chemistry, vol.268, issue.44, pp.26178-26183, 1995.
DOI : 10.1111/j.1365-2958.1990.tb00576.x

W. T. Lowther, H. Weissbach, F. Etienne, N. Brot, and B. W. Matthews, The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB, Nature Structural Biology, vol.9, issue.5, pp.348-52, 2002.
DOI : 10.1038/nsb783

S. V. Lymar, J. K. Et, and . Hurst, Rapid reaction between peroxonitrite ion and carbon dioxide: Implications for biological activity, Journal of the American Chemical Society, vol.117, issue.34, pp.8867-8868, 1995.
DOI : 10.1021/ja00139a027

M. A. Marchetti, W. Lee, T. L. Cowell, T. M. Wells, H. Weissbach et al., Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells, Experimental Eye Research, vol.83, issue.5, pp.1281-1287, 2006.
DOI : 10.1016/j.exer.2006.07.005

E. Mariani, M. C. Polidori, A. Cherubini, and P. Mecocci, Oxidative stress in brain aging, neurodegenerative and vascular diseases: An overview, Journal of Chromatography B, vol.827, issue.1, pp.65-75, 2005.
DOI : 10.1016/j.jchromb.2005.04.023

M. A. Marletta, Nitric oxide synthase structure and mechanism, J Biol Chem, vol.268, issue.17, pp.12231-12235, 1993.

J. M. Mates, C. Perez-gomez, and I. Nunez-de-castro, Antioxidant enzymes and human diseases, Clinical Biochemistry, vol.32, issue.8, pp.595-603, 1999.
DOI : 10.1016/S0009-9120(99)00075-2

J. M. Mccord, I. Et, and . Fridovich, Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J Biol Chem, vol.244, issue.22, pp.6049-55, 1969.

G. Merenyi, J. Lind, G. Czapski, and S. Goldstein, The decomposition of peroxynitrite does not yield nitroxyl anion and singlet oxygen, Proceedings of the National Academy of Sciences, vol.121, issue.6, pp.8216-8224, 2000.
DOI : 10.1021/ja9921165

M. Mohri, P. S. Reinach, A. Kanayama, M. Shimizu, J. Moskovitz et al., Suppression of the TNFalpha-induced increase in IL-1alpha expression by hypochlorite in human corneal epithelial cells, Invest Ophthalmol Vis Sci, vol.43, issue.10, pp.3190-3195, 2002.

H. M. Morrison, D. Burnett, and R. A. Stockley, -Proteinase Inhibitor, Biological Chemistry Hoppe-Seyler, vol.126, issue.1, pp.371-379, 1986.
DOI : 10.1016/0006-291X(85)90602-3

J. Moskovitz, Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.213-222, 2005.
DOI : 10.1016/j.bbapap.2004.09.003

J. Moskovitz, S. Bar-noy, W. M. Williams, J. Requena, B. S. Berlett et al., Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals, Proceedings of the National Academy of Sciences, vol.60, issue.5150, pp.98-12920, 2001.
DOI : 10.1126/science.8108730

J. Moskovitz, J. M. Poston, B. S. Berlett, N. J. Nosworthy, R. Szczepanowski et al., Identification and Characterization of a Putative Active Site for Peptide Methionine Sulfoxide Reductase (MsrA) and Its Substrate Stereospecificity, Journal of Biological Chemistry, vol.43, issue.19, pp.14167-72, 2000.
DOI : 10.1016/S0014-5793(99)00888-1

J. Moskovitz, V. K. Singh, J. Requena, B. J. Wilkinson, R. K. Jayaswal et al., Purification and Characterization of Methionine Sulfoxide Reductases from Mouse and Staphylococcus aureus and Their Substrate Stereospecificity, Biochemical and Biophysical Research Communications, vol.290, issue.1, pp.62-67, 2002.
DOI : 10.1006/bbrc.2001.6171

E. Mössner, M. Huber-wunderlich, and R. Glockshuber, thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases, Protein Science, vol.34, issue.5, pp.1233-1244, 1998.
DOI : 10.1042/bj3151001

E. Moutevelis, J. Et, and . Warwicker, Prediction of pKa and redox properties in the thioredoxin superfamily, Protein Science, vol.4, issue.10, pp.2744-52, 2004.
DOI : 10.1110/ps.8.2.418

F. L. Muller, Y. Liu, and H. Van-remmen, Complex III Releases Superoxide to Both Sides of the Inner Mitochondrial Membrane, Journal of Biological Chemistry, vol.258, issue.47, pp.49064-73, 2004.
DOI : 10.1074/jbc.274.48.33931

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

A. R. Mushegian, E. V. Et, and . Koonin, A minimal gene set for cellular life derived by comparison of complete bacterial genomes., Proceedings of the National Academy of Sciences, vol.93, issue.19, pp.10268-73, 1996.
DOI : 10.1073/pnas.93.19.10268

F. Neiers, A. Kriznik, S. Boschi-muller, and G. Branlant, Evidence for a New Sub-class of Methionine Sulfoxide Reductases B with an Alternative Thioredoxin Recognition Signature, Journal of Biological Chemistry, vol.9, issue.41, pp.42462-42470, 2004.
DOI : 10.1073/pnas.072603099

URL : https://hal.archives-ouvertes.fr/hal-01636385

F. Neiers, S. Sonkaria, A. Olry, S. Boschii-muller, and G. Branlant, Characterization of the amino acids from neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step, J Biol Chem, 2007.
URL : https://hal.archives-ouvertes.fr/hal-01690652

F. Neiers, Mécanisme, catalyse et spécificité structurale des méthionine sulfoxyde réductases de classe B et la protéine PilB de Neisseria meningitidis, Thèse, Enzymologie moléculaire, 2007.

T. Ogino, M. Hosako, K. Hiramatsu, M. Omori, M. Ozaki et al., Oxidative modification of I??B by monochloramine inhibits tumor necrosis factor ??-induced NF-??B activation, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1746, issue.2, pp.135-177, 2005.
DOI : 10.1016/j.bbamcr.2005.10.005

A. Olry, S. Boschi-muller, H. Yu, D. Burnel, and G. Branlant, -sulfoxide reductases B, Protein Science, vol.376, issue.11, pp.2828-2865, 2005.
DOI : 10.1038/376788a0

L. P. Olson, M. D. Bartberger, and K. N. Houk, Species, Journal of the American Chemical Society, vol.125, issue.13, pp.3999-4006, 2003.
DOI : 10.1021/ja029619m

URL : https://hal.archives-ouvertes.fr/hal-01268762

Z. Otwinowski, W. Et, and . Minor, [20] Processing of X-ray diffraction data collected in oscillation mode, Methods in Enzymology, vol.276, pp.307-326, 1997.
DOI : 10.1016/S0076-6879(97)76066-X

P. Pal, R. , D. B. Oien, F. Y. Ersen, and J. Moskovitz, Elevated levels of brain-pathologies associated with neurodegenerative diseases in the methionine sulfoxide reductase A knockout mouse, Experimental Brain Research, vol.278, issue.4, pp.765-74, 2007.
DOI : 10.1016/j.bbapap.2004.09.009

S. Panjikar, V. Parthasarathy, V. S. Lamzin, M. S. Weiss, and P. A. Tucker, : an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment, Acta Crystallographica Section D Biological Crystallography, vol.61, issue.4, pp.449-457, 2005.
DOI : 10.1107/S0907444905001307

W. Panmanee, P. Vattanaviboon, L. B. Poole, and S. Mongkolsuk, Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress, Journal of Bacteriology, vol.188, issue.4, pp.1389-95, 2006.
DOI : 10.1128/JB.188.4.1389-1395.2006

N. S. Pannu, R. J. Et, and . Read, The application of multivariate statistical techniques improves single-wavelength anomalous diffraction phasing, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.1, pp.22-27, 2004.
DOI : 10.1107/S0907444903020808

A. Perrakis, R. Morris, and V. S. Lamzin, Automated protein model building combined with iterative structure refinement, Nature Structural Biology, vol.6, issue.5, pp.458-63, 1999.
DOI : 10.1038/8263

M. V. Petoukhov, D. I. Et, and . Svergun, Global Rigid Body Modeling of Macromolecular Complexes against Small-Angle Scattering Data, Biophysical Journal, vol.89, issue.2, pp.1237-50, 2005.
DOI : 10.1529/biophysj.105.064154

C. R. Picot, M. Perichon, K. C. Lundberg, B. Friguet, L. I. Szweda et al., Alterations in mitochondrial and cytosolic methionine sulfoxide reductase activity during cardiac ischemia and reperfusion, Experimental Gerontology, vol.41, issue.7, pp.663-670, 2006.
DOI : 10.1016/j.exger.2006.03.011

L. Pirkkala, P. Nykanen, and L. Sistonen, Roles of the heat shock transcription factors in regulation of the heat shock response and beyond, The FASEB Journal, vol.15, issue.7, pp.1118-1149, 2001.
DOI : 10.1046/j.1432-1327.1998.2550703.x

W. A. Pryor, K. N. Houk, C. S. Foote, J. M. Fukuto, L. J. Ignarro et al., Free radical biology and medicine: it's a gas, man!, American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, vol.291, issue.3, pp.491-511, 2006.
DOI : 10.1021/jp048661w

Y. Qi, N. V. Et, and . Grishin, Structural classification of thioredoxin-like fold proteins, Proteins: Structure, Function, and Bioinformatics, vol.5, issue.2, pp.376-388, 2005.
DOI : 10.1016/S0022-2836(05)80360-2

J. Qin, G. M. Clore, W. P. Kennedy, J. Kuszewski, and A. M. Gronenborn, The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal, Structure, vol.4, issue.5, pp.613-620, 1996.
DOI : 10.1016/S0969-2126(96)00065-2

J. Qin, G. M. Clore, W. M. Poindexter-kennedy, J. R. Huth, and A. M. Gronenborn, Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF??B, Structure, vol.3, issue.3, pp.289-297, 1995.
DOI : 10.1016/S0969-2126(01)00159-9

M. Quinonez, M. Difranco, and F. Gonzalez, Involvement of Methionine Residues in the Fast Inactivation Mechanism of the Sodium Current from Toad Skeletal Muscle Fibers, Journal of Membrane Biology, vol.169, issue.2, pp.83-90, 1999.
DOI : 10.1007/s002329900520

F. M. Ranaivoson, B. Kauffmann, F. Neiers, J. Wu, S. Boschi-muller et al., The X-ray Structure of the N-terminal Domain of PILB from Neisseria meningitidis Reveals a Thioredoxin-fold, Journal of Molecular Biology, vol.358, issue.2, pp.443-54, 2006.
DOI : 10.1016/j.jmb.2006.02.025

URL : https://hal.archives-ouvertes.fr/hal-00089656

A. E. Reed, P. V. Et, and . Schleyer, Chemical bonding in hypervalent molecules. The dominance of ionic bonding and negative hyperconjugation over d-orbital participation, Journal of the American Chemical Society, vol.112, issue.4, pp.1434-1445, 1990.
DOI : 10.1021/ja00160a022

S. G. Rhee, H. Z. Chae, and K. Kim, Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling, Free Radical Biology and Medicine, vol.38, issue.12, pp.1543-52, 2005.
DOI : 10.1016/j.freeradbiomed.2005.02.026

N. Rouhier, B. Kauffmann, F. Tete-favier, P. Palladino, P. Gans et al., Functional and Structural Aspects of Poplar Cytosolic and Plastidial Type A Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.19, issue.5, pp.3367-78, 2007.
DOI : 10.1074/jbc.M307471200

URL : https://hal.archives-ouvertes.fr/hal-00207696

N. Rouhier, C. V. Santos, L. Tarrago, and P. Rey, Plant methionine sulfoxide reductase A and B multigenic families, Photosynthesis Research, vol.136, issue.235, pp.1-16, 2006.
DOI : 10.1016/j.bbapap.2004.09.001

A. Roussel and C. Cambillau, The TURBO-FRODO Graphics Package. Silicon Graphics Geometry Partners Directory. Mountain View, USA, Silicon Graphics, p.86, 1991.

H. Ruan, X. D. Tang, M. L. Chen, M. L. Joiner, G. Sun et al., High-quality life extension by the enzyme peptide methionine sulfoxide reductase, Proceedings of the National Academy of Sciences, vol.292, issue.5514, pp.2748-53, 2002.
DOI : 10.1126/science.1057987

C. A. Sacksteder, J. E. Whittier, Y. Xiong, J. Li, N. A. Galeva et al., Tertiary Structural Rearrangements upon Oxidation of Methionine145 in Calmodulin Promotes Targeted Proteasomal Degradation, Biophysical Journal, vol.91, issue.4, pp.1480-93, 2006.
DOI : 10.1529/biophysj.106.086033

K. U. Schallreuter, K. Rubsam, B. Chavan, C. Zothner, J. M. Gillbro et al., Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus, Biochemical and Biophysical Research Communications, vol.342, issue.1, pp.145-52, 2006.
DOI : 10.1016/j.bbrc.2006.01.124

C. Schoneich, Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.111-120, 2005.
DOI : 10.1016/j.bbapap.2004.09.009

C. Schoneich, D. Pogocki, G. L. Hug, and K. Bobrowski, Free Radical Reactions of Methionine in Peptides:?? Mechanisms Relevant to ??-Amyloid Oxidation and Alzheimer's Disease, Journal of the American Chemical Society, vol.125, issue.45, pp.13700-13713, 2003.
DOI : 10.1021/ja036733b

V. S. Sharov, D. A. Ferrington, T. C. Squier, and C. Schoneich, Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase, FEBS Letters, vol.333, issue.3, pp.247-50, 1999.
DOI : 10.1006/abbi.1996.0370

M. D. Shelton, P. B. Chock, and J. J. , -Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation, Antioxidants & Redox Signaling, vol.7, issue.3-4, pp.3-4, 2005.
DOI : 10.1089/ars.2005.7.348

R. Shringarpure, T. Grune, J. Mehlhase, and K. J. Davies, Ubiquitin Conjugation Is Not Required for the Degradation of Oxidized Proteins by Proteasome, Journal of Biological Chemistry, vol.269, issue.1, pp.311-318, 2003.
DOI : 10.1042/bj3070297

V. K. Singh, J. Et, and . Moskovitz, Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress, Microbiology, vol.149, issue.10, pp.2739-2747, 2003.
DOI : 10.1099/mic.0.26442-0

E. P. Skaar, D. M. Tobiason, J. Quick, R. C. Judd, H. Weissbach et al., The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species, Proceedings of the National Academy of Sciences, vol.40, issue.2, pp.99-10108, 2002.
DOI : 10.1016/0092-8674(85)90143-6

P. G. Sreekumar, R. Kannan, J. Yaung, C. K. Spee, S. J. Ryan et al., Protection from oxidative stress by methionine sulfoxide reductases in RPE cells, Biochemical and Biophysical Research Communications, vol.334, issue.1, pp.245-53, 2005.
DOI : 10.1016/j.bbrc.2005.06.081

E. R. Stadtman, R. L. Et, and . Levine, Free radical-mediated oxidation of free amino acids and amino acid residues in proteins, Amino Acids, vol.25, issue.3-4, pp.3-4, 2003.
DOI : 10.1007/s00726-003-0011-2

E. R. Stadtman, H. Van-remmen, A. Richardson, N. B. Wehr, and R. L. Levine, Methionine oxidation and aging, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.135-175, 2005.
DOI : 10.1016/j.bbapap.2004.08.010

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, M. G. Grutter, R. Glockshuber et al., Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation, Structure, vol.13, issue.7, pp.985-93, 2005.
DOI : 10.1016/j.str.2005.04.014

D. I. Svergun, M. V. Petoukhov, and M. H. Koch, Determination of Domain Structure of Proteins from X-Ray Solution Scattering, Biophysical Journal, vol.80, issue.6, pp.2946-53, 2001.
DOI : 10.1016/S0006-3495(01)76260-1

C. Taggart, D. Cervantes-laurean, G. Kim, N. G. Mcelvaney, N. Wehr et al., Oxidation of either methionine 351 or methionine 358 in alpha 1- antitrypsin causes loss of anti-neutrophil elastase activity, J Biol Chem, vol.275, issue.35, pp.27258-65, 2000.

M. K. Taha, M. So, H. S. Seifert, E. Billyard, and C. Marchal, Pilin expression in Neisseria gonorrhoeae is under both positive and negative transcriptional control, EMBO Journal, vol.7, issue.13, pp.4367-4378, 1988.

T. Takahashi, M. M. Nau, I. Chiba, M. J. Birrer, R. K. Rosenberg et al., p53: a frequent target for genetic abnormalities in lung cancer, Science, vol.246, issue.4929, pp.246-491, 1989.
DOI : 10.1126/science.2554494

X. D. Tang, H. Daggett, M. Hanner, M. L. Garcia, O. B. Mcmanus et al., Oxidative Regulation of Large Conductance Calcium-Activated Potassium Channels, The Journal of General Physiology, vol.3, issue.3, pp.253-74, 2001.
DOI : 10.1016/S0008-6363(99)00085-1

P. Tavares, A. S. Pereira, J. J. Moura, and I. Moura, Metalloenzymes of the denitrification pathway, Journal of Inorganic Biochemistry, vol.100, issue.12, pp.2087-100, 2006.
DOI : 10.1016/j.jinorgbio.2006.09.003

A. B. Taylor, D. M. Benglis, J. , S. Dhandayuthapani, and P. J. Hart, Structure of Mycobacterium tuberculosis Methionine Sulfoxide Reductase A in Complex with Protein-Bound Methionine, Journal of Bacteriology, vol.185, issue.14, pp.4119-4145, 2003.
DOI : 10.1128/JB.185.14.4119-4126.2003

M. M. Teixeira, F. Q. Cunha, A. Noronha-dutra, and J. Hothersall, Production of singlet oxygen by eosinophils activated in vitro by C5a and leukotriene B4, FEBS Letters, vol.32, issue.3, pp.265-273, 1999.
DOI : 10.1016/0014-5793(93)80621-Z

A. Telfer, S. M. Bishop, D. Phillips, and J. Barber, Isolated photosynthetic reaction center of photosystem II as a sensitizer for the formation of singlet oxygen. Detection and quantum yield determination using a chemical trapping technique, The Journal of biological chemistry, vol.269, issue.18, pp.13244-53, 1994.

F. Tete-favier, D. Cobessi, S. Boschi-muller, S. Azza, G. Branlant et al., Crystal Structure of the Escherichia coli Peptide Methionine Sulphoxide Reductase at 1.9 ?? Resolution, Structure, vol.8, issue.11, pp.1167-78, 2000.
DOI : 10.1016/S0969-2126(00)00526-8

URL : https://hal.archives-ouvertes.fr/hal-00151127

S. R. Thorpe, J. W. Et, and . Baynes, Maillard reaction products in tissue proteins: New products and new perspectives, Amino Acids, vol.25, issue.3-4, pp.3-4, 2003.
DOI : 10.1007/s00726-003-0017-9

M. Triesscheijn, P. Baas, J. H. Schellens, and F. A. Stewart, Photodynamic Therapy in Oncology, The Oncologist, vol.11, issue.9, pp.1034-1078, 2006.
DOI : 10.1634/theoncologist.11-9-1034

K. Uchida, 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress, Progress in Lipid Research, vol.42, issue.4, pp.318-361, 2003.
DOI : 10.1016/S0163-7827(03)00014-6

S. Utaida, P. M. Dunman, D. Macapagal, E. Murphy, S. J. Projan et al., Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell-wall-stress stimulon, Microbiology, vol.149, issue.10, pp.2719-2751, 2003.
DOI : 10.1099/mic.0.26426-0

A. Vagin, A. Et, and . Teplyakov, : an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6, pp.1022-1025, 1997.
DOI : 10.1107/S0021889897006766

M. Valko, D. Leibfritz, J. Moncol, M. T. Cronin, M. Mazur et al., Free radicals and antioxidants in normal physiological functions and human disease, The International Journal of Biochemistry & Cell Biology, vol.39, issue.1, pp.44-84, 2007.
DOI : 10.1016/j.biocel.2006.07.001

J. Vijayalakshmi, M. K. Mukhergee, J. Graumann, U. Jakob, and M. A. Saper, The 2.2 ?? Crystal Structure of Hsp33, Structure, vol.9, issue.5, pp.367-75, 2001.
DOI : 10.1016/S0969-2126(01)00597-4

W. Vogt, Oxidation of methionyl residues in proteins: Tools, targets, and reversal, Free Radical Biology and Medicine, vol.18, issue.1, pp.93-105, 1995.
DOI : 10.1016/0891-5849(94)00158-G

S. Vougier, J. Mary, N. Dautin, J. Vinh, B. Friguet et al., Adenylate Cyclase, as Probed by Selective Oxidation and Repair by the Peptide Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.67, issue.29, pp.30210-30218, 2004.
DOI : 10.1074/jbc.M209180200

URL : https://hal.archives-ouvertes.fr/hal-01636955

C. Walling, Fenton's reagent revisited, Accounts of Chemical Research, vol.8, issue.4, pp.125-131, 1975.
DOI : 10.1021/ar50088a003

N. J. Wang, S. Gottesman, M. C. Willingham, M. M. Gottesman, and M. R. Maurizi, A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease., Proceedings of the National Academy of Sciences, vol.90, issue.23, pp.11247-11251, 1993.
DOI : 10.1073/pnas.90.23.11247

C. M. Weeks, R. Et, and . Miller, version 2.0, Journal of Applied Crystallography, vol.32, issue.1, pp.120-124, 1999.
DOI : 10.1107/S0021889898010504

M. S. Weiss, R. Et, and . Hilgenfeld, factor as a quality indicator for X-ray data, Journal of Applied Crystallography, vol.30, issue.2, pp.203-205, 1997.
DOI : 10.1107/S0021889897003907

H. Weissbach, L. Resnick, and N. Brot, Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.203-215, 2005.
DOI : 10.1016/j.bbapap.2004.10.004

C. C. Winterbourn, Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid, Toxicology, vol.181, issue.182, pp.223-230, 2002.
DOI : 10.1016/S0300-483X(02)00286-X

T. M. Wizemann, J. Moskovitz, B. J. Pearce, D. Cundell, C. G. Arvidson et al., Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens., Proceedings of the National Academy of Sciences, vol.93, issue.15, pp.93-7985, 1996.
DOI : 10.1073/pnas.93.15.7985

S. P. Wolff, R. T. Et, and . Dean, Glucose autoxidation and protein modification. The potential role of ???autoxidative glycosylation??? in diabetes, Biochemical Journal, vol.245, issue.1, pp.243-50, 1987.
DOI : 10.1042/bj2450243

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, Is a Disulfide Reductase That Can Recycle Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.254, issue.13, pp.12344-50, 2005.
DOI : 10.1128/JB.184.7.2005-2018.2002

URL : https://hal.archives-ouvertes.fr/hal-01690798

H. Yasui, S. Hayashi, and H. Sakurai, Possible Involvement of Singlet Oxygen Species as Multiple Oxidants in P450 Catalytic Reactions, Drug Metabolism and Pharmacokinetics, vol.20, issue.1, pp.1-13, 2005.
DOI : 10.2133/dmpk.20.1

W. G. Zumft, Cell biology and molecular basis of denitrification, Microbiol Mol Biol Rev, vol.61, issue.4, pp.533-616, 1997.