K. G. Reddie, C. , and K. S. , Expanding the functional diversity of proteins through cysteine oxidation, Current Opinion in Chemical Biology, vol.12, issue.6, pp.746-754, 2008.
DOI : 10.1016/j.cbpa.2008.07.028

S. W. Kang, I. C. Baines, R. , and S. G. , Characterization of a Mammalian Peroxiredoxin That Contains One Conserved Cysteine, Journal of Biological Chemistry, vol.25, issue.11, pp.6303-6311, 1998.
DOI : 10.1111/j.1432-1033.1972.tb01711.x

W. Kong, S. Shiota, Y. Shi, H. Nakayama, and K. Nakayama, A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp), Biochemical Journal, vol.351, issue.1, pp.107-114, 2000.
DOI : 10.1042/bj3510107

Z. A. Wood, E. Schröder, R. Harris, J. Poole, and L. B. , Structure, mechanism and regulation of peroxiredoxins, Trends in Biochemical Sciences, vol.28, issue.1, pp.32-40, 2003.
DOI : 10.1016/S0968-0004(02)00003-8

M. B. Toledano, A. Delaunay, L. Monceau, and F. Tacnet, Microbial H2O2 sensors as archetypical redox signaling modules, Trends in Biochemical Sciences, vol.29, issue.7, pp.351-357, 2004.
DOI : 10.1016/j.tibs.2004.05.005

H. H. Jang, K. O. Lee, Y. H. Chi, B. G. Jung, S. K. Park et al., Two Enzymes in One, Cell, vol.117, issue.5, pp.625-635, 2004.
DOI : 10.1016/j.cell.2004.05.002

URL : https://doi.org/10.1016/j.cell.2004.05.002

J. C. Lim, H. I. Choi, Y. S. Park, H. W. Nam, H. A. Woo et al., Irreversible Oxidation of the Active-site Cysteine of Peroxiredoxin to Cysteine Sulfonic Acid for Enhanced Molecular Chaperone Activity, Journal of Biological Chemistry, vol.17, issue.suppl., pp.28873-28880, 2008.
DOI : 10.1007/s00018-005-5190-4

Z. A. Wood, L. B. Poole, and P. A. Karplus, Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling, Science, vol.300, issue.5619, pp.650-653, 2003.
DOI : 10.1126/science.1080405

M. Aran, D. Caporaletti, A. M. Senn, M. T. Tellez-de-iñon, M. R. Girotti et al., ATP-dependent modulation and autophosphorylation of rapeseed 2-Cys peroxiredoxin, FEBS Journal, vol.269, issue.7, pp.1450-1463, 2008.
DOI : 10.1046/j.1432-1033.2002.03049.x

J. H. Seo, J. C. Lim, D. Y. Lee, K. S. Kim, G. Piszczek et al., Novel Protective Mechanism against Irreversible Hyperoxidation of Peroxiredoxin, Journal of Biological Chemistry, vol.78, issue.20, pp.13455-13465, 2009.
DOI : 10.1074/jbc.M505362200

URL : http://www.jbc.org/content/284/20/13455.full.pdf

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

A. P. Vivancos, E. A. Castillo, B. Biteau, C. Nicot, J. Ayté et al., A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway, Proceedings of the National Academy of Sciences, vol.7, issue.3-4, pp.8875-8880, 2005.
DOI : 10.1089/ars.2005.7.327

S. M. Bozonet, V. J. Findlay, A. M. Day, J. Cameron, E. A. Veal et al., Oxidation of a Eukaryotic 2-Cys Peroxiredoxin Is a Molecular Switch Controlling the Transcriptional Response to Increasing Levels of Hydrogen Peroxide, Journal of Biological Chemistry, vol.14, issue.24, pp.23319-23327, 2005.
DOI : 10.1101/gad.5.1.60

H. A. Woo, S. H. Bae, S. Park, R. , and S. G. , Sestrin 2 Is Not a Reductase for Cysteine Sulfinic Acid of Peroxiredoxins, Antioxidants & Redox Signaling, vol.11, issue.4, pp.739-745, 2009.
DOI : 10.1089/ars.2008.2360

X. Roussel, G. Béchade, A. Kriznik, A. Van-dorsselaer, S. Sanglier-cianferani et al., Evidence for the Formation of a Covalent Thiosulfinate Intermediate with Peroxiredoxin in the Catalytic Mechanism of Sulfiredoxin, Journal of Biological Chemistry, vol.96, issue.33, pp.22371-22382, 2008.
DOI : 10.1021/bi061824h

URL : https://hal.archives-ouvertes.fr/hal-01652689

T. J. Jönsson, M. S. Murray, L. C. Johnson, and W. T. Lowther, Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate, Journal of Biological Chemistry, vol.555, issue.35, pp.23846-23851, 2008.
DOI : 10.1074/jbc.273.17.10454

T. J. Jönsson, A. W. Tsang, W. T. Lowther, and C. M. Furdui, Identification of Intact Protein Thiosulfinate Intermediate in the Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Human Sulfiredoxin, Journal of Biological Chemistry, vol.343, issue.34, pp.22890-22894, 2008.
DOI : 10.1074/jbc.M800493200

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

S. B. Mulrooney, W. , and C. H. Jr, Evidence for two conformational states of thioredoxin reductase from Escherichia coli: Use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation, Protein Science, vol.270, issue.10, pp.2188-2195, 1997.
DOI : 10.1016/0005-2795(71)90204-2

B. Biteau, A Sulfirédoxine, une Nouvelle Enzyme Illustrant les Deux Facettes Biologiques de l'H 2 O 2 : Toxicite et Signalisation, 2005.

T. S. Chang, W. Jeong, H. A. Woo, S. M. Lee, S. Park et al., Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine, Journal of Biological Chemistry, vol.255, issue.49, pp.50994-51001, 2004.
DOI : 10.1038/emm.1999.9

W. Jeong, S. J. Park, T. S. Chang, D. Y. Lee, R. et al., Molecular Mechanism of the Reduction of Cysteine Sulfinic Acid of Peroxiredoxin to Cysteine by Mammalian Sulfiredoxin, Journal of Biological Chemistry, vol.8, issue.20, pp.14400-14407, 2006.
DOI : 10.1016/S0969-2126(00)00147-7

A. A. Bondareva, M. R. Capecchi, S. V. Iverson, Y. Li, N. I. Lopez et al., Free Radic, Biol. Med, vol.43, pp.911-923, 2007.