C. M. Park, L. Weerasinghe, J. J. Day, J. M. Fukuto, and M. Xian, Persulfides: current knowledge and challenges in chemistry and chemical biology, Molecular BioSystems, vol.11, issue.7, pp.1775-1785, 2015.

P. K. Yadav, M. Martinov, V. Vitvitsky, J. Seravalli, R. Wedmann et al., Biosynthesis and Reactivity of Cysteine Persulfides in Signaling, Journal of the American Chemical Society, vol.138, issue.1, pp.289-299, 2015.

J. I. Toohey, Erratum to ?Sulfur signaling: Is the agent sulfide or sulfane?? [Anal. Biochem. 413 (2011) 1?7], Analytical Biochemistry, vol.415, issue.2, p.221, 2011.

T. Ida, T. Sawa, H. Ihara, Y. Tsuchiya, Y. Watanabe et al., Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling, Proceedings of the National Academy of Sciences, vol.111, issue.21, pp.7606-7611, 2014.

E. Cuevasanta, M. Lange, J. Bonanata, E. L. Coitiño, G. Ferrer-sueta et al., Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide, Journal of Biological Chemistry, vol.290, issue.45, pp.26866-26880, 2015.

E. Cuevasanta, M. N. Möller, and B. Alvarez, Biological chemistry of hydrogen sulfide and persulfides, Archives of Biochemistry and Biophysics, vol.617, pp.9-25, 2017.

R. E. Hansen, D. Roth, and J. R. Winther, Quantifying the global cellular thiol-disulfide status, Proceedings of the National Academy of Sciences, vol.106, issue.2, pp.422-427, 2009.

A. Vasas, É. Dóka, I. Fábián, and P. Nagy, Kinetic and thermodynamic studies on the disulfide-bond reducing potential of hydrogen sulfide, Nitric Oxide, vol.46, pp.93-101, 2015.

D. Kessler, Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes, FEMS Microbiology Reviews, vol.30, issue.6, pp.825-840, 2006.

M. Cavuzic, Y. Liu, and . Biomolecules, , vol.7, p.27, 2017.

L. Zheng, R. H. White, V. L. Cash, R. F. Jack, and D. R. Dean, Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis., Proceedings of the National Academy of Sciences, vol.90, issue.7, pp.2754-2758, 1993.

L. Zheng, R. H. White, V. L. Cash, and D. R. Dean, Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product, Biochemistry, vol.33, issue.15, pp.4714-4720, 1994.

R. Colnaghi, G. Cassinelli, M. Drummond, F. Forlani, and S. Pagani, Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition, FEBS Letters, vol.500, issue.3, pp.153-156, 2001.

G. D. Westrop, I. Georg, and G. H. Coombs, The Mercaptopyruvate Sulfurtransferase of Trichomonas vaginalis Links Cysteine Catabolism to the Production of Thioredoxin Persulfide, Journal of Biological Chemistry, vol.284, issue.48, pp.33485-33494, 2009.

D. Bordo and P. Bork, The rhodanese/Cdc25 phosphatase superfamily, EMBO reports, vol.3, issue.8, pp.741-746, 2002.

R. Cipollone, P. Ascenzi, and P. Visca, Common themes and variations in the rhodanese superfamily, IUBMB Life, vol.59, issue.2, pp.51-59, 2007.

M. S. Alphey, R. A. Williams, J. C. Mottram, G. H. Coombs, and W. N. Hunter, The Crystal Structure ofLeishmania major3-Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.278, issue.48, pp.48219-48227, 2003.

P. K. Yadav, K. Yamada, T. Chiku, M. Koutmos, and R. Banerjee, Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.288, issue.27, pp.20002-20013, 2013.

Y. Mikami, N. Shibuya, Y. Kimura, N. Nagahara, Y. Ogasawara et al., Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide, Biochemical Journal, vol.439, issue.3, pp.479-485, 2011.

N. Nagahara and T. Nishino, Role of Amino Acid Residues in the Active Site of Rat Liver Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.271, issue.44, pp.27395-27401, 1996.

A. Spallarossa, F. Forlani, A. Carpen, A. Armirotti, S. Pagani et al., The ""Rhodanese"" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli, J. Mol. Biol, vol.335, pp.583-93, 2003.

G. T. Huang and J. S. Yu, Enzyme Catalysis that Paves the Way for S-Sulfhydration via Sulfur Atom Transfer, The Journal of Physical Chemistry B, vol.120, issue.20, pp.4608-4615, 2016.

E. Mössner, M. Huber-wunderlich, and R. Glockshuber, Characterization ofEscherichia colithioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases, Protein Science, vol.7, issue.5, pp.1233-1244, 1998.

S. B. Mulrooney and C. H. Williams, 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.6, issue.10, pp.2188-2195, 2008.

P. F. Cook and . Ed, Enzyme mechanism from isotope effects, 1991.

B. R. Rabin, Co-operative Effects in Enzyme Catalysis: A Possible Kinetic Model Based on Substrate-Induced Conformation Isomerization, Biochemical Journal, vol.102, issue.2, pp.22C-23C, 1967.

C. Frieden, Slow Transitions and Hysteretic Behavior in Enzymes, Annual Review of Biochemistry, vol.48, issue.1, pp.471-489, 1979.

M. Antoine, S. Boschi-muller, and G. Branlant, Kinetic Characterization of the Chemical Steps Involved in the Catalytic Mechanism of Methionine Sulfoxide Reductase A fromNeisseria meningitidis, Journal of Biological Chemistry, vol.278, issue.46, pp.45352-45357, 2003.

F. Talfournier, N. Colloc'h, J. P. Mornon, and G. Branlant, Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis, European Journal of Biochemistry, vol.252, issue.3, pp.447-457, 1998.

D. Susan-resiga and T. Nowak, The Proton Transfer Step Catalyzed by Yeast Pyruvate Kinase, Journal of Biological Chemistry, vol.278, issue.15, pp.12660-12671, 2003.

M. Coincon, W. Wang, J. Sygusch, and S. Y. Seah, Crystal Structure of Reaction Intermediates in Pyruvate Class II Aldolase, Journal of Biological Chemistry, vol.287, issue.43, pp.36208-36221, 2012.

R. Abdolrasulnia and J. L. Wood, Transfer of persulfide sulfur from thiocystine to rhodanese, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.567, issue.1, pp.135-143, 1979.

K. Abe and H. Kimura, The possible role of hydrogen sulfide as an endogenous neuromodulator, The Journal of Neuroscience, vol.16, issue.3, pp.1066-1071, 1996.

H. Adams, W. Teertstra, M. Koster, and J. Tommassen, PspE (phage-shock protein E) of Escherichia coli is a rhodanese, FEBS Letters, vol.518, issue.1-3, pp.173-176, 2002.

H. Adams, W. Teertstra, M. Koster, and J. Tommassen, PspE (phage-shock protein E) of Escherichia coli is a rhodanese, FEBS Letters, vol.518, issue.1-3, pp.173-176, 2002.

A. F. Agrò, C. Cannella, M. T. Graziani, and D. Cavallini, A possible role for rhodanese: The formation of ?labile? sulfur from thiosulfate, FEBS Letters, vol.16, issue.3, pp.172-174, 1971.

E. Aizenman, S. A. Lipton, and R. H. Loring, Selective modulation of NMDA responses by reduction and oxidation, Neuron, vol.2, issue.3, pp.1257-1263, 1989.

M. S. Alphey, R. A. Williams, J. C. Mottram, G. H. Coombs, and W. N. Hunter, The Crystal Structure ofLeishmania major3-Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.278, issue.48, pp.48219-48227, 2003.

M. Aminlari and H. Gilanpour, Comparative studies on the distribution of rhodanese in different tissues of domestic animals, Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, vol.99, issue.3, pp.673-677, 1991.

E. Andersson, H. Westberg, I. Bryngelsson, A. Magnuson, and B. Persson, Cancer incidence among Swedish pulp and paper mill workers: a cohort study of sulphate and sulphite mills, International Archives of Occupational and Environmental Health, vol.86, issue.5, pp.529-540, 2012.

A. D. Ang, A. Konigstorfer, G. I. Giles, and M. Bhatia, Measuring free tissue sulfide, Advances in Biological Chemistry, vol.02, issue.04, pp.360-365, 2012.

N. K. Arden and K. M. Leyland, Osteoarthritis year 2013 in review: clinical, Osteoarthritis and Cartilage, vol.21, issue.10, pp.1409-1413, 2013.

K. D. Augustyn, M. R. Jackson, and M. S. Jorns, Use of Tissue Metabolite Analysis and Enzyme Kinetics To Discriminate between Alternate Pathways for Hydrogen Sulfide Metabolism, Biochemistry, vol.56, issue.7, pp.986-996, 2017.

Y. Azumi and A. Watanabe, Evidence for a Senescence-Associated Gene Induced by Darkness, Plant Physiology, vol.95, issue.2, pp.577-583, 1991.

R. O. Beauchamp, J. S. Bus, J. A. Popp, C. J. Boreiko, D. A. Andjelkovich et al., A Critical Review of the Literature on Hydrogen Sulfide Toxicity, CRC Critical Reviews in Toxicology, vol.13, issue.1, pp.25-97, 1984.

J. Be?towski, Hydrogen sulfide in pharmacology and medicine ? An update, Pharmacological Reports, vol.67, issue.3, pp.647-658, 2015.

H. Bhattacharjee, J. Sheng, A. A. Ajees, R. Mukhopadhyay, and B. P. Rosen, Adventitious Arsenate Reductase Activity of the Catalytic Domain of the Human Cdc25B and Cdc25C Phosphatases, Biochemistry, vol.49, issue.4, pp.802-809, 2010.

D. Bordo and P. Bork, The rhodanese/Cdc25 phosphatase superfamily, EMBO reports, vol.3, issue.8, pp.741-746, 2002.

D. Bordo, D. Deriu, R. Colnaghi, A. Carpen, S. Pagani et al., The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families, Journal of Molecular Biology, vol.298, issue.4, pp.691-704, 2000.

J. L. Borowitz, P. G. Gunasekar, and G. E. Isom, Hydrogen cyanide generation by ?-opiate receptor activation: possible neuromodulatory role of endogenous cyanide, Brain Research, vol.768, issue.1-2, pp.294-300, 1997.

T. Bostelaar, V. Vitvitsky, J. Kumutima, B. E. Lewis, P. K. Yadav et al., Hydrogen Sulfide Oxidation by Myoglobin, Journal of the American Chemical Society, vol.138, issue.27, pp.8476-8488, 2016.

J. A. Brito, F. L. Sousa, M. Stelter, T. M. Bandeiras, C. Vonrhein et al., Structural and Functional Insights into Sulfide:Quinone Oxidoreductase,, Biochemistry, vol.48, issue.24, pp.5613-5622, 2009.

A. C. Bulmer, K. Ried, J. T. Blanchfield, and K. Wagner, The anti-mutagenic properties of bile pigments, Mutation Research/Reviews in Mutation Research, vol.658, issue.1-2, pp.28-41, 2008.

E. F. Burguera, R. Meijide-failde, and F. J. Blanco, Hydrogen Sulfide and Inflammatory Joint Diseases, Current Drug Targets, vol.18, issue.14, 2017.

B. Cagianut, H. P. Schnebli, K. Rhyner, and J. Furrer, Decreased thiosulfate sulfur transferase (rhodanese) in Leber's hereditary optic atrophy, Klinische Wochenschrift, vol.62, issue.18, pp.850-854, 1984.

C. Cannella, L. Pecci, A. F. Agro, G. Federici, B. Pensa et al., Selenium Binding to Beef-Kidney Rhodanese, European Journal of Biochemistry, vol.55, issue.1, pp.285-289, 1975.

S. Carballal, M. Trujillo, E. Cuevasanta, S. Bartesaghi, M. N. Möller et al., Reactivity of hydrogen sulfide with peroxynitrite and other oxidants of biological interest, Free Radical Biology and Medicine, vol.50, issue.1, pp.196-205, 2011.

M. Chattopadhyay, R. Kodela, K. R. Olson, and K. Kashfi, NOSH?aspirin (NBS-1120), a novel nitric oxide- and hydrogen sulfide-releasing hybrid is a potent inhibitor of colon cancer cell growth in vitro and in a xenograft mouse model, Biochemical and Biophysical Research Communications, vol.419, issue.3, pp.523-528, 2012.

R. Cipollone, P. Ascenzi, and P. Visca, Common themes and variations in the rhodanese superfamily, IUBMB Life, vol.59, issue.2, pp.51-59, 2007.

C. J. Clemedson, H. I. Hultman, and B. O. Sörbo, The Antidote Effect of Some Sulfur Compounds and Rhodanese in Experimental Cyanide Poisoning., Acta Physiologica Scandinavica, vol.32, issue.2-3, pp.245-251, 1954.

C. Coletta, A. Papapetropoulos, K. Erdelyi, G. Olah, K. Modis et al., Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation, Proceedings of the National Academy of Sciences, vol.109, issue.23, pp.9161-9166, 2012.

J. P. Collman, S. Ghosh, A. Dey, and R. A. Decréau, Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation, Proceedings of the National Academy of Sciences, vol.106, issue.52, pp.22090-22095, 2009.

R. Colnaghi, G. Cassinelli, M. Drummond, F. Forlani, and S. Pagani, Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition, FEBS Letters, vol.500, issue.3, pp.153-156, 2001.

G. Cornilescu, D. A. Vinarov, E. M. Tyler, J. L. Markley, and C. C. Cornilescu, Solution structure of a single-domain thiosulfate sulfurtransferase fromArabidopsis thaliana, Protein Science, vol.15, issue.12, pp.2836-2841, 2006.

A. Cornish-bowden and M. L. Cárdenas, Co-operativity in monomeric enzymes, Journal of Theoretical Biology, vol.124, issue.1, pp.1-23, 1987.

M. S. Cortese, A. B. Caplan, and R. L. Crawford, Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid), BMC Evolutionary Biology, vol.2, issue.1, p.8, 2002.

M. M. Cortese-krott, G. G. Kuhnle, A. Dyson, B. O. Fernandez, M. Grman et al., Key bioactive reaction products of the NO/H2S interaction are S/N-hybrid species, polysulfides, and nitroxyl, Proceedings of the National Academy of Sciences, vol.112, issue.34, pp.E4651-E4660, 2015.

M. M. Cortese-krott, D. Pullmann, and M. Feelisch, Nitrosopersulfide (SSNO ? ) targets the Keap-1/Nrf2 redox system, Pharmacological Research, vol.113, pp.490-499, 2016.

J. C. Crawhall, A review of the clinical presentation and laboratory findings in two uncommon hereditary disorders of sulfur amino acid metabolism, ?-mercaptolactate cysteine disulfideuria and sulfite oxidase deficiency, Clinical Biochemistry, vol.18, issue.3, pp.139-142, 1985.

E. Cuevasanta, M. Lange, J. Bonanata, E. L. Coitiño, G. Ferrer-sueta et al., Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide, Journal of Biological Chemistry, vol.290, issue.45, pp.26866-26880, 2015.

E. Cuevasanta, M. N. Möller, and B. Alvarez, Biological chemistry of hydrogen sulfide and persulfides, Arch. Biochem. Biophys, 2016.

T. N. Das, R. E. Huie, P. Neta, and S. Padmaja, Reduction Potential of the Sulfhydryl Radical: Pulse Radiolysis and Laser Flash Photolysis Studies of the Formation and Reactions of ·SH and HSSH·-in Aqueous Solutions, The Journal of Physical Chemistry A, vol.103, issue.27, pp.5221-5226, 1999.

T. N. De-boer, A. M. Huisman, A. A. Polak, A. G. Niehoff, A. C. Van-rinsum et al., The chondroprotective effect of selective COX-2 inhibition in osteoarthritis: ex vivo evaluation of human cartilage tissue after in vivo treatment, Osteoarthritis and Cartilage, vol.17, issue.4, pp.482-488, 2009.

M. Delhase, M. Hayakawa, Y. Chen, and M. Karin, Positive and Negative Regulation of IB Kinase Activity Through IKK Subunit Phosphorylation, Science, vol.284, issue.5412, pp.309-313, 1999.

I. Di-meo, G. Fagiolari, A. Prelle, C. Viscomi, M. Zeviani et al., Chronic Exposure to Sulfide Causes Accelerated Degradation of Cytochrome c Oxidase in Ethylmalonic Encephalopathy, Antioxidants & Redox Signaling, vol.15, issue.2, pp.353-362, 2011.

I. Di-meo, C. Lamperti, and V. Tiranti, Mitochondrial diseases caused by toxic compound accumulation: from etiopathology to therapeutic approaches, EMBO Molecular Medicine, vol.7, issue.10, pp.1257-1266, 2015.

E. Distrutti, L. Sediari, A. Mencarelli, B. Renga, S. Orlandi et al., Evidence That Hydrogen Sulfide Exerts Antinociceptive Effects in the Gastrointestinal Tract by Activating KATP Channels, Journal of Pharmacology and Experimental Therapeutics, vol.316, issue.1, pp.325-335, 2005.

A. Drousiotou, I. Dimeo, R. Mineri, T. Georgiou, G. Stylianidou et al., Ethylmalonic encephalopathy: application of improved biochemical and molecular diagnostic approaches, Clinical Genetics, vol.79, issue.4, pp.385-390, 2011.

J. O. Edwards and R. G. Pearson, The Factors Determining Nucleophilic Reactivities, Journal of the American Chemical Society, vol.84, issue.1, pp.16-24, 1962.

A. El-sahili, Etude du mécanisme d'une thioltransférase : la 3-mercaptopyruvate sulfurtransférase d'Escherichia coli -Rapport Master 2, Laboratoire AREMS, 2012.

S. A. Everett and P. Wardman, [5] Perthiols as antioxidants: Radical-scavenging andprooxidative mechanisms, Methods in Enzymology, vol.251, pp.55-69, 1995.

E. B. Fauman, J. P. Cogswell, B. Lovejoy, W. J. Rocque, W. Holmes et al., HUMAN CDC25A CATALYTIC DOMAIN, Cdc25A. Cell, vol.93, pp.617-625, 1998.

W. Ferdinand, The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase, Biochemical Journal, vol.98, issue.1, pp.278-283, 1966.

S. Fiorucci, E. Distrutti, G. Cirino, and J. L. Wallace, The Emerging Roles of Hydrogen Sulfide in the Gastrointestinal Tract and Liver, Gastroenterology, vol.131, issue.1, pp.259-271, 2006.

F. Forlani, A. Carpen, and S. Pagani, Evidence that elongation of the catalytic loop of the Azotobacter vinelandii rhodanese changed selectivity from sulfur- to phosphate-containing substrates, Protein Engineering Design and Selection, vol.16, issue.7, pp.515-519, 2003.

B. Fox, J. Schantz, R. Haigh, M. E. Wood, P. K. Moore et al., Inducible hydrogen sulfide synthesis in chondrocytes and mesenchymal progenitor cells: is H2S a novel cytoprotective mediator in the inflamed joint?, Journal of Cellular and Molecular Medicine, vol.16, issue.4, pp.896-910, 2012.

B. Fräsdorf, C. Radon, and S. Leimkühler, Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans, Journal of Biological Chemistry, vol.289, issue.50, pp.34543-34556, 2014.

M. Fu, W. Zhang, L. Wu, G. Yang, H. Li et al., Hydrogen sulfide (H2S) metabolism in mitochondria and its regulatory role in energy production, Proceedings of the National Academy of Sciences, vol.109, issue.8, pp.2943-2948, 2012.

J. M. Fukuto, S. J. Carrington, D. J. Tantillo, J. G. Harrison, L. J. Ignarro et al., Small Molecule Signaling Agents: The Integrated Chemistry and Biochemistry of Nitrogen Oxides, Oxides of Carbon, Dioxygen, Hydrogen Sulfide, and Their Derived Species, Chemical Research in Toxicology, vol.25, issue.4, pp.769-793, 2012.

J. Furne, A. Saeed, and M. D. Levitt, Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values, American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, vol.295, issue.5, pp.R1479-R1485, 2008.

J. A. Gibson, G. E. Sladen, and A. M. Dawson, Protein absorption and ammonia production: the effects of dietary protein and removal of the colon, British Journal of Nutrition, vol.35, issue.1, pp.61-65, 1976.

L. R. Goodwin, D. Francom, F. P. Dieken, J. D. Taylor, M. W. Warenycia et al., Determination of Sulfide in Brain Tissue by Gas Dialysis/Ion Chromatography: Postmortem Studies and Two Case Reports, Journal of Analytical Toxicology, vol.13, issue.2, pp.105-109, 1989.

M. Goubern, M. Andriamihaja, T. Nübel, F. Blachier, and F. Bouillaud, Sulfide, the first inorganic substrate for human cells, The FASEB Journal, vol.21, issue.8, pp.1699-1706, 2007.

J. R. Green and J. Westley, Mechanism of rhodanese action: polarographic studies, J. Biol. Chem, vol.236, pp.3047-3050, 1961.

R. Greiner, Z. Pálinkás, K. Bäsell, D. Becher, H. Antelmann et al., Polysulfides Link H2S to Protein Thiol Oxidation, Antioxidants & Redox Signaling, vol.19, issue.15, pp.1749-1765, 2013.

C. Ha, S. Tian, K. Sun, D. Wang, J. Lv et al., Hydrogen sulfide attenuates IL-1?-induced inflammatory signaling and dysfunction of osteoarthritic chondrocytes, International Journal of Molecular Medicine, vol.35, issue.6, pp.1657-1666, 2015.

U. Hannestad, J. Mårtensson, R. Sjödahl, and B. Sörbo, 3-Mercaptolactate cysteine disulfiduria: Biochemical studies on affected and unaffected members of a family, Biochemical Medicine, vol.26, issue.1, pp.106-114, 1981.

J. D. Hayes, M. Mcmahon, S. Chowdhry, and A. T. Dinkova-kostova, Cancer Chemoprevention Mechanisms Mediated Through the Keap1?Nrf2 Pathway, Antioxidants & Redox Signaling, vol.13, issue.11, pp.1713-1748, 2010.

B. J. Henriques, T. G. Lucas, J. V. Rodrigues, J. H. Frederiksen, M. S. Teixeira et al., Ethylmalonic Encephalopathy ETHE1 R163W/R163Q Mutations Alter Protein Stability and Redox Properties of the Iron Centre, PLoS ONE, vol.9, issue.9, p.e107157, 2014.

H. Higashitsuji, H. Higashitsuji, T. Nagao, K. Nonoguchi, S. Fujii et al., A novel protein overexpressed in hepatoma accelerates export of NF-?B from the nucleus and inhibits p53-dependent apoptosis, Cancer Cell, vol.2, issue.4, pp.335-346, 2002.

T. M. Hildebrandt and M. K. Grieshaber, Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria, FEBS Journal, vol.275, issue.13, pp.3352-3361, 2008.

K. Hofmann, P. Bucher, and A. V. Kajava, A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain, Journal of Molecular Biology, vol.282, issue.1, pp.195-208, 1998.

R. Hosoki, N. Matsuki, and H. Kimura, The Possible Role of Hydrogen Sulfide as an Endogenous Smooth Muscle Relaxant in Synergy with Nitric Oxide, Biochemical and Biophysical Research Communications, vol.237, issue.3, pp.527-531, 1997.

J. M. Hourihan, J. G. Kenna, and J. D. Hayes, The Gasotransmitter Hydrogen Sulfide Induces Nrf2-Target Genes by Inactivating the Keap1 Ubiquitin Ligase Substrate Adaptor Through Formation of a Disulfide Bond Between Cys-226 and Cys-613, Antioxidants & Redox Signaling, vol.19, issue.5, pp.465-481, 2013.

G. Huang and J. K. Yu, Enzyme Catalysis that Paves the Way for S-Sulfhydration via Sulfur Atom Transfer, The Journal of Physical Chemistry B, vol.120, issue.20, pp.4608-4615, 2016.

J. Huang, H. Niknahad, S. Khan, and P. J. O?brien, Hepatocyte-Catalysed Detoxification of Cyanide by l- and d-Cysteine, Biochemical Pharmacology, vol.55, issue.12, pp.1983-1990, 1998.

Y. Huang, C. Tang, J. Du, and H. Jin, Endogenous Sulfur Dioxide: A New Member of Gasotransmitter Family in the Cardiovascular System, Oxidative Medicine and Cellular Longevity, vol.2016, pp.1-9, 2016.

T. Ida, T. Sawa, H. Ihara, Y. Tsuchiya, Y. Watanabe et al., Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling, Proceedings of the National Academy of Sciences, vol.111, issue.21, pp.7606-7611, 2014.

M. R. Jackson, S. L. Melideo, and M. S. Jorns, Human Sulfide:Quinone Oxidoreductase Catalyzes the First Step in Hydrogen Sulfide Metabolism and Produces a Sulfane Sulfur Metabolite, Biochemistry, vol.51, issue.34, pp.6804-6815, 2012.

R. Jarabak and J. Westley, 3-Mercaptopyruvate sulfurtransferase: rapid equilibrium-ordered mechanism with cyanide as the acceptor substrate, Biochemistry, vol.19, issue.5, pp.900-904, 1980.

W. P. Jencks and J. Carriuolo, Reactivity of Nucleophilic Reagents toward Esters, Journal of the American Chemical Society, vol.82, issue.7, pp.1778-1786, 1960.

M. Jung, S. Kasamatsu, T. Matsunaga, S. Akashi, K. Ono et al., Protein polysulfidation-dependent persulfide dioxygenase activity of ethylmalonic encephalopathy protein 1, Biochemical and Biophysical Research Communications, vol.480, issue.2, pp.180-186, 2016.

O. Kabil and R. Banerjee, Characterization of Patient Mutations in Human Persulfide Dioxygenase (ETHE1) Involved in H2S Catabolism, Journal of Biological Chemistry, vol.287, issue.53, pp.44561-44567, 2012.

O. Kabil and R. Banerjee, Redox Biochemistry of Hydrogen Sulfide, Journal of Biological Chemistry, vol.285, issue.29, pp.21903-21907, 2010.

O. Kabil and R. Banerjee, Redox Biochemistry of Hydrogen Sulfide, Journal of Biological Chemistry, vol.285, issue.29, pp.21903-21907, 2010.

M. Karin and Y. Ben-neriah, Phosphorylation Meets Ubiquitination: The Control of NF-?B Activity, Annual Review of Immunology, vol.18, issue.1, pp.621-663, 2000.

K. Kashfi, Anti-Cancer Activity of New Designer Hydrogen Sulfide-Donating Hybrids, Antioxidants & Redox Signaling, vol.20, issue.5, pp.831-846, 2014.

T. W. Kensler, N. Wakabayashi, and S. Biswal, Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway, Annual Review of Pharmacology and Toxicology, vol.47, issue.1, pp.89-116, 2007.

H. Kimura, Hydrogen Sulfide and Polysulfide Signaling, Antioxidants & Redox Signaling, vol.27, issue.10, pp.619-621, 2017.

H. Kimura, Hydrogen polysulfide (H2S n ) signaling along with hydrogen sulfide (H2S) and nitric oxide (NO), Journal of Neural Transmission, vol.123, issue.11, pp.1235-1245, 2016.

H. Kimura, Hydrogen sulfide and polysulfides as signaling molecules, Proceedings of the Japan Academy, Series B, vol.91, issue.4, pp.131-159, 2015.

H. Kimura, Signaling Molecules: Hydrogen Sulfide and Polysulfide, Antioxidants & Redox Signaling, vol.22, issue.5, pp.362-376, 2015.

Y. Kimura, Y. Goto, and H. Kimura, Hydrogen Sulfide Increases Glutathione Production and Suppresses Oxidative Stress in Mitochondria, Antioxidants & Redox Signaling, vol.12, issue.1, pp.1-13, 2010.

Y. Kimura and H. Kimura, Hydrogen sulfide protects neurons from oxidative stress, The FASEB Journal, vol.18, issue.10, pp.1165-1167, 2004.

Y. Kimura, Y. Mikami, K. Osumi, M. Tsugane, J. Oka et al., Polysulfides are possible H 2 S?derived signaling molecules in rat brain, The FASEB Journal, vol.27, issue.6, pp.2451-2457, 2013.

Y. Kimura, Y. Toyofuku, S. Koike, N. Shibuya, N. Nagahara et al., Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain, Scientific Reports, vol.5, issue.1, p.14774, 2015.

A. Kobayashi, M. Kang, H. Okawa, M. Ohtsuji, Y. Zenke et al., Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2, Molecular and Cellular Biology, vol.24, issue.16, pp.7130-7139, 2004.

E. Lagoutte, S. Mimoun, M. Andriamihaja, C. Chaumontet, F. Blachier et al., Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1797, issue.8, pp.1500-1511, 2010.

A. P. Landry, D. P. Ballou, and R. Banerjee, H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase, Journal of Biological Chemistry, vol.292, issue.28, pp.11641-11649, 2017.

K. R. Leininger and J. Westley, The mechanism of the rhodanese-catalyzed thiosulfatecyanide reaction. Thermodynamic and activation parameters, J. Biol. Chem, vol.243, pp.1892-1899, 1968.

M. D. Levitt, M. S. Abdel-rehim, and J. Furne, Free and Acid-Labile Hydrogen Sulfide Concentrations in Mouse Tissues: Anomalously High Free Hydrogen Sulfide in Aortic Tissue, Antioxidants & Redox Signaling, vol.15, issue.2, pp.373-378, 2011.

H. Li, F. Yang, X. Kang, B. Xia, and C. Jin, Solution Structures and Backbone Dynamics of Escherichia coli Rhodanese PspE in Its Sulfur-Free and Persulfide-Intermediate Forms: Implications for the Catalytic Mechanism of Rhodanese?,?, Biochemistry, vol.47, issue.15, pp.4377-4385, 2008.

X. Li, M. Ellman, P. Muddasani, N. C. Wang, G. Cs-szabo et al., Prostaglandin E2and its cognate EP receptors control human adult articular cartilage homeostasis and are linked to the pathophysiology of osteoarthritis, Arthritis & Rheumatism, vol.60, issue.2, pp.513-523, 2009.

M. Libiad, P. K. Yadav, V. Vitvitsky, M. Martinov, and R. Banerjee, Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway, Journal of Biological Chemistry, vol.289, issue.45, pp.30901-30910, 2014.

D. R. Linden, J. Furne, G. J. Stoltz, M. S. Abdel-rehim, M. D. Levitt et al., Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the CNS, British Journal of Pharmacology, vol.165, issue.7, pp.2178-2190, 2012.

S. Ling, W. Wang, L. Yu, J. Peng, X. Cai et al., Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN? binding defined by EPR-based hybrid method, Scientific Reports, vol.6, issue.1, 2016.

A. R. Lippert, E. J. New, and C. J. Chang, Reaction-Based Fluorescent Probes for Selective Imaging of Hydrogen Sulfide in Living Cells, Journal of the American Chemical Society, vol.133, issue.26, pp.10078-10080, 2011.

A. K. Macleod, M. Mcmahon, S. M. Plummer, L. G. Higgins, T. M. Penning et al., Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1?NRF2 pathway, and not the BACH1?NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds, Carcinogenesis, vol.30, issue.9, pp.1571-1580, 2009.

A. Matthies, M. Nimtz, and S. Leimkühler, Molybdenum Cofactor Biosynthesis in Humans: Identification of a Persulfide Group in the Rhodanese-like Domain of MOCS3 by Mass Spectrometry?, Biochemistry, vol.44, issue.21, pp.7912-7920, 2005.

J. G. Mccoy, C. A. Bingman, E. Bitto, M. M. Holdorf, C. A. Makaroff et al., Structure of an ETHE1-like protein fromArabidopsis thaliana, Acta Crystallographica Section D Biological Crystallography, vol.62, issue.9, pp.964-970, 2006.

S. L. Melideo, M. R. Jackson, and M. S. Jorns, Biosynthesis of a Central Intermediate in Hydrogen Sulfide Metabolism by a Novel Human Sulfurtransferase and Its Yeast Ortholog, Biochemistry, vol.53, issue.28, pp.4739-4753, 2014.

Y. Mikami and H. Kimura, A mechanism of retinal protection from light-induced degeneration by hydrogen sulfide, Communicative & Integrative Biology, vol.5, issue.2, pp.169-171, 2012.

Y. Mikami, N. Shibuya, Y. Kimura, N. Nagahara, Y. Ogasawara et al., Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide, Biochemical Journal, vol.439, issue.3, pp.479-485, 2011.

S. Mimoun, M. Andriamihaja, C. Chaumontet, C. Atanasiu, R. Benamouzig et al., Detoxification of H2S by Differentiated Colonic Epithelial Cells: Implication of the Sulfide Oxidizing Unit and of the Cell Respiratory Capacity, Antioxidants & Redox Signaling, vol.17, issue.1, pp.1-10, 2012.
URL : https://hal.archives-ouvertes.fr/hal-00966772

J. Mitchell, P. Paul, H. Chen, A. Morris, M. Payling et al., Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase, Proceedings of the National Academy of Sciences, vol.107, issue.16, pp.7556-7561, 2010.

K. Módis, C. Coletta, K. Erdélyi, A. Papapetropoulos, and C. Szabo, Intramitochondrial hydrogen sulfide production by 3?mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics, The FASEB Journal, vol.27, issue.2, pp.601-611, 2012.

K. Módis, P. Panopoulos, C. Coletta, A. Papapetropoulos, and C. Szabo, Hydrogen sulfide-mediated stimulation of mitochondrial electron transport involves inhibition of the mitochondrial phosphodiesterase 2A, elevation of cAMP and activation of protein kinase A, Biochemical Pharmacology, vol.86, issue.9, pp.1311-1319, 2013.

R. R. Moest, Hydrogen sulfide determination by the methylene blue method, Analytical Chemistry, vol.47, issue.7, pp.1204-1205, 1975.

M. N. Möller, J. R. Lancaster, and A. Denicola, Chapter 2 The Interaction of Reactive Oxygen and Nitrogen Species with Membranes, Free Radical Effects on Membranes, vol.61, pp.23-42, 2008.

N. M. Morton, J. Beltram, R. N. Carter, Z. Michailidou, G. Gorjanc et al., Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness, Nature Medicine, vol.22, issue.7, pp.771-779, 2016.

E. Mössner, M. Huber-wunderlich, and R. Glockshuber, Characterization ofEscherichia colithioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases, Protein Science, vol.7, issue.5, pp.1233-1244, 1998.

N. Motl, M. A. Skiba, O. Kabil, J. L. Smith, and R. Banerjee, Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase?rhodanese fusion protein functions in sulfur assimilation, Journal of Biological Chemistry, vol.292, issue.34, pp.14026-14038, 2017.

E. G. Mueller, P. M. Palenchar, and C. J. Buck, The Role of the Cysteine Residues of ThiI in the Generation of 4-Thiouridine in tRNA, Journal of Biological Chemistry, vol.276, issue.36, pp.33588-33595, 2001.

S. B. Mulrooney, Application of a Single-Plasmid Vector for Mutagenesis and High-Level Expression of Thioredoxin Reductase and Its Use to Examine Flavin Cofactor Incorporation, Protein Expression and Purification, vol.9, issue.3, pp.372-378, 1997.

A. K. Mustafa, M. M. Gadalla, N. Sen, S. Kim, W. Mu et al., H2S Signals Through Protein S-Sulfhydration, Science Signaling, vol.2, issue.96, pp.ra72-ra72, 2009.

N. Nagahara, T. Ito, H. Kitamura, and T. Nishino, Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis, Histochemistry and Cell Biology, vol.110, issue.3, pp.243-250, 1998.

N. Nagahara, Q. Li, and N. Sawada, Do Antidotes for Acute Cyanide Poisoning Act on Mercaptopyruvate Sulfurtransferase to Facilitate Detoxification?, Current Drug Targets - Immune, Endocrine & Metabolic Disorders, vol.3, issue.3, pp.198-204, 2003.

N. Nagahara, M. Nagano, T. Ito, K. Shimamura, T. Akimoto et al., Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: a model for human mercaptolactate-cysteine disulfiduria, Scientific Reports, vol.3, issue.1, 2013.

N. Nagahara and T. Nishino, Role of Amino Acid Residues in the Active Site of Rat Liver Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.271, issue.44, pp.27395-27401, 1996.

D. L. Nandi and J. Westley, Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese, The International Journal of Biochemistry & Cell Biology, vol.30, issue.9, pp.973-977, 1998.

P. Neta and R. E. Huie, Free-radical chemistry of sulfite., Environmental Health Perspectives, vol.64, pp.209-217, 1985.

E. A. Nudler and K. Shatalin, Methods for treating infections by targeting microbial h2s-producing enzymes, 2012.

N. Oganesyan, I. Ankoudinova, S. Kim, and R. Kim, Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization, Protein Expression and Purification, vol.52, issue.2, pp.280-285, 2007.

Y. Ogasawara, K. Ishii, T. Togawa, and S. Tanabe, Determination of Bound Sulfur in Serum by Gas Dialysis/High-Performance Liquid Chromatography, Analytical Biochemistry, vol.215, issue.1, pp.73-81, 1993.

Y. Ogasawara, G. Lacourciere, and T. C. Stadtman, Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system, Proceedings of the National Academy of Sciences, vol.98, issue.17, pp.9494-9498, 2001.

K. R. Olson, J. A. Donald, R. A. Dombkowski, and S. F. Perry, Evolutionary and comparative aspects of nitric oxide, carbon monoxide and hydrogen sulfide, Respiratory Physiology & Neurobiology, vol.184, issue.2, pp.117-129, 2012.

K. Ono, T. Akaike, T. Sawa, Y. Kumagai, D. A. Wink et al., Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: Implications of their possible biological activity and utility, Free Radical Biology and Medicine, vol.77, pp.82-94, 2014.

J. M. Osmond and N. L. Kanagy, Modulation of hydrogen sulfide by vascular hypoxia, Hypoxia, vol.2, pp.117-126, 2014.

O. Ozsoy, S. Aras, A. Ozkan, H. Parlak, M. Aslan et al., The effect of ingested sulfite on visual evoked potentials, lipid peroxidation, and antioxidant status of brain in normal and sulfite oxidase-deficient aged rats, Toxicology and Industrial Health, vol.32, issue.7, pp.1197-1207, 2014.

A. Papapetropoulos, A. Pyriochou, Z. Altaany, G. Yang, A. Marazioti et al., Hydrogen sulfide is an endogenous stimulator of angiogenesis, Proceedings of the National Academy of Sciences, vol.106, issue.51, pp.21972-21977, 2009.

S. Park and J. A. Imlay, High Levels of Intracellular Cysteine Promote Oxidative DNA Damage by Driving the Fenton Reaction, Journal of Bacteriology, vol.185, issue.6, pp.1942-1950, 2003.

S. E. Patterson, B. Moeller, H. T. Nagasawa, R. Vince, D. L. Crankshaw et al., Development of sulfanegen for mass cyanide casualties, Annals of the New York Academy of Sciences, vol.1374, issue.1, pp.202-209, 2016.

S. E. Patterson, A. R. Monteil, J. F. Cohen, D. L. Crankshaw, R. Vince et al., Cyanide Antidotes for Mass Casualties: Water-Soluble Salts of the Dithiane (Sulfanegen) from 3-Mercaptopyruvate for Intramuscular Administration, Journal of Medicinal Chemistry, vol.56, issue.3, pp.1346-1349, 2013.

L. Pecci, B. Pensa, M. Costa, P. L. Cignini, and C. Cannella, Reaction of rhodanese with dithiothreitol, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.445, issue.1, pp.104-111, 1976.

I. Pettinati, J. Brem, M. A. Mcdonough, and C. J. Schofield, Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy, Human Molecular Genetics, vol.24, issue.9, pp.2458-2469, 2015.

A. M. Pickering, R. A. Linder, H. Zhang, H. J. Forman, and K. J. Davies, Nrf2-dependent Induction of Proteasome and Pa28?? Regulator Are Required for Adaptation to Oxidative Stress, Journal of Biological Chemistry, vol.287, issue.13, pp.10021-10031, 2012.

R. Picton, M. C. Eggo, G. A. Merrill, M. J. Langman, and S. Singh, Mucosal protection against sulphide: importance of the enzyme rhodanese, Gut, vol.50, issue.2, pp.201-205, 2002.

J. H. Ploegman, G. Drent, K. H. Kalk, and W. G. Hol, Structure of bovine liver rhodanese. I. Structure determination at 2.5 A resolution and a comparison of the conformation and sequence of its two domains, J. Mol. Biol, vol.123, pp.557-594, 1978.

Z. Rasheed, N. Rasheed, and A. Alghasham, Lactoferrin from Camelus dromedarius inhibits nuclear transcription Factor-kappa B activation, cyclooxygenase-2 expression and prostaglandin E2 production in stimulated human chondrocytes, Pharmacognosy Research, vol.8, issue.2, p.135, 2016.

W. K. Ray, G. Zeng, M. B. Potters, A. M. Mansuri, and T. J. Larson, Characterization of a 12-Kilodalton Rhodanese Encoded byglpE of Escherichia coli and Its Interaction with Thioredoxin, Journal of Bacteriology, vol.182, issue.8, pp.2277-2284, 2000.

S. I. Reja, N. Sharma, M. Gupta, P. Bajaj, V. Bhalla et al., A Highly Selective Fluorescent Probe for Detection of Hydrogen Sulfide in Living Systems: In Vitro and in Vivo Applications, Chemistry - A European Journal, vol.23, issue.41, pp.9872-9878, 2017.

S. Riahi and C. N. Rowley, Why Can Hydrogen Sulfide Permeate Cell Membranes?, Journal of the American Chemical Society, vol.136, issue.43, pp.15111-15113, 2014.

J. Ricard, J. Meunier, and J. Buc, Regulatory Behavior of Monomeric Enzymes. 1. The Mnemonical Enzyme Concept, European Journal of Biochemistry, vol.49, issue.1, pp.195-208, 1974.

D. Rickard and G. W. Luther, Chemistry of iron sulfides, Chem. Rev, vol.107, pp.514-562, 2007.

K. Robert, F. Vialard, E. Thiery, K. Toyama, P. Sinet et al., Expression of the cystathionine beta synthase (CBS) gene during mouse development and immunolocalization in adult brain, J. Histochem. Cytochem. Off. J. Histochem. Soc, vol.51, pp.363-371, 2003.

G. A. Rockwood, D. E. Thompson, and I. Petrikovics, Dimethyl trisulfide, Toxicology and Industrial Health, vol.32, issue.12, pp.2009-2016, 2016.

W. E. Roediger, J. Moore, and W. Babidge, Colonic sulfide in pathogenesis and treatment of ulcerative colitis, Digestive Diseases and Sciences, vol.42, issue.8, pp.1571-1579, 1997.

S. A. Sattler, X. Wang, K. M. Lewis, P. J. Dehan, C. Park et al., Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-?-lactamase Superfamily, Journal of Biological Chemistry, vol.290, issue.31, pp.18914-18923, 2015.

J. C. Savage and D. H. Gould, Determination of sulfide in brain tissue and rumen fluid by ion-interaction reversed-phase high-performance liquid chromatography, Journal of Chromatography B: Biomedical Sciences and Applications, vol.526, pp.540-545, 1990.

U. Schumann and S. Subramani, Special delivery from mitochondria to peroxisomes, Trends in Cell Biology, vol.18, issue.6, pp.253-256, 2008.

D. G. Searcy and S. H. Lee, Sulfur reduction by human erythrocytes, The Journal of Experimental Zoology, vol.282, issue.3, pp.310-322, 1998.

K. Shatalin, E. Shatalina, A. Mironov, and E. Nudler, H2S: a universal defense against antibiotics in bacteria, Science, vol.334, pp.986-990, 2011.

X. Shen, C. B. Pattillo, S. Pardue, S. C. Bir, R. Wang et al., Measurement of plasma hydrogen sulfide in vivo and in vitro. Free Radic, Biol. Med, vol.50, pp.1021-1031, 2011.

X. Shen, E. A. Peter, S. Bir, R. Wang, and C. G. Kevil, Analytical measurement of discrete hydrogen sulfide pools in biological specimens, Free Radical Biology and Medicine, vol.52, issue.11-12, pp.2276-2283, 2012.

N. Shibuya, S. Koike, M. Tanaka, M. Ishigami-yuasa, Y. Kimura et al., A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells, Nat. Commun, vol.4, p.1366, 2013.

N. Shibuya, Y. Mikami, Y. Kimura, N. Nagahara, and H. Kimura, Vascular Endothelium Expresses 3-Mercaptopyruvate Sulfurtransferase and Produces Hydrogen Sulfide, Journal of Biochemistry, vol.146, issue.5, pp.623-626, 2009.

N. Shibuya, M. Tanaka, M. Yoshida, Y. Ogasawara, T. Togawa et al., 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide that is stored as bound sulfane sulfur in the brain, Neuroscience Research, vol.65, p.S57, 2009.

E. Shigetomi, O. Jackson-weaver, R. T. Huckstepp, T. J. O'dell, and B. S. Khakh, TRPA1 Channels Are Regulators of Astrocyte Basal Calcium Levels and Long-Term Potentiation via Constitutive D-Serine Release, Journal of Neuroscience, vol.33, issue.24, pp.10143-10153, 2013.

V. E. Shih, I. F. Abroms, J. L. Johnson, M. Carney, R. Mandell et al., Sulfite Oxidase Deficiency, New England Journal of Medicine, vol.297, issue.19, pp.1022-1028, 1977.

A. Smirnov, C. Comte, A. Mager-heckel, V. Addis, I. A. Krasheninnikov et al., Mitochondrial Enzyme Rhodanese Is Essential for 5 S Ribosomal RNA Import into Human Mitochondria, Journal of Biological Chemistry, vol.285, issue.40, pp.30792-30803, 2010.

A. Smirnov, N. Entelis, R. P. Martin, and I. Tarassov, Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18, Genes & Development, vol.25, issue.12, pp.1289-1305, 2011.

A. Smirnov, I. Tarassov, A. Mager-heckel, M. Letzelter, R. P. Martin et al., Two distinct structural elements of 5S rRNA are needed for its import into human mitochondria, RNA, vol.14, issue.4, pp.749-759, 2008.

A. Spallarossa, J. L. Donahue, T. J. Larson, M. Bolognesi, and D. Bordo, Escherichia coli GlpE Is a Prototype Sulfurtransferase for the Single-Domain Rhodanese Homology Superfamily, Structure, vol.9, issue.11, pp.1117-1125, 2001.

A. Spallarossa, F. Forlani, A. Carpen, A. Armirotti, S. Pagani et al., The ""Rhodanese"" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli, J. Mol. Biol, vol.335, pp.583-593, 2003.

G. Stein, G. Rao, S. Duron, S. G. Chapman, J. Sydserff et al., Use of cse inhibitors for the treatment of cutaneous injuries or conditions and sleep-related breathing disorders, 2016.

M. H. Stipanuk, Metabolism of Sulfur-Containing Amino Acids, Annual Review of Nutrition, vol.6, issue.1, pp.179-209, 1986.

M. H. Stipanuk and P. W. Beck, Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat, Biochemical Journal, vol.206, issue.2, pp.267-277, 1982.

M. H. Stipanuk, J. E. Dominy, J. Lee, and R. M. Coloso, Mammalian Cysteine Metabolism: New Insights into Regulation of Cysteine Metabolism, The Journal of Nutrition, vol.136, issue.6, pp.1652S-1659S, 2006.

Y. Sun, Y. Cao, W. Wang, S. Ma, T. Yao et al., Hydrogen sulphide is an inhibitor of L-type calcium channels and mechanical contraction in rat cardiomyocytes, Cardiovascular Research, vol.79, issue.4, pp.632-641, 2008.

M. Swaroop, K. Bradley, T. Ohura, T. Tahara, M. D. Roper et al., Rat cystathionine beta-synthase. Gene organization and alternative splicing, J. Biol. Chem, vol.267, pp.11455-11461, 1992.

D. M. Sylvester and C. Sander, Immunohistochemical localization of rhodanese, The Histochemical Journal, vol.22, issue.4, pp.197-200, 1990.

C. Szabo, C. Coletta, C. Chao, K. Modis, B. Szczesny et al., Tumor-derived hydrogen sulfide, produced by cystathionine- -synthase, stimulates bioenergetics, cell proliferation, and angiogenesis in colon cancer, Proceedings of the National Academy of Sciences, vol.110, issue.30, pp.12474-12479, 2013.

R. L. Tatusov, M. Y. Galperin, D. A. Natale, and E. V. Koonin, The COG database: a tool for genome-scale analysis of protein functions and evolution, Nucleic Acids Research, vol.28, issue.1, pp.33-36, 2000.

H. Teng, B. Wu, K. Zhao, G. Yang, L. Wu et al., Oxygen-sensitive mitochondrial accumulation of cystathionine -synthase mediated by Lon protease, Proceedings of the National Academy of Sciences, vol.110, issue.31, pp.12679-12684, 2013.

J. G. Thomas and F. Baneyx, Protein Misfolding and Inclusion Body Formation in RecombinantEscherichia coliCells Overexpressing Heat-shock Proteins, Journal of Biological Chemistry, vol.271, issue.19, pp.11141-11147, 1996.

V. Tiranti, P. D?adamo, E. Briem, G. Ferrari, R. Mineri et al., Ethylmalonic Encephalopathy Is Caused by Mutations in ETHE1, a Gene Encoding a Mitochondrial Matrix Protein, The American Journal of Human Genetics, vol.74, issue.2, pp.239-252, 2004.

V. Tiranti, C. Viscomi, T. Hildebrandt, I. Di-meo, R. Mineri et al., Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy, Nature Medicine, vol.15, issue.2, pp.200-205, 2009.

V. Tiranti and M. Zeviani, Altered Sulfide (H2S) Metabolism in Ethylmalonic Encephalopathy, Cold Spring Harbor Perspectives in Biology, vol.5, issue.1, pp.a011437-a011437, 2013.

J. I. Toohey, The conversion of H2S to sulfane sulfur, Nature Reviews Molecular Cell Biology, vol.13, issue.12, pp.803-803, 2012.

T. P. Vacek, N. Qipshidze, and S. C. Tyagi, Hydrogen sulfide and sodium nitroprusside compete to activate/deactivate MMPs in bone tissue homogenates. Vasc. Health Risk Manag, vol.9, pp.117-123, 2013.

V. Vitvitsky, P. K. Yadav, A. Kurthen, and R. Banerjee, Sulfide Oxidation by a Noncanonical Pathway in Red Blood Cells Generates Thiosulfate and Polysulfides, Journal of Biological Chemistry, vol.290, issue.13, pp.8310-8320, 2015.

J. L. Wallace and R. Wang, Hydrogen sulfide-based therapeutics: exploiting a unique but ubiquitous gasotransmitter, Nature Reviews Drug Discovery, vol.14, issue.5, pp.329-345, 2015.

F. Wan, D. E. Anderson, R. A. Barnitz, A. Snow, N. Bidere et al., Ribosomal Protein S3: A KH Domain Subunit in NF-?B Complexes that Mediates Selective Gene Regulation, Cell, vol.131, issue.5, pp.927-939, 2007.

R. Wang, Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed, Physiological Reviews, vol.92, issue.2, pp.791-896, 2012.

R. Wang, Two's company, three's a crowd: can H 2 S be the third endogenous gaseous transmitter?, The FASEB Journal, vol.16, issue.13, pp.1792-1798, 2002.

M. W. Warenycia, L. R. Goodwin, C. G. Benishin, R. J. Reiffenstein, D. M. Francom et al., Acute hydrogen sulfide poisoning, Biochemical Pharmacology, vol.38, issue.6, pp.973-981, 1989.

K. Wenzel, S. B. Felix, C. Flachmeier, P. Heere, W. Schulze et al., Identification and Characterization of KAT, a Novel Gene Preferentially Expressed in Several Human Cancer Cell Lines, Biological Chemistry, vol.384, issue.5, pp.763-775, 2003.

J. Westley, [37] Thiosulfate: Cyanide sulfurtransferase (Rhodanese), Methods in Enzymology, vol.77, pp.285-291, 1981.

J. Westley and D. Heyse, Mechanisms of sulfur transfer catalysis. Sulfhydryl-catalyzed transfer of thiosulfonate sulfur, J. Biol. Chem, vol.246, pp.1468-1474, 1971.

J. Westley and T. Nakamoto, Mechanism of rhodanese action: isotopic tracer studies, J. Biol. Chem, vol.237, pp.547-549, 1962.

G. D. Westrop, I. Georg, and G. H. Coombs, The Mercaptopyruvate Sulfurtransferase of Trichomonas vaginalis Links Cysteine Catabolism to the Production of Thioredoxin Persulfide, Journal of Biological Chemistry, vol.284, issue.48, pp.33485-33494, 2009.

D. B. Whitehouse, C. J. Poole, P. R. Kind, and D. A. Hopkinson, Rhodanese isozymes in three subjects with Leber's optic neuropathy., Journal of Medical Genetics, vol.26, issue.2, pp.113-115, 1989.

N. L. Whitfield, E. L. Kreimier, F. C. Verdial, N. Skovgaard, and K. R. Olson, Reappraisal of H2S/sulfide concentration in vertebrate blood and its potential significance in ischemic preconditioning and vascular signaling, American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, vol.294, issue.6, pp.R1930-R1937, 2008.

R. A. Williams, S. M. Kelly, J. C. Mottram, and G. H. Coombs, 3-Mercaptopyruvate Sulfurtransferase of LeishmaniaContains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism, Journal of Biological Chemistry, vol.278, issue.3, pp.1480-1486, 2002.

M. D. Wolfe, F. Ahmed, G. M. Lacourciere, C. T. Lauhon, T. C. Stadtman et al., Functional Diversity of the Rhodanese Homology Domain, Journal of Biological Chemistry, vol.279, issue.3, pp.1801-1809, 2003.

P. K. Yadav, M. Martinov, V. Vitvitsky, J. Seravalli, R. Wedmann et al., Biosynthesis and Reactivity of Cysteine Persulfides in Signaling, Journal of the American Chemical Society, vol.138, issue.1, pp.289-299, 2015.

P. K. Yadav, K. Yamada, T. Chiku, M. Koutmos, and R. Banerjee, Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase, Journal of Biological Chemistry, vol.288, issue.27, pp.20002-20013, 2013.

H. Yamasaki, The NO world for plants: achieving balance in an open system, Plant, Cell and Environment, vol.28, issue.1, pp.78-84, 2005.

H. Yamasaki and M. F. Cohen, Biological consilience of hydrogen sulfide and nitric oxide in plants: Gases of primordial earth linking plant, microbial and animal physiologies, Nitric Oxide, vol.55-56, pp.91-100, 2016.

W. Zhao, J. Zhang, Y. Lu, and R. Wang, The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener, The EMBO Journal, vol.20, issue.21, pp.6008-6016, 2001.