메뉴 건너뛰기




Volumn 77, Issue , 2014, Pages 82-94

Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: Implications of their possible biological activity and utility

Author keywords

Hydrogen sulfide; Persulfides; Polysulfides; Thiol redox; Thiols

Indexed keywords

HYDROGEN SULFIDE; METAL; PEROXIDE; SULFUR DERIVATIVE; DISULFIDE;

EID: 84908432800     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.09.007     Document Type: Review
Times cited : (344)

References (102)
  • 1
    • 84860117196 scopus 로고    scopus 로고
    • Physiological implications of hydrogen sulfide: A whiff exploration that blossomed
    • Wang, R. Physiological implications of hydrogen sulfide: a whiff exploration that blossomed. Physiol. Rev. 92(791-896):2012; 2012.
    • (2012) Physiol. Rev. , vol.92 , Issue.791-896 , pp. 2012
    • Wang, R.1
  • 2
    • 78651457395 scopus 로고    scopus 로고
    • Hydrogen sulfide: Its production, release and functions
    • Kimura, H. Hydrogen sulfide: its production, release and functions. Amino Acids 41:113-121; 2011.
    • (2011) Amino Acids , vol.41 , pp. 113-121
    • Kimura, H.1
  • 3
    • 84873410143 scopus 로고    scopus 로고
    • Biology and therapeutic potential of hydrogen sulfide and hydrogen sulfide-releasing chimeras
    • Kashfi, K.; Olson, K. R. Biology and therapeutic potential of hydrogen sulfide and hydrogen sulfide-releasing chimeras. Biochem. Pharmacol. 85:689-703; 2013.
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 689-703
    • Kashfi, K.1    Olson, K.R.2
  • 8
    • 63049105151 scopus 로고    scopus 로고
    • Hydrogen sulfide and the vasculature: A novel vasculoprotective entity and regulator of nitric oxide bioavailability
    • Whiteman, M.; Moore, P. K. Hydrogen sulfide and the vasculature: a novel vasculoprotective entity and regulator of nitric oxide bioavailability. J. Cell. Mol. Med. 13:488-507; 2009.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 488-507
    • Whiteman, M.1    Moore, P.K.2
  • 9
    • 84890121826 scopus 로고    scopus 로고
    • Chemical aspects of hydrogen sulfide measurements in physiological samples
    • Nagy, P.; Palinkas, Z.; Nagy, A.; Budai, B.; Toth, I.; Vasas, A. Chemical aspects of hydrogen sulfide measurements in physiological samples. Biochim. Biophys. Acta 1840:876-891; 2014.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 876-891
    • Nagy, P.1    Palinkas, Z.2    Nagy, A.3    Budai, B.4    Toth, I.5    Vasas, A.6
  • 10
    • 84859857546 scopus 로고    scopus 로고
    • Small molecule signaling agents: The integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide and their derived species
    • Fukuto, J. M.; Carrington, S. J.; Tantillo, D. J.; Harrison, J. G; Ignarro, L. J.; Freeman, B. A.; Chen, A.; Wink, D. A. Small molecule signaling agents: the integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide and their derived species. Chem. Res. Toxicol. 25:769-793; 2012.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 769-793
    • Fukuto, J.M.1    Carrington, S.J.2    Tantillo, D.J.3    Harrison, J.G.4    Ignarro, L.J.5    Freeman, B.A.6    Chen, A.7    Wink, D.A.8
  • 12
    • 85044685848 scopus 로고
    • Nomenclature of organic chemistry: Definitive rules for section c. Characteristic groups containing carbon, hydrogen, oxygen, nitrogen, halogen, sulfur, selenium and/or tellurium
    • Verkade, P. E.; Cahn, R. S.; Capell, L. T.; Dyson, G. M.; Kersaint, G.; Lozac'h, N.; Mitchell, A. D.; Nutting, H. S.; Richter, F.; Veibel, S. Nomenclature of organic chemistry: definitive rules for section c. Characteristic groups containing carbon, hydrogen, oxygen, nitrogen, halogen, sulfur, selenium and/or tellurium. Int. Union Pure Appl. Chem 11:260; 1965.
    • (1965) Int. Union Pure Appl. Chem , vol.11 , pp. 260
    • Verkade, P.E.1    Cahn, R.S.2    Capell, L.T.3    Dyson, G.M.4    Kersaint, G.5    Lozac'h, N.6    Mitchell, A.D.7    Nutting, H.S.8    Richter, F.9    Veibel, S.10
  • 13
    • 84881513267 scopus 로고    scopus 로고
    • Chemical foundations of hydrogen sulfide biology
    • Li, Q.; Lancaster Jr. J. R. Chemical foundations of hydrogen sulfide biology. Nitric Oxide 35:21-34; 2013.
    • (2013) Nitric Oxide , vol.35 , pp. 21-34
    • Li, Q.1    Lancaster, J.R.2
  • 14
    • 84881191992 scopus 로고    scopus 로고
    • Hydrogen sulfide chemical biology: Pathophysiological roles and detection
    • Kolluru, G. K.; Shen, X.; Bir, S. C.; Kevil, C. G. Hydrogen sulfide chemical biology: pathophysiological roles and detection. Nitric Oxide 35:5-20; 2013.
    • (2013) Nitric Oxide , vol.35 , pp. 5-20
    • Kolluru, G.K.1    Shen, X.2    Bir, S.C.3    Kevil, C.G.4
  • 15
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil, O.; Banerjee, R. Redox biochemistry of hydrogen sulfide. J. Biol. Chem. 285:21903-21907; 2010.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 17
    • 0001874683 scopus 로고
    • Reduction potentials involving inorganic free radicals in aqueous solution
    • Stanbury, D. M. Reduction potentials involving inorganic free radicals in aqueous solution. Adv. Inorg. Chem. 33:69-138; 1989.
    • (1989) Adv. Inorg. Chem. , vol.33 , pp. 69-138
    • Stanbury, D.M.1
  • 19
    • 42149180604 scopus 로고    scopus 로고
    • The interaction of human neuroglobin with hydrogen sulphide
    • Brittain, T.; Yosaatmadja, Y.; Henty, K. The interaction of human neuroglobin with hydrogen sulphide. IUBMB Life 60:135-138; 2008.
    • (2008) IUBMB Life , vol.60 , pp. 135-138
    • Brittain, T.1    Yosaatmadja, Y.2    Henty, K.3
  • 21
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacterial symbiosis
    • Kraus, D. W.; Wittenberg, J. B. Hemoglobins of the Lucina pectinata/bacterial symbiosis. J. Biol. Chem. 265:16043-16053; 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 22
    • 0025167226 scopus 로고
    • Hemoglobins of the Lucina/ bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of ferric proteins
    • Kraus, D. W.; Wittenberg, J. B.; Lu, J. F.; Peisach, J. Hemoglobins of the Lucina/ bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of ferric proteins. J. Biol. Chem. 265:16054-16059; 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16054-16059
    • Kraus, D.W.1    Wittenberg, J.B.2    Lu, J.F.3    Peisach, J.4
  • 23
    • 0029945653 scopus 로고    scopus 로고
    • Structural bases for sulfide recognition in Lucina pectinata hemoglobin I
    • Rizzi,M.; Wittenberg, J. B.; Coda, A.; Ascenzi, P.; Bolognesi, M. Structural bases for sulfide recognition in Lucina pectinata hemoglobin I. J. Mol. Biol. 258:1-5; 1996.
    • (1996) J. Mol. Biol. , vol.258 , pp. 1-5
    • Rizzi, M.1    Wittenberg, J.B.2    Coda, A.3    Ascenzi, P.4    Bolognesi, M.5
  • 24
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: An X-ray crystallographic study
    • Bolognesi, M.; Rosano, C.; Losso, R.; Borassi, A.; Rizzi, M.; Wittenberg, J. B.; Boffi, A.; Ascenzi, P. Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-ray crystallographic study. Biophys. J. 77:1093-1099; 1999.
    • (1999) Biophys. J. , vol.77 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5    Wittenberg, J.B.6    Boffi, A.7    Ascenzi, P.8
  • 25
    • 0034684222 scopus 로고    scopus 로고
    • 2S solubility via the reaction with ferric hemoglobin I from the bivalve mollusk Lucina pectinata
    • 2S solubility via the reaction with ferric hemoglobin I from the bivalve mollusk Lucina pectinata. Biochim. Biophys. Acta 1523:206-208; 2000.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 206-208
    • Boffi, A.1    Rizzi, M.2    Monacelli, F.3    Ascenzi, P.4
  • 27
    • 0032540246 scopus 로고    scopus 로고
    • Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata
    • Nguyen, B.; Zhao, X.; Vyas, K.; LaMar, G. N.; Lile, A.; Brucker, E. A.; Phillips Jr. G. N.; Olson, J. S.; Wittenberg, J. B. Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata. J. Biol. Chem. 273:9517-9526; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9517-9526
    • Nguyen, B.1    Zhao, X.2    Vyas, K.3    LaMar, G.N.4    Lile, A.5    Brucker, E.A.6    Phillips, G.N.7    Olson, J.S.8    Wittenberg, J.B.9
  • 31
    • 0036146130 scopus 로고    scopus 로고
    • Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: Correlation with tissue sulfide concentrations in the rat brain, liver, lung and nasal epithelium
    • Dorman, D. C.; Moulin, F. J. -M.; McManus, B. E.; Mahle, K. C.; James, R. A.; Struve, M. F. Cytochrome oxidase inhibition induced by acute hydrogen sulfide inhalation: correlation with tissue sulfide concentrations in the rat brain, liver, lung and nasal epithelium. Toxicol. Sci. 65:18-25; 2002.
    • (2002) Toxicol. Sci. , vol.65 , pp. 18-25
    • Dorman, D.C.1    Moulin, F.J.M.2    McManus, B.E.3    Mahle, K.C.4    James, R.A.5    Struve, M.F.6
  • 33
    • 34247093873 scopus 로고    scopus 로고
    • Suspended animation-like state protects mice from lethal hypoxia
    • Blackstone, E.; Roth, M. B. Suspended animation-like state protects mice from lethal hypoxia. Shock 27:370-372; 2007.
    • (2007) Shock , vol.27 , pp. 370-372
    • Blackstone, E.1    Roth, M.B.2
  • 34
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance
    • Cooper, C. E.; Brown, G. C. The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance. J. Bioeng. Biomembr 40:533-539; 2008.
    • (2008) J. Bioeng. Biomembr , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 35
    • 0022554531 scopus 로고
    • Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of Solemya reidi
    • Powell, M. A.; Somero, G. N. Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of Solemya reidi. Science 233:563-566; 1986.
    • (1986) Science , vol.233 , pp. 563-566
    • Powell, M.A.1    Somero, G.N.2
  • 36
    • 0035030625 scopus 로고    scopus 로고
    • Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria
    • Yong, R.; Searcy, D. G. Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria. Comp. Biochem. Physiol. Part B 129:129-137; 2001.
    • (2001) Comp. Biochem. Physiol. Part B , vol.129 , pp. 129-137
    • Yong, R.1    Searcy, D.G.2
  • 38
    • 76049087222 scopus 로고    scopus 로고
    • Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation
    • Collman, J. P.; Ghosh, S.; Dey, A.; Decreau, R. A. Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation. Proc. Natl. Acad. Sci. USA 106:22090-22095; 2009.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22090-22095
    • Collman, J.P.1    Ghosh, S.2    Dey, A.3    Decreau, R.A.4
  • 39
    • 57349171934 scopus 로고    scopus 로고
    • Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values
    • Furne, J.; Saeed, A.; Levitt, M. D. Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values. Am. J. Physiol. Regul. Integr. Comp. Physiol 295:R1479-R1485; 2008.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.295 , pp. R1479-R1485
    • Furne, J.1    Saeed, A.2    Levitt, M.D.3
  • 41
    • 77958095282 scopus 로고    scopus 로고
    • Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides
    • Nagy, P.; Winterbourn, C. C. Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides. Chem. Res. Toxicol. 23:1541-1543; 2010.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1541-1543
    • Nagy, P.1    Winterbourn, C.C.2
  • 44
    • 84875712387 scopus 로고    scopus 로고
    • Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways
    • Nagy, P. Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways. Antiox. Redox Signal 18:1623-1641; 2013.
    • (2013) Antiox. Redox Signal , vol.18 , pp. 1623-1641
    • Nagy, P.1
  • 45
    • 79953712285 scopus 로고    scopus 로고
    • Sulfur signaling: Is the agent sulfide or sulfane
    • Toohey, J. I. Sulfur signaling: is the agent sulfide or sulfane. Anal. Biochem. 413:1-7; 2011.
    • (2011) Anal. Biochem. , vol.413 , pp. 1-7
    • Toohey, J.I.1
  • 46
    • 0019577528 scopus 로고
    • The mechanism of the L-cystine cleavage reaction catalyzed by rat liver γ-cystathionase
    • Yamanishi, T.; Tuboi, S. The mechanism of the L-cystine cleavage reaction catalyzed by rat liver γ-cystathionase. J. Biochem. 89:1913-1921; 1981.
    • (1981) J. Biochem. , vol.89 , pp. 1913-1921
    • Yamanishi, T.1    Tuboi, S.2
  • 47
    • 0022464168 scopus 로고
    • Metabolism of sulfur-containing amino acids
    • Stipanuk, M. Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 6:179-209; 1986.
    • (1986) Annu. Rev. Nutr. , vol.6 , pp. 179-209
    • Stipanuk, M.1
  • 48
    • 3142685079 scopus 로고    scopus 로고
    • Extracellular thiols and thiol/disulfide redox metabolism
    • Moriarty-Craige, S. E.; Jones, D. P. Extracellular thiols and thiol/disulfide redox metabolism. Annu. Rev. Nutr. 24:481-509; 2004.
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 481-509
    • Moriarty-Craige, S.E.1    Jones, D.P.2
  • 49
    • 0018963749 scopus 로고
    • Transport interaction of L-cysteine and L-glutamate in human diploid fibroblasts in culture
    • Bannai, S.; Kitamura, E. Transport interaction of L-cysteine and L-glutamate in human diploid fibroblasts in culture. J. Biol. Chem. 255:2372-2376; 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 50
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • Bannai, S. Exchange of cystine and glutamate across plasma membrane of human fibroblasts. J. Biol. Chem. 261:2256-2263; 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 51
    • 84859031263 scopus 로고    scopus 로고
    • -: Cystine supplier and beyond
    • -: cystine supplier and beyond. Amino Acids 42:231-246; 2012.
    • (2012) Amino Acids , vol.42 , pp. 231-246
    • Conrad, M.1    Sato, H.2
  • 54
    • 0026605725 scopus 로고
    • Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress
    • Miura, K.; Ishii, T.; Sugita, Y.; Bannai, S. Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress. Am. J. Physiol. 262 (Cell Physiol. 31:C50-C58; 1992.
    • (1992) Am. J. Physiol. 262 Cell Physiol. , vol.31 , pp. C50-C58
    • Miura, K.1    Ishii, T.2    Sugita, Y.3    Bannai, S.4
  • 55
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control
    • Jones, D. P.; Go, Y. -M.; Anderson, C. L.; Zielger, T. R.; Kinkade Jr. J. M.; Kirlin, W. G. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J 18:1246-1248; 2004.
    • (2004) FASEB J , vol.18 , pp. 1246-1248
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Zielger, T.R.4    Kinkade, J.M.5    Kirlin, W.G.6
  • 56
  • 57
    • 34548460186 scopus 로고    scopus 로고
    • Control of extracellular cysteine/cystine redox state by HT-29 cells is independent of cellular glutathione
    • Anderson, C.; Iyer, S. S.; Ziegler, T. R.; Jones, D. P. Control of extracellular cysteine/cystine redox state by HT-29 cells is independent of cellular glutathione. Am. J. Physiol. Integr. Comp. Physiol 293:R1069-R1075; 2007.
    • (2007) Am. J. Physiol. Integr. Comp. Physiol , vol.293 , pp. R1069-R1075
    • Anderson, C.1    Iyer, S.S.2    Ziegler, T.R.3    Jones, D.P.4
  • 58
    • 84867522886 scopus 로고    scopus 로고
    • Human sulfide:Quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
    • Jackson, M. R.; Melideo, S. L.; Jorns, M. S. Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite. Biochemistry 51:6804-6815; 2012.
    • (2012) Biochemistry , vol.51 , pp. 6804-6815
    • Jackson, M.R.1    Melideo, S.L.2    Jorns, M.S.3
  • 60
  • 61
    • 0010854216 scopus 로고
    • Reaction of cystine with sodium sulfide in sodium hydroxide solution
    • Rao, G. S.; Gorin, G. Reaction of cystine with sodium sulfide in sodium hydroxide solution. J. Org. Chem. 24:749-753; 1959.
    • (1959) J. Org. Chem. , vol.24 , pp. 749-753
    • Rao, G.S.1    Gorin, G.2
  • 62
    • 84879776406 scopus 로고    scopus 로고
    • Persulfide reactivity in the detection of protein S-sulfhydration
    • Pan, J.; Carroll, K. S. Persulfide reactivity in the detection of protein S-sulfhydration. ACS Chem. Biol. 8:1110-1116; 2013.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1110-1116
    • Pan, J.1    Carroll, K.S.2
  • 64
    • 0029002386 scopus 로고
    • Perthiols as antioxidants: Radical-scavenging and prooxidative mechanisms
    • Everett, S. A.; Wardman, P. Perthiols as antioxidants: radical-scavenging and prooxidative mechanisms. Methods Enzymol. 251:55-69; 1995.
    • (1995) Methods Enzymol. , vol.251 , pp. 55-69
    • Everett, S.A.1    Wardman, P.2
  • 66
    • 33947471043 scopus 로고
    • The factors determining nucleophilic reactivities
    • Edwards, J. O.; Pearson, R. G. The factors determining nucleophilic reactivities. J. Am. Chem. Soc. 84:16-24; 1962.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 16-24
    • Edwards, J.O.1    Pearson, R.G.2
  • 68
    • 0006240737 scopus 로고
    • Microbial transsulfuration: The mechanism of an enzymatic disulfide elimination reaction
    • Flavin, M. Microbial transsulfuration: the mechanism of an enzymatic disulfide elimination reaction. J. Biol. Chem. 237:768-777; 1962.
    • (1962) J. Biol. Chem. , vol.237 , pp. 768-777
    • Flavin, M.1
  • 70
    • 0014963075 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by cyanide
    • Massey, V.; Edmondson, D. On the mechanism of inactivation of xanthine oxidase by cyanide. J. Biol. Chem. 245:6595-6598; 1970.
    • (1970) J. Biol. Chem. , vol.245 , pp. 6595-6598
    • Massey, V.1    Edmondson, D.2
  • 71
    • 0016156485 scopus 로고
    • Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase
    • Branzoli, U.; Massey, V. Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase. J. Biol. Chem. 249:4346-4349; 1974.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4346-4349
    • Branzoli, U.1    Massey, V.2
  • 73
    • 0024817618 scopus 로고
    • Sulphane sulphur in biological systems: A possible regulatory role
    • Toohey, J. I. Sulphane sulphur in biological systems: a possible regulatory role. Biochem. J. 264:625-632; 1989.
    • (1989) Biochem. J. , vol.264 , pp. 625-632
    • Toohey, J.I.1
  • 74
    • 84878793080 scopus 로고    scopus 로고
    • New fluorescent probes for sulfane sulfurs and the application in bioimaging
    • Chen, W.; Liu, C.; Peng, B.; Zhao, Y.; Pacheco, A.; Xian, M. New fluorescent probes for sulfane sulfurs and the application in bioimaging. Chem. Sci. 4:2892-2896; 2014.
    • (2014) Chem. Sci. , vol.4 , pp. 2892-2896
    • Chen, W.1    Liu, C.2    Peng, B.3    Zhao, Y.4    Pacheco, A.5    Xian, M.6
  • 75
    • 0344884373 scopus 로고
    • The chemistry of aliphatic disulfides. III. Formation of sulfides during cleavage by cyanide ion
    • Hiskey, R. G.; Carroll, F. I. The chemistry of aliphatic disulfides. III. Formation of sulfides during cleavage by cyanide ion. J. Am. Chem. Soc. 83:4647-4650; 1961.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 4647-4650
    • Hiskey, R.G.1    Carroll, F.I.2
  • 76
    • 33947486730 scopus 로고
    • Chemistry of aliphatic disulfides. VI. Effect of α-alkylation on the cyanide cleavage of unsymmetrical disulfides
    • Hiskey, R. G.; Bowers, W. H.; Harpp, D. N. Chemistry of aliphatic disulfides. VI. Effect of α-alkylation on the cyanide cleavage of unsymmetrical disulfides. J. Am. Chem. Soc. 86:2010-2014; 1964.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 2010-2014
    • Hiskey, R.G.1    Bowers, W.H.2    Harpp, D.N.3
  • 78
    • 84986435687 scopus 로고
    • Theoretical investigation of the relative stabilities of XSSX and X2SS isomers (X=F, Cl, H, and CH3)
    • Bickelhaupt, F. M.; Sola, M.; Schleyer, P. v. R. Theoretical investigation of the relative stabilities of XSSX and X2SS isomers (X=F, Cl, H, and CH3). J. Comput. Chem. 16:465-477; 1995.
    • (1995) J. Comput. Chem. , vol.16 , pp. 465-477
    • Bickelhaupt, F.M.1    Sola, M.2    Schleyer, P.V.R.3
  • 81
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe, J.; van der Donk, W. A. Protein radicals in enzyme catalysis. Chem. Rev. 98:705-762; 1998.
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 82
    • 34248581972 scopus 로고    scopus 로고
    • The oxidizing power of the glutathione thiyl radical as measured by its electrode potential at physiological pH
    • Madej, E.; Wardman, P. The oxidizing power of the glutathione thiyl radical as measured by its electrode potential at physiological pH. Arch. Biochem. Biophys. 462:94-102; 2007.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 94-102
    • Madej, E.1    Wardman, P.2
  • 83
    • 0002226173 scopus 로고
    • Thermochemistry and kinetics of sulfur-containing molecules and radicals
    • Benson, S. W. Thermochemistry and kinetics of sulfur-containing molecules and radicals. Chem. Rev. 78:23-35; 1978.
    • (1978) Chem. Rev. , vol.78 , pp. 23-35
    • Benson, S.W.1
  • 84
    • 0015231837 scopus 로고
    • The presence of S°-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c
    • Massey, V.; Williams Jr. C. H.; Palmer, G. The presence of S°-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c. Biochem. Biophys. Res. Commun. 42:730-738; 1971.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 730-738
    • Massey, V.1    Williams, C.H.2    Palmer, G.3
  • 85
    • 0020044332 scopus 로고
    • Inhibition of rat liver cytochrome P-450 by benzyl hydrodisulfide
    • Sawahata, T.; Neal, R. A. Inhibition of rat liver cytochrome P-450 by benzyl hydrodisulfide. Mol. Pharmacol. 21:464-467; 1982.
    • (1982) Mol. Pharmacol. , vol.21 , pp. 464-467
    • Sawahata, T.1    Neal, R.A.2
  • 86
    • 0000550353 scopus 로고
    • Perthiyl radicals. Trisulfide radical ions, and sulfate formation. A combined photolysis and radiolysis study on redox processes with organic di- and trisulfides
    • Everett, S. A.; Schoneich, C.; Stwart, J. H.; Asmus, K.-D. Perthiyl radicals. Trisulfide radical ions, and sulfate formation. A combined photolysis and radiolysis study on redox processes with organic di- and trisulfides. J. Phys. Chem. 96:306-314; 1992.
    • (1992) J. Phys. Chem. , vol.96 , pp. 306-314
    • Everett, S.A.1    Schoneich, C.2    Stwart, J.H.3    Asmus, K.-D.4
  • 87
    • 77954221839 scopus 로고    scopus 로고
    • Redox chemistry of biological thiols
    • Nagy, P.; Winterbourn, C. C. Redox chemistry of biological thiols. Adv. Mol. Toxicol 4:183-222; 2010.
    • (2010) Adv. Mol. Toxicol , vol.4 , pp. 183-222
    • Nagy, P.1    Winterbourn, C.C.2
  • 88
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: The role of oxidation state in protein structure and function
    • Jacob, C.; Giles, G. I.; Giles, N. M.; Sies, H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew. Chem. Int. Ed. 42:4742-4758; 2003.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 90
    • 0037403325 scopus 로고    scopus 로고
    • Comparative effects of mono-, di-, tri- and tetrasuflides derived from plants of the Allium family: Redox cycling in vitro and hemolytic activity and phase 3 enzyme induction in vivo
    • Munday, R.; Munday, J. S.; Munday, C. M. Comparative effects of mono-, di-, tri- and tetrasuflides derived from plants of the Allium family: redox cycling in vitro and hemolytic activity and phase 3 enzyme induction in vivo. Free Radic. Biol. Med. 34:1200-1211; 2003.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1200-1211
    • Munday, R.1    Munday, J.S.2    Munday, C.M.3
  • 91
    • 0017348703 scopus 로고
    • Kinetics and mechanism of oxidation of hydrogen sulfide by hydrogen peroxide in acidic solution
    • Hoffmann, M. R. Kinetics and mechanism of oxidation of hydrogen sulfide by hydrogen peroxide in acidic solution. Environ. Sci. Technol. 11:61-66; 1977.
    • (1977) Environ. Sci. Technol. , vol.11 , pp. 61-66
    • Hoffmann, M.R.1
  • 92
    • 84880277784 scopus 로고    scopus 로고
    • The biological chemistry of hydrogen peroxide
    • Winterbourn, C. C. The biological chemistry of hydrogen peroxide. Methods Enzymol. 528:4-24; 2013.
    • (2013) Methods Enzymol. , vol.528 , pp. 4-24
    • Winterbourn, C.C.1
  • 94
    • 3042670074 scopus 로고    scopus 로고
    • Oxygen, oxysterols, ouabain and ozone: A cautionary tale
    • Smith, L. L. Oxygen, oxysterols, ouabain and ozone: a cautionary tale. Free Radic. Biol. Med. 37:318-324; 2004.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 318-324
    • Smith, L.L.1
  • 96
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, α-tocopherol and ascorbate
    • Buettner, G. R. The pecking order of free radicals and antioxidants: lipid peroxidation, α-tocopherol and ascorbate. Arch. Biochem. Biophys. 300:535-543; 1993.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 97
    • 0000261014 scopus 로고
    • Redox potentials of some sulfur-containing radicals
    • Surdhar, P. S.; Armstrong, D. A. Redox potentials of some sulfur-containing radicals. J. Phys. Chem. 90:5915-5917; 1986.
    • (1986) J. Phys. Chem. , vol.90 , pp. 5915-5917
    • Surdhar, P.S.1    Armstrong, D.A.2
  • 98
    • 33845281728 scopus 로고
    • Reduction potentials and exchange reactions of thiyl radicals and disulfide anion radicals
    • Surdhar, P. S.; Armstrong, D. A. Reduction potentials and exchange reactions of thiyl radicals and disulfide anion radicals. J. Phys. Chem. 91:6532-6537; 1987.
    • (1987) J. Phys. Chem. , vol.91 , pp. 6532-6537
    • Surdhar, P.S.1    Armstrong, D.A.2
  • 100
    • 37049085085 scopus 로고
    • One- and two-electron reduction potentials of peroxyl radicals and related species
    • Merenyi, G.; Lind, J.; Engman, L. One- and two-electron reduction potentials of peroxyl radicals and related species,. J. Chem. Soc. Perkin Trans 2:2551-2553; 1994.
    • (1994) J. Chem. Soc. Perkin Trans , vol.2 , pp. 2551-2553
    • Merenyi, G.1    Lind, J.2    Engman, L.3
  • 101
    • 83655165310 scopus 로고    scopus 로고
    • 2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • 2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci. Signal 4:1-12; 2011.
    • (2011) Sci. Signal , vol.4 , pp. 1-12
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tomks, N.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.