Thiol chemistry in peroxidase catalysis and redox signaling

Antioxidants and Redox Signaling

Volumn 10, Issue 9, 2008, Pages 1549-1564

  Bindoli, Alberto ^a   Fukuto, Jon M ^b   Forman, Henry Jay ^c  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; GLUTATHIONE; HYDROGEN PEROXIDE; PEROXIDASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; SULFONIC ACID DERIVATIVE; THIOL DERIVATIVE; THIOREDOXIN;

CATALYSIS; CELL COMMUNICATION; CELL DEATH; CHEMICAL REACTION KINETICS; ENZYME MECHANISM; HUMAN; MITOCHONDRIAL MEMBRANE; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; REACTION ANALYSIS; REVIEW;

CATALYSIS; HYDROGEN PEROXIDE; MODELS, BIOLOGICAL; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PEROXIDASES; SIGNAL TRANSDUCTION; SULFHYDRYL COMPOUNDS;

EID: 46449110295     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2008.2063     Document Type: Review

References (185)

1. Adam-Vizi V, and Chinopoulos C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol Sci 27: 639-645, 2006.
2. Allison WS. Formation and reactions of sulfenic acids in proteins. Acc Chem Res 9: 293-299, 1976.
3. Andreyev AY, Kushnareva YE, and Starkov AA. Mitochondrial metabolism of reactive oxygen species. Biochemistry (Moscow) 70: 200-214, 2005.
4. Aracena-Parks P, Goonasekera SA, Gilman CP, Dirksen RT, Hidalgo C, and Hamilton SL. Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. J Biol Chem 281: 40354-40368, 2006.
5. Arnér ES and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267: 6102-6109, 2000.
6. Arnér ESJ and Holmgren A. The thioredoxin system in cancer. Semin Cancer Biol 16: 420-426, 2006.
7. Bae YS, Kang SW, Seo MS, Baines IC, Tekle E, Chock PB, and Rhee SG. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem 272: 217-221, 1997.
8. Barnard PJ and Berners-Price SJ. Targeting the mitochondrial cell death pathway with gold compounds. Coordin Chem Rev 251: 1889-1902, 2007.
9. Bedard K and Krause KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87: 245-313, 2007.
10. Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ, and Murphy MP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defense. J Biol Chem 279: 47939-47951, 2004.
11. Berggren M, Gallegos A, Gasdaska JR, Gasdaska PY, Warneke J, and Powis G. Thioredoxin and thioredoxin reductase gene expression in human tumors cell lines and the effects of serum stimulation and hypoxia. Anticancer Res 16: 3459-3466, 1996.
12. Berndt C, Lillig CH, and Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 292: H1227-H1236, 2007.
13. Biteau B, Labarre J, and Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425: 980-984, 2003.
14. Brigelius-Flohé R and Banning A. Sulforaphane and selenium, partners in adaptive response and prevention of cancer. Free Radic Res 40: 775-787, 2006.
15. Brigelius-Flohé R. Tissue-specific functions of individual glutathione peroxidases. Free Radic Biol Med 27: 951-965, 1999.
16. Brookes PS, Levonen A-L, Shiva S, Sarti P, and Darley-Usmar VM. Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species. Free Radic Biol Med 33: 755-764, 2002.
17. Brookes PS, Yoon Y, Robotham JL, Anders MW, and Sheu S-S. Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am J Physiol Cell Physiol 287: C817-C833, 2004.
18. Budanov AV, Sablina AA, Feinstein E, Koonin EV, and Chumakov PM. Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 304: 596-600, 2004.
19. Burner U, Furtmuller PG, Kettle AJ, Koppenol WH, and Obinger C. Mechanism of reaction of myeloperoxidase with nitrite. J Biol Chem 275: 20597-20601, 2000.
20. Cadenas E and Davies KJA. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29: 222-230, 2000.
21. Cadenas E. Mitochondrial free radical production and cell signaling. Mol Aspects Med 25: 17-26, 2004.
22. Carballal S, Alvarez B, Turell L, Botti H, Freeman BA, and Radi R. Sulfenic acid in human serum albumin. Amino Acids 32: 543-551, 2007.
23. Caruso F, Villa R, Rossi M, Pettinari C, Paduano F, Pennati M, Daidone MG, and Zaffaroni N. Mitochondria are primary targets in apoptosis induced by the mixed phosphine gold species chlorotriphenylphosphine-1, 3-bis(diphenylphosphino) propanegold(I) in melanoma cell lines. Biochem Pharmacol 73: 773-781, 2006.
24. Cary SPL, Winger JA, and Marletta MA. Tonic and acute nitric oxide signaling through soluble guanylate cyclase is mediated by nonheme nitric oxide, ATP, and GTP. Proc Natl Acad Sci U S A 102: 13064-13069, 2005.
25. Cassidy PB, Edes K, Nelson CC, Parsawar K, Fitzpatrick FA, and Moos PJ. Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles. Carcinogenesis 27: 2538-2549, 2006.
26. Cha MK, Kim HK, and Kim IH. Thioredoxin-linked "thiol peroxidases" from periplasmic space of Escherichia coli. J Biol Chem 270: 28635-28641, 1995.
27. Claiborne A, Miller H, Parsonage D, and Ross RP. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7: 1483-1490, 1993.
28. rd, Charrier V, and Parsonage D. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38: 15407-15416, 1999.
29. Coronnello M, Mini E, Caciagli B, Cinellu MA, Bindoli A, Gabbiani C, and Messori L. Mechanisms of cytotoxicity of selected organogold(III) compounds. J Med Chem 48: 6761-6765, 2005.
30. Cross AR and Jones OTG. Enzymic mechanisms of superoxide production. Biochim Biophys Acta 1057: 281-298, 1991.
31. Cross AR and Segal AW. The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems. Biochim Biophys Acta 1657: 1-22, 2004.
32. D'Aquino M, Bullion C, Chopra M, Devi D, Devi S, Dunster C, James G, Komuro E, Kundu S, Niki E, Raza F, Robertson F, Sharma J, and Willson R. Sulfhydryl free radical formation enzymatically, by sonolysis, by radiolysis, and thermally: vitamin A, curcumin, muconic acid, and related conjugated olefins as references. Methods Enzymol 233: 34-46, 1994.
33. Dada LA, Chandel NS, Ridge KM, Pedemonte C, Bertorello AM, and Sznajder JI. Hypoxia-induced endocytosis of Na,K-ATPase in alveolar epithelial cells is mediated by mitochondrial reactive oxygen species and PKC-ζ. J Clin Invest 111: 1057-1064, 2003.
34. Daily D, Vlamis-Gardikas A, Offen D, Mittelmann L, Melamed E, Holmgren A, and Barzilai A. Glutaredoxin protects cerebellar granulae neurons from dopamine-induced apoptosis by dual activation of the ras-phosphoinositide 3-kinase and Jun N-terminal kinase pathway. J Biol Chem 276: 21618-21626, 2001.
35. Dalle-Donne I, Milzani A, Gagliano N, Colombo R, Giustarini D, and Rossi R. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid Redox Signal 10: 445-473, 2008.
36. 2-generating system. Exp Cell Res 273: 187-196, 2002.
37. Denu JM and Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implication for redox regulation. Biochemistry 37: 5633-5642, 1998.
38. Dickinson DA and Forman HJ. Cellular glutathione and thiols metabolism. Biochem Pharmacol 64: 1019-1026, 2002.
39. Dröge W. Free radicals in the physiological control of cell function. Physiol Rev 82: 47-95, 2002.
40. Dugan LL, Sensi SL, Canzoniero LM, Handran SD, Rothman SM, Lin TS, Goldberg MP, and Choi DW. Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate. J Neurosci 15: 6377-6388, 1995.
41. Ellis HR and Poole LB. Novel application of 7-chloro-4-nitrobenzo-2-oxa- 1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry 36: 15013-15018, 1997.
42. Finkel T. Redox-dependent signal transduction. FEBS LETT 476: 52-54, 2000.
43. Flohé L, Loschen G, Günzler WA, and Eichele E. Glutathione peroxidase, V: the kinetic mechanism. Hoppe-Seyler's Z Physiol Chem 353: 987-999, 1972.
44. Ford E, Hughes MN, and Wardman P. Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine and uric acid at physiological pH. Free Radic Biol Med 32: 1314-1323, 2002.
45. Forman HJ and Kennedy JA. Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem Biophys Res Commun 60: 1044-1050, 1974.
46. Forman HJ and Torres M. Signaling by respiratory burst in macrophages. IUBMB Life 51: 365-371, 2001.
47. Forman HJ, Fukuto JM, Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287: C246-C256, 2004.
48. 2 in studies of signal transduction. Free Radic Biol Med 42: 926-932, 2007.
49. Friedman M. The chemistry and biochemistry of the sulfhydryl group in amino acids, peptides and proteins. Oxford: Pergamon Press, 1973.
50. Gamblin DP, Garnier P, Ward SJ, Oldham NJ, Fairbanks AJ, and Davies BG. Glycosyl phenylthiosulfonates (Glyco-PTS): novel reagents for glycoprotein synthesis. Org Biomol Chem 1: 3642-3644, 2003.
51. Gasdaska PY, Oblong JE, Cotgreave IA, and Powis G. The predicted aminoacid sequence of human thioredoxin is identical to that of the autocrine growth factor human T-cell derived factor (ADF): thioredoxin mRNA is elevated in some human tumors. Biochim Biophys Acta 1218: 292-296, 1994.
52. Geiszt M and Leto TL. The Nox family of NAD(P)H oxidases: host defense and beyond. J Biol Chem 279: 51715-51718, 2004.
53. Giorgio M, Trinei M, Migliaccio E, and Pelicci PG. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8: 722-728, 2007.
54. Gladyshev VN, Jeang KT, and Stadtman TC. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci U S A 93: 6146-6151, 1996.
55. Gow AJ, Buerk DG, and Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem 272: 2841-2845, 1997.
56. Grogan TM, Fenoglio-Prieser C, Zeheb R, Bellamy W, Frutiger Y, Vela E, Stemmerman G, Macdonald J, Richter L, Gallegos A, and Powis G. Thioredoxin a putative oncogene product is overexpressed in gastric carcinoma and associated with increased proliferation and increased cell survival. Hum Pathol 31: 475-481, 2000.
57. Gromer S, Arscott LD, Williams CHJr, Schirmer RH, and Becker K. Human placenta thioredoxin reductase: isolation of the selenoenzyme, steady-state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273: 20096-20101, 1998.
58. Gromer S, Urig S, and Becker K. The thioredoxin system: from science to clinic. Med Res Rev 24: 40-89, 2004.
59. Gunter TE, Yule DI, Gunter KK, Eliseev RA, and Salter JD. Calcium and mitochondria. FEBS LETT 567: 96-102, 2004.
60. Hess DT, Matsumoto A, Kim SO, Marshall HE, and Stamler JS. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol 6: 150-166, 2005.
61. Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, and Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci U S A 94: 3633-3638, 1997.
62. Hofmann B, Hecht HJ, and Flohé L. Peroxiredoxins. Biol Chem 383: 347-364, 2002.
63. Hogg DR. The chemistry of sulphenic acids and esters. In: Patai S ed. The chemistry of sulphenic acids and their derivatives. New York: John Wiley and Sons, 1990:361-402.
64. Holmgren A and Luthman M. Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry 17: 4071-4077, 1978.
65. Holmgren A, Johansson C, Berndt C, Lönn ME, Hudemann C, and Lillig CH. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans 33: 1375-1377, 2005.
66. Holmgren A. Thioredoxin: structure and functions. Trends Biochem Sci 6: 26-28, 1981.
67. Iles KE, Dickinson DA, Watanabe N, Iwamoto T, and Forman HJ. AP-1 activation through endogenous H2O2 generation by alveolar macrophages. Free Radic Biol Med 32: 1302-1313, 2002.
68. Isogai Y, Iizuka T, and Shiro Y. The mechanism of electron donation to molecular oxygen by phagocytic cytochrome b558. J Biol Chem 270: 7853-7857, 1995.
69. Jeong W, Park SJ, Chang T-S, Lee D-Y, and Rhee SG. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J Biol Chem 281: 14400-14407, 2006.
70. Jocelyn PC. Biochemistry of the SH group. London: Academic Press, 1972.
71. Johansson C, Lillig CH, and Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity acccepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279: 7537-7543, 2004.
72. Kabe Y, Ando K, Hirao S, Yoshida M, and Handa H. Redox regulation of NF-kB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 7: 395-403, 2005.
73. Kang SW, Baines IC, and Rhee SG. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem 273: 6303-6311, 1998.
74. Kice JL and Cleveland JP. Nucleophilic substitution reactions involving sulfenic acids and sulfenyl derivatives: nucleophile-and acid-catalyzed oxygen-18 exchange of phenylbenzenethiolsulfinate. J Am Chem Soc 95: 104-109, 1973.
75. Kice JL. Mechanisms and reactivity in reactions of organic oxyacids of sulfur and their anhydrides. Adv Phys Org Chem 17: 65-181, 1980.
76. Kim KH, Rodriguez AM, Carrico PM, and Melendez JA. Potential mechanisms for the inhibition of tumor cell growth by manganese superoxide dismutase. Antioxid Redox Signal 3: 361-373, 2001.
77. Kim YC, Yamaguchi Y, Kondo N, Masutani H, and Yodoi J. Thioredoxin-dependent redox regulation of the antioxidant responsive element (ARE) in electrophile response. Oncogene 22: 1860-1865, 2003.
78. Kolberg M, Strand KR, Graff P, and Andersson KK. Structure, function, and mechanism of ribonucleotide reductases. Biochim Biophys Acta 1699: 1-34, 2004.
79. Kroemer G, Galluzzi L, and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87: 99-163, 2007.
80. Lambeth JD, Kawahara T, and Diebold B. Regulation of Nox and Duox enzymatic activity and expression. Free Radic Biol Med 43: 319-331, 2007.
81. Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4: 181-189, 2004.
82. Lambeth JD. Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radic Biol Med. 43: 332-347, 2007.
83. Laurent TC, Moore EC, and Reichard P. Enzymatic synthesis of deoxyribonucleotides, IV: isolation and characterization of thioredoxin, the hydrogen donor from Escherichia Coli B. J Biol Chem 239: 3436-3444, 1964.
84. Lee S-R, Kim J-R, Kwon K-S, Yoon HW, Levine RL, Ginsburg A, and Rhee SG. Molecular cloning and characterization of a mitochondrial selenocysteine- containing thioredoxin reductase from rat liver. J Biol Chem 274: 4722-4734, 1999.
85. Levine RL, Moskovitz J, and Stadtman ER. Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 50: 301-307, 2000.
86. Li N, Ragheb K, Lawler G, Sturgis J, Rajwa B, Melendez JA, and Robinson JP. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive species production. J Biol Chem 278: 8516-1525, 2003.
87. Lillig CH and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 9: 25-47, 2007.
88. Lillig CH, Lönn ME, Enoksson M, Fernandes AP, and Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells towards doxorubicin and phenylarsine oxide. Proc Natl Acad Sci U S A 101: 13227-13232, 2004.
89. Lim MD, Lorkovic IM, and Ford PC. NO and NOx interactions with group 8 metalloporphyrins. J Inorg Biochem 99: 151-165, 2005.
90. Little C and O'Brien PJ. Mechanism of peroxide-inactivation of the sulphydryl enzyme glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 10: 533-538, 1969.
91. Liu H, Zhang H, Iles KE, Rinna A, Merrill G, Yodoi J, Torres M, and Forman HJ. The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages. Free Radic Res 40: 865-874, 2006.
92. Liu JJ, Galettis P, Farr A, Maharaj L, Samarasinha H, McGechan AC, Baguley BC, Bowen RJ, Berners-Price SJ, and McKeage MJ. In vitro antitumour and hepatotoxicity profiles of Au(I) and Ag(I) bidentate pyridyl phosphine complexes and relationships to cellular uptake. J Inorg Biochem 102: 303-310, 2008.
93. rd ed. New York: Academic Press, 1977:239-402.
94. 2 within the hydrophobic interior of biological membranes. Proc Natl Acad Sci U S A 95: 2175-2179, 1998.
95. Loschen G, Azzi A, Richter C, and Flohé L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS LETT 42: 68-72, 1974.
96. 2 production in pigeon heart mitochondria. FEBS LETT 18: 261-264, 1971.
97. Lu J, Chew E-H, and Holmgren A. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc Natl Acad Sci U S A 104: 12288-12293, 2007.
98. Mahadev K, Wu X, Zilbering A, Zhu L, Lawrence JTR, and Goldstein BJ. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of distal insulin signaling cascade in 3T3-L1 adipocytes. J Biol Chem 276: 48662-48669, 2001.
99. Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, and Tanaka H. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J Biol Chem 274: 3182-3188, 1999.
100. Martinez-Ruiz A and Lamas S. S-nitrosylation: a potential new paradigm in signal transduction. Cardiovasc Res 62: 43-52, 2004.
101. Marzano C, Gandin V, Folda A, Scutari G, Bindoli A, and Rigobello MP. Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells. Free Radic Biol Med 42: 872-881, 2007.
102. Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, and Hay RT. Thioredoxin regulates the DNA binding activity of NFkB by reducing a disulfide bond involving cysteine 62. Nucleic Acid Res 20: 3821-3830, 1992.
103. Meier B, Radeke HH, Selle S, Younes M, Sies H, Resch K, and Habermehl GG. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha. Biochem J 263: 539-545, 1989.
104. Meyer EB and Wells WW. Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin. Free Radic Biol Med 26: 770-776, 1999.
105. Moran LK, Gutteridge JMC, and Quinlan GJ. Thiols in cellular redox signaling and control. Curr Med Chem 8: 763-772, 2001.
106. Morel Y and Barouki R. Repression of gene expression by oxidative stress. Biochem J 342: 481-496, 1999.
107. Mustacich D and Powis G. Thioredoxin reductase. Biochem J 346: 1-8, 2000.
108. Nakamura H, Bai J, Nishinaka Y, Ueda S, Sasada T, Ohshio G, Imamura M, Takabayashi A, Yamaoka Y, and Yodoi J. Expression of thioredoxin and glutaredoxin, redox regulating proteins, in pancreatic cancer. Cancer Detect Prev 24: 53-60, 2000.
109. Nakamura H, Masutani H, Tagaya Y, Yamauchi A, Inamoto T, Nanbu Y, Fuji S, Ozawa K, and Yodoi J. Expression and growth-promoting effect of adult T-cell leukemia-derived factor: a human thioredoxin homologue in hepatocellular carcinoma. Cancer 69: 2091-2097, 1992.
110. Nemoto S, Takeda K, Yu Z-X, Ferrans VJ, and Finkel T. Role for mitochondrial oxidants as regulators of cellular metabolism. Mol Cell Biol 20: 7311-7318, 2000.
111. O'Donnell VB, and Azzi A. High rates of superoxide generation by cultured human fibroblasts: involvement of a lipid-metabolizing enzyme. Biochem J 318: 805-812, 1996.
112. Orrenius S, Gogvadze V, and Zhivotovsky B. Mitochondrial oxidative stress: implications for cell death. Annu Rev Pharmacol Toxicol 47: 143-183, 2007.
113. Pani G, Bedogni B, Colavitti R, Anzevino R, Borrello S, and Galeotti T. Cell compartmentalization in redox signaling. IUBMB Life 52: 7-16, 2001.
114. Paolicchi A, Dominici S, Pieri L, Maellaro E, and Pompella A. Glutathione catabolism as a signaling mechanism. Biochem Pharmacol 64: 1027-1035, 2002.
115. Park SJ and Kim I-S. The role of p38 MAPK activation in auranofin-induced apoptosis of human promyelocytic leukaemia HL-60 cells. Br J Pharmacol 146: 506-513, 2005.
116. Pascal I and Tarbell DS. The kinetics of the oxidation of a mercaptan to the corresponding disulfide by aqueous hydrogen peroxide. J Am Chem Soc 79: 6015-6020, 1957.
117. Patwari P and Lee RT. Thioredoxins, mitochondria and hypertension. Am J Pathol 170: 805-808, 2007.
118. Pennington JD, Wang TJC, Nguyen P, Sun L, Bisht K, Smart DD, and Gius D. Redox-sensitive signaling factors as a novel molecular targets for cancer therapy. Drug Resist Updat 8: 322-330, 2005.
119. Poole LB and Ellis HR. Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. Methods Enzymol 348: 122-136, 2002.
120. Poole LB, Karplus PA, and Claiborne A. Protein sulfenic acids in redox signaling. Annu Rev Pharmacol Toxicol 44: 325-347, 2004.
121. Powis G and Kirkpatrick DL. Thioredoxin signaling as a target for cancer therapy. Curr Opin Pharmacol 7: 392-397, 2007.
122. Powis G, Briehl M, and Oblong J. Redox signalling and the control of cell growth and death. Pharmacol Ther 68: 149-173, 1995.
123. Quillet-Mary A, Jaffrézou JP, Mansat V, Bordier C, Naval J, and Laurent G. Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J Biol Chem 272: 21388-21395, 1997.
124. Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, and Lunardi J. Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site. J Biol Chem 277: 19396-19401, 2002.
125. Rackham O, Nichols SJ, Leedman PJ, Berners-Price SJ, and Filipovska A. A gold(I) phosphine complex selectively induces apoptosis in breast cancer cells: implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol 74: 992-1002, 2007.
126. Raha S and Robinson BH. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 25: 502-508, 2000.
127. Ramachandran A, Moellering D, Go YM, Shiva S, Levonen AL, Jo H, Patel RP, Parthasarathy S, and Darley-Usmar VM. Activation of c-Jun N-terminal kinase and apoptosis in endothelial cells mediated by endogenous generation of hydrogen peroxide. Biol Chem 383: 693-701, 2002.
128. 2-dependent ERK1/2 activation. J Biol Chem 276: 14264-14271, 2001.
129. Rhee SG, Bae YS, Lee S-R, and Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci STKE 2000(53)PE1, 2000.
130. Rhee SG, Chae HY, and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 38: 1543-1552, 2005.
131. Rhee SG, Chang TS, Bae YS, Lee SR, Kang SW. Cellular regulation by hydrogen peroxide. J Am Soc Nephrol 14: S211-S215, 2003.
132. Rhee SG. H2O2, a necessary evil for cell signaling. Science 312: 1882-1883, 2006.
133. Rigobello MP, Callegaro MP, Barzon E, Benetti M, and Bindoli A. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radic Biol Med 24: 370-376, 1998.
134. Rigobello MP, Folda A, Scutari G, and Bindoli A. The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria. Arch Biochem Biophys 441: 112-122, 2005.
135. Rigobello MP, Messori L, Marcon G, Cinellu MA, Bragadin M, Folda A, Scutari G, and Bindoli A. Gold complexes inhibit mitochondrial thioredoxin reductase: consequences on mitochondrial functions. J Inorg Biochem 98: 1634-1641, 2004.
136. Rigobello MP, Scutari G, Boscolo R, and Bindoli A. Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative. Br J Pharmacol 136: 1162-1168, 2002.
137. Rigobello MP, Scutari G, Folda A, and Bindoli A. Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c. Biochem Pharmacol 67: 689-696, 2004.
138. Roy B and Garthwaite J. Nitric oxide activation of guanylyl cyclase in cells revisited. Proc Natl Acad Sci U S A 103: 12185-12190, 2006.
139. Saggioro D, Rigobello MP, Paloschi L, Folda A, Moggach SA, Parsons S, Ronconi L, Fregona D, and Bindoli A. Gold(III)-dithiocarbamato complexes induce cancer cell death triggered by thioredoxin redox system inhibition and activation of ERK pathway. Chem Biol 14: 1128-1139, 2007.
140. Saitoh M, Nishitoh H, Fujii M, Takeda K, Tobiume K, Sawada Y, Kawabata M, Miyazono K, and Ichijo H. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17: 2596-2606, 1998.
141. Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423: 769-773, 2003.
142. Sauer H, Wartenberg M, and Hescheler J. Reactive oxygen species as intracellular messengers during cell growth and differentiation. Cell Physiol Biochem 11: 173-186, 2001.
143. Savige WE and Maclaren JA. Oxidation of disulfides, with special reference to cystine. In: Kharasch N, ed. The chemistry of organic sulfur compounds. Oxford: Pergamon Press, 1966, vol 2:367-402.
144. Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/ glutathione couple. Free Radic Biol Med 30: 1191-1212, 2001.
145. Schulze-Osthoff K, Beyaert R, Vandevoorde V, Haegeman G, and Fiers W. Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects on TNF. EMBO J 12: 3095-3104, 1993.
146. Schweizer U, Chiu J, and Köhrle J. Peroxide and peroxide-degrading enzymes in the thyroid. Antioxid Redox Signal 2008, this issue.
147. Smith DJ Maggio ET, and Kenyon GL. Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes. Biochemistry 14: 766-771, 1975.
148. Stadtman TC. Selenocysteine. Annu Rev Biochem 65: 83-100, 1996.
149. Steffen Y, Gruber C, Schewe T, and Sies H. Mono-O-methylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase. Arch Biochem Biophys 469: 209-219, 2008.
150. Steffen Y, Schewe T, and Sies H. (-)-Epicatechin elevates nitric oxide in endothelial cells via inhibition of NADPH oxidase. Biochem Biophys Res Comm 359: 828-833, 2007.
151. Stone JR, and Yang S. Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 8: 243-270, 2006.
152. Stone JR. An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys 422: 119-124, 2004.
153. Stubbe J and van der Donk WA. Protein radicals in enzyme catalysis. Chem Rev 98: 705-762, 1998.
154. Sun Q-A, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, and Gladyshev VN. Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem 274: 24522-24530, 1999.
155. 2 for platelet-derived growth factor signal transduction. Science 270: 296-299, 1995.
156. Suzuki YJ, Forman HJ, and Sevanian A. Oxidants as stimulators of signal transduction. Free Radic Biol Med 22: 269-285, 1997.
157. Taylor ER, Hurrell F, Shannon RJ, Lin T-K, Hirst J, and Murphy MP. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J Biol Chem 278: 19603-19610, 2003.
158. Torchinskii YM. Sulfhydryl and disulfide groups of proteins. New York: Consultants Bureau. (Plenum Publishing Corporation), 1974.
159. Tosatto SCE, Bosello V, Fogolari F, Mauri P, Roveri A, Toppo S, Flohé L, Ursini F, and Maiorino M. The catalytic site of glutathione peroxidases. Antioxid Redox Signal 2008, this issue.
160. Trotter EW and Grant CM. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep 4: 184-188, 2003.
161. Ueno M, Masutani H, Arai RJ, Yamauchi A, Hirota K, Sakai T, Inamoto T, Yamaoka Y, Yodoj J, and Nikaido T. Thioredoxin-dependent redox regulation of p53-mediated p21 activation. J Biol Chem 274: 35809-35815, 1999.
162. Urig S and Becker K. On the potential of thioredoxin reductase inhibitors for cancer therapy. Sem Cancer Biol 16: 452-465, 2006.
163. van der Vliet A. NADPH oxidases in lung biology and pathology: host defense enzymes, and more. Free Radic Biol Med (2008), doi:10.1016/j.freeradbiomed.2007.11.016.
164. van Montfort RL, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003.
165. Wakabayashi N, Dinkova-Kostova AT, Holtzclaw WD, Kang MI, Kobayashi A, Yamamoto M, Kensler TW, and Talaly P. Protection against electrophiles and oxidant stress by induction of phase 2 response: fate of cysteines of the Keap1 sensor modified by inducers. Proc Natl Acad Sc U S A 101: 2040-2045, 2004.
166. Walker LJ, Robson CN, Black E, Gillespie D, and Hickson ID. Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding. Mol Cell Biol 9: 5370-5376, 1993.
167. Wardman P. Evaluation of the "radical sink" hypothesis from a chemical-kinetic viewpoint. J Radioanal Nucl Chem 232: 23-27, 1998.
168. Weidner JP and Block SS. Mixed thiolsulfonates and sulfonamides from polyfunctional mercaptans using trifluoromethyl thiosulfonates. J Med Chem 15: 564-567, 1972.
169. Welsh SJ, Bellamy WT, Briehl MM, and Powis G. The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis. Cancer Res 62: 5089-5095, 2002.
170. Werner E and Werb Z. Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases. J Cell Biol 158: 357-368, 2002.
171. Willett WS and Copley SD. Identification and localization of a stable sulfenic acid in peroxide-treated tetrachlorohydroquinone dehalogenase using electrospray mass spectrometry. Chem Biol 3: 851-857, 1996.
172. Winterbourn CC and Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 27: 322-328, 1999.
173. Woo HA, Chae HZ, Hwang SC, Yang K-S, Kim K, and Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300: 653-656, 2003.
174. Wood ZA, Poole LB, and Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653, 2003.
175. Wynn R and Richards FM. Chemical modifications of protein thiols: formation of mixed disulfides. Method Enzymol 251: 351-356, 1995.
176. Xanthoudakis S and Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J 11: 653-655, 1992.
177. Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, and Rhee SG. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 277: 38029-38036, 2002.
178. Yang S, Misner BJ, Chiu RJ, and Meyskens FL Jr. Redox effector factor-1, combined with reactive oxygen species, plays an important role in the transformation of JB6 cells. Carcinogenesis 28: 2382-2390, 2007.
179. Yoo M-H, Xu X-M, Carlson BA, Gladyshev VN, and Hatfield DL. Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells. J Biol Chem 281: 13005-13008, 2006.
180. Zhang DD and Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 23: 8137-8151, 2003.
181. Zhang DX and Gutterman DD. Mitochondrial reactive oxygen species-mediated signaling in endothelial cells. Am J Physiol Heart Circ Physiol 292: H2023-H2031, 2007.
182. Zhang R, Al-Lamki R, Bai L, Streb JW, Miano JM, Bradley J, and Min W. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 94: 1483-1491, 2004.
183. Zhao Y-L and Houk KN. Thionitroxides, RSNHO: the structure of the SNO moiety in "S-nitrosohemoglobin: a possible NO reservoir and transporter. J Am Chem Soc 128: 1422-1423, 2006.
184. Zhong L, Arnér ES, Ljung J, Aslund F, and Holmgren A. Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J Biol Chem 273: 8581-8591, 1998.
185. 2+. J Biol Chem 279: 4166-4174, 2004.