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Volumn 22, Issue 2, 2013, Pages 131-137

Oxygen: How do we stand it?

Author keywords

Free radical; Hydrogen peroxide; Nitric oxide; Oxidative stress; Reactive oxygen species; Singlet oxygen; Superoxide; Superoxide assay; Superoxide dismutase

Indexed keywords

ANTIOXIDANT; CATALASE; ENZYME; OXYGEN; PEROXIDASE; POLYACRYLAMIDE GEL; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; NITRIC OXIDE;

EID: 84873660953     PISSN: 10117571     EISSN: 14230151     Source Type: Journal    
DOI: 10.1159/000339212     Document Type: Review
Times cited : (71)

References (52)
  • 1
    • 0020804138 scopus 로고
    • Preparation and stabilization of aqueous/ethanolic superoxide solutions
    • Bielski BHJ, Arudi RL: Preparation and stabilization of aqueous/ethanolic superoxide solutions. Anal Biochem 1983; 133: 170-178
    • (1983) Anal Biochem , vol.133 , pp. 170-178
    • Bielski, B.H.J..1    Arudi, R.L.2
  • 2
    • 0030993117 scopus 로고    scopus 로고
    • Superoxide-driven aconitase FE-S center cycling
    • Gardner PR: Superoxide-driven aconitase FE-S center cycling. Biosci Rep 1997; 17: 33-42
    • (1997) Biosci Rep , vol.17 , pp. 33-42
    • Gardner, P.R.1
  • 3
    • 0029868750 scopus 로고    scopus 로고
    • The role of iron-sulfur clusters in in vivo hydroxyl radical production
    • Liochev SI: The role of iron-sulfur clusters in in vivo hydroxyl radical production. Free Radic Res 1996; 25: 369-384
    • (1996) Free Radic Res , vol.25 , pp. 369-384
    • Liochev, S.I.1
  • 4
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA: Pathways of oxidative damage. Annu Rev Microbiol 2003; 57: 395-418
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 5
    • 0025800392 scopus 로고
    • Assay of metabolic superoxide production in Escherichia coli
    • Imlay JA, Fridovich I: Assay of metabolic superoxide production in Escherichia coli . J Biol Chem 1991; 266: 6957-6965
    • (1991) J Biol Chem , vol.266 , pp. 6957-6965
    • Imlay, J.A.1    Fridovich, I.2
  • 6
    • 84864600170 scopus 로고    scopus 로고
    • Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria
    • DOI: 10.1016/j.abb.2012.02.007
    • Chiang SM, Schellhorn HE: Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria. Arch Biochem Biophys DOI: 10.1016/j.abb.2012.02.007
    • Arch Biochem Biophys
    • Chiang, S.M.1    Schellhorn, H.E.2
  • 7
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I: Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 244: 6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 8
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson EK, Fridovich I: The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975; 14: 5294-5299
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 9
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis
    • Klug D, Rabani J, Fridovich I: A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J Biol Chem 1972; 247: 4839-4842
    • (1972) J Biol Chem , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovich, I.3
  • 10
    • 0031569871 scopus 로고    scopus 로고
    • The copperand zinc-containing superoxide dismutase from Escherichia coli : Molecular weight and stability
    • Benov L, Sage H, Fridovich I: The copperand zinc-containing superoxide dismutase from Escherichia coli : Molecular weight and stability. Arch Biochem Biophys 1997; 340: 305-310
    • (1997) Arch Biochem Biophys , vol.340 , pp. 305-310
    • Benov, L.1    Sage, H.2    Fridovich, I.3
  • 11
    • 0028841185 scopus 로고
    • Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli
    • Battistoni A, Rotilio G: Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli . FEBS Lett 1995; 374: 199-202
    • (1995) FEBS Lett , vol.374 , pp. 199-202
    • Battistoni, A.1    Rotilio, G.2
  • 12
    • 0036121283 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase
    • Marklund SL: Extracellular superoxide dismutase. Methods Enzymol 2002; 349: 74-80
    • (2002) Methods Enzymol , vol.349 , pp. 74-80
    • Marklund, S.L.1
  • 13
    • 0015832348 scopus 로고
    • Superoxide dismutases of Escherichia coli : intracellular localization and functions
    • Gregory EM, Yost FJ Jr, Fridovich I: Superoxide dismutases of Escherichia coli : intracellular localization and functions. J Bacteriol 1973; 115: 987-991
    • (1973) J Bacteriol , vol.115 , pp. 987-991
    • Gregory, E.M.1    Yost Jr., F.J.2    Fridovich, I.3
  • 14
    • 0014962945 scopus 로고
    • Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme
    • Keele BB Jr, McCord JM, Fridovich I: Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme. J Biol Chem 1970; 245: 6176-6181
    • (1970) J Biol Chem , vol.245 , pp. 6176-6181
    • Keele Jr., B.B.1    McCord, J.M.2    Fridovich, I.3
  • 15
    • 0015903497 scopus 로고
    • An iron containing superoxide dismutase from Escherichia coli
    • Yost FJ Jr, Fridovich I: An iron containing superoxide dismutase from Escherichia coli . J Biol Chem 1973; 248: 4905-4908
    • (1973) J Biol Chem , vol.248 , pp. 4905-4908
    • Yost Jr., F.J.1    Fridovich, I.2
  • 16
    • 0026794023 scopus 로고
    • Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli
    • Privalle CT, Fridovich I: Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli . J Biol Chem 1992; 267: 9140-9145
    • (1992) J Biol Chem , vol.267 , pp. 9140-9145
    • Privalle, C.T.1    Fridovich, I.2
  • 17
    • 0028862883 scopus 로고
    • Metal uptake of recombinant cambialistic superoxide dismutase from Propionibacterium shermanii is affected by growth conditions of host Escherichia coli cells
    • Gabbianelli R, Battistoni A, Polizio F, Carrì MT, De Martino A, Meier B, Desideri A, Rotilio G: Metal uptake of recombinant cambialistic superoxide dismutase from Propionibacterium shermanii is affected by growth conditions of host Escherichia coli cells. Biochem Biophys Res Commun 1995; 216: 841-847
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 841-847
    • Gabbianelli, R.1    Battistoni, A.2    Polizio, F.3    Carrì, M.T.4    De Martino, A.5    Meier, B.6    Desideri, A.7    Rotilio, G.8
  • 18
    • 0024308039 scopus 로고
    • Superoxide dismutases. An adaptation to a paramagnetic gas
    • Fridovich I: Superoxide dismutases. An adaptation to a paramagnetic gas. J Biol Chem 1989; 264: 7761-7764
    • (1989) J Biol Chem , vol.264 , pp. 7761-7764
    • Fridovich, I.1
  • 19
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA: Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 2008; 77: 755-776
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 20
    • 0029849183 scopus 로고    scopus 로고
    • Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
    • Kim EJ, Kim HP, Hah YC, Roe JH: Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor . Eur J Biochem 1996; 241: 178-185
    • (1996) Eur J Biochem , vol.241 , pp. 178-185
    • Kim, E.J.1    Kim, H.P.2    Hah, Y.C.3    Roe, J.H.4
  • 22
    • 0035892642 scopus 로고    scopus 로고
    • Assay of superoxide dismutase: Cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide
    • Okado-Matsumoto A, Fridovich I: Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide. Anal Biochem 2001; 298: 337-342
    • (2001) Anal Biochem , vol.298 , pp. 337-342
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 24
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase
    • Misra HP, Fridovich I: The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 1972; 247: 3170-3175
    • (1972) J Biol Chem , vol.247 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, I.2
  • 25
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S, Marklund G: Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974; 47: 469-474
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 26
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I: Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 1971; 44: 276-287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 27
    • 0028965665 scopus 로고
    • Superoxide from glucose oxidase or from nitroblue tetrazolium
    • Liochev SI, Fridovich I: Superoxide from glucose oxidase or from nitroblue tetrazolium. Arch Biochem Biophys 1995; 318: 408-410
    • (1995) Arch Biochem Biophys , vol.318 , pp. 408-410
    • Liochev, S.I.1    Fridovich, I.2
  • 28
    • 0030722559 scopus 로고    scopus 로고
    • The tetrazolium dyes MTS and XTT provide new quantitative assays for superoxide and superoxide dismutase
    • Sutherland MW, Learmonth BA: The tetrazolium dyes MTS and XTT provide new quantitative assays for superoxide and superoxide dismutase. Free Radic Res 1997; 27: 283-289
    • (1997) Free Radic Res , vol.27 , pp. 283-289
    • Sutherland, M.W.1    Learmonth, B.A.2
  • 29
    • 0031554917 scopus 로고    scopus 로고
    • Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3 -{1-[(phenylamino)-carbonyl]-3,4-tetrazolium}-bis(4-methoxy-6-nitro) benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase
    • Ukeda H, Maeda S, Ishii T, Sawamura M: Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3 -{1-[(phenylamino)-carbonyl]-3, 4-tetrazolium}-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase. Anal Biochem 1997; 251: 206-209
    • (1997) Anal Biochem , vol.251 , pp. 206-209
    • Ukeda, H.1    Maeda, S.2    Ishii, T.3    Sawamura, M.4
  • 30
    • 0037112670 scopus 로고    scopus 로고
    • Is reduction of the sulfonated tetrazolium 2,3-bis(2-methoxy-4-nitro-5- sulfophenyl)-2-tetrazolium 5-carboxanilide a reliable measure of intracellular superoxide production?
    • Benov L, Fridovich I: Is reduction of the sulfonated tetrazolium 2,3-bis(2-methoxy-4-nitro-5-sulfophenyl)-2-tetrazolium 5-carboxanilide a reliable measure of intracellular superoxide production? Anal Biochem 2002; 310: 186-190
    • (2002) Anal Biochem , vol.310 , pp. 186-190
    • Benov, L.1    Fridovich, I.2
  • 31
    • 38149142769 scopus 로고    scopus 로고
    • Detection of 2-hydroxyethidium in cellular systems: A unique marker product of superoxide and hydroethidine
    • Zielonka J, Vasquez-Vivar J, Kalyanaraman B: Detection of 2-hydroxyethidium in cellular systems: a unique marker product of superoxide and hydroethidine. Nat Protoc 2008; 3: 8-21
    • (2008) Nat Protoc , vol.3 , pp. 8-21
    • Zielonka, J.1    Vasquez-Vivar, J.2    Kalyanaraman, B.3
  • 32
    • 0015596284 scopus 로고
    • Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior BM, Kipnes RS, Curnutte JT: Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 1973; 52: 741-744
    • (1973) J Clin Invest , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 33
    • 0242460542 scopus 로고    scopus 로고
    • Oxidative killing of microbes by neutrophils
    • Roos D, Van Bruggen R, Meischl C: Oxidative killing of microbes by neutrophils. Microbes Infect 2003; 5: 1307-1315
    • (2003) Microbes Infect , vol.5 , pp. 1307-1315
    • Roos, D.1    Van Bruggen, R.2    Meischl, C.3
  • 34
    • 84856247093 scopus 로고    scopus 로고
    • Relationship between oxidative stress and inflammatory cytokines in diabetic nephropathy
    • Elmarakby AA, Sullivan JC: Relationship between oxidative stress and inflammatory cytokines in diabetic nephropathy. Cardiovasc Ther 2012; 30: 49-59
    • (2012) Cardiovasc Ther , vol.30 , pp. 49-59
    • Elmarakby, A.A.1    Sullivan, J.C.2
  • 35
    • 84855892790 scopus 로고    scopus 로고
    • Oxidant stress, mitochondria, and cell death mechanisms in drug-induced liver injury: Lessons learned from acetaminophen hepatotoxicity
    • Jaeschke H, McGill MR, Ramachandran A: Oxidant stress, mitochondria, and cell death mechanisms in drug-induced liver injury: lessons learned from acetaminophen hepatotoxicity. Drug Metab Rev 2012; 44: 88-106
    • (2012) Drug Metab Rev , vol.44 , pp. 88-106
    • Jaeschke, H.1    McGill, M.R.2    Ramachandran, A.3
  • 36
    • 84856293321 scopus 로고    scopus 로고
    • The redox stress hypothesis of aging
    • Sohal RS, Orr WC: The redox stress hypothesis of aging. Free Radic Biol Med 2012; 52: 539-555
    • (2012) Free Radic Biol Med , vol.52 , pp. 539-555
    • Sohal, R.S.1    Orr, W.C.2
  • 37
    • 82955248175 scopus 로고    scopus 로고
    • Role of oxidative stress in disease progression in stage B, a precursor of heart failure
    • Bhimaraj A, Tang WHW: Role of oxidative stress in disease progression in stage B, a precursor of heart failure. Heart Fail Clin 2012; 8: 101-111
    • (2012) Heart Fail Clin , vol.8 , pp. 101-111
    • Bhimaraj, A.1    Tang, W.H.W.2
  • 38
    • 79956191022 scopus 로고    scopus 로고
    • Role of oxidative stress and DNA damage in human carcinogenesis
    • Kryston TB, Georgiev AB, Pissis P, Georgakilas AG: Role of oxidative stress and DNA damage in human carcinogenesis. Mutat Res 2011; 711: 193-201
    • (2011) Mutat Res , vol.711 , pp. 193-201
    • Kryston, T.B.1    Georgiev, A.B.2    Pissis, P.3    Georgakilas, A.G.4
  • 39
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng M, Storz G: Redox sensing by prokaryotic transcription factors. Biochem Pharmacol 2000; 59: 1-6
    • (2000) Biochem Pharmacol , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 40
    • 0026784249 scopus 로고
    • Two-stage control of an oxidative stress regulon: The Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene
    • Nunoshiba T, Hidalgo E, Cuevas CFA, Demple B: Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene. J Bacteriol 1992; 174: 6054-6060
    • (1992) J Bacteriol , vol.174 , pp. 6054-6060
    • Nunoshiba, T.1    Hidalgo, E.2    Cuevas, C.F.A.3    Demple, B.4
  • 41
    • 0029770061 scopus 로고    scopus 로고
    • Two-stage gene regulation of the superoxide stress response soxRS system in Escherichia coli
    • Nunoshiba T: Two-stage gene regulation of the superoxide stress response soxRS system in Escherichia coli . Crit Rev Eukaryot Gene Expr 1996; 6: 377-389
    • (1996) Crit Rev Eukaryot Gene Expr , vol.6 , pp. 377-389
    • Nunoshiba, T.1
  • 42
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner PR, Fridovich I: Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 1991; 266: 19328-19333
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 43
    • 0027258954 scopus 로고
    • Modulation of the fumarases of Escherichia coli in response to oxidative stress
    • Liochev SI, Fridovich I: Modulation of the fumarases of Escherichia coli in response to oxidative stress. Arch Biochem Biophys 1993; 301: 379-384
    • (1993) Arch Biochem Biophys , vol.301 , pp. 379-384
    • Liochev, S.I.1    Fridovich, I.2
  • 44
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli , is controlled by the soxRS regulon
    • Liochev SI, Fridovich I: Fumarase C, the stable fumarase of Escherichia coli , is controlled by the soxRS regulon. Proc Natl Acad Sci USA 1992; 89: 5892-5896
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 45
    • 0027411681 scopus 로고
    • Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: Positive control of the micF antisense RNA by the soxRS locus
    • Chou JH, Greenberg JT, Demple B: Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus. J Bacteriol 1993; 175: 1026-1031
    • (1993) J Bacteriol , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 46
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • Antelmann H, Helmann JD: Thiol-based redox switches and gene regulation. Antioxid Redox Signal 2011; 14: 1049-1063
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 47
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello PJ, Demple B: Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 2001; 19: 109-114
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 48
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thioldisulfide status
    • Åslund F, Zheng M, Beckwith J, Storz G: Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thioldisulfide status. Proc Natl Acad Sci USA 1999; 96: 6161-6165
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6161-6165
    • Åslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 49
    • 0032040092 scopus 로고    scopus 로고
    • Free radical formation in the peroxynitrous acid (ONOOH)/peroxynitrite (ONOO-) system
    • Merényi G, Lind J: Free radical formation in the peroxynitrous acid (ONOOH)/peroxynitrite (ONOO-) system. Chem Res Toxicol 1998; 11: 243-246
    • (1998) Chem Res Toxicol , vol.11 , pp. 243-246
    • Merényi, G.1    Lind, J.2
  • 50
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • Radi R: Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci USA 2004; 101: 4003-4008
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 51
    • 0344196903 scopus 로고    scopus 로고
    • NOdependent protein nitration: A cell signaling event or an oxidative inflammatory response?
    • Schopfer FJ, Baker PRS, Freeman BA: NOdependent protein nitration: a cell signaling event or an oxidative inflammatory response? Trends Biochem Sci 2003; 28: 646-654
    • (2003) Trends Biochem Sci , vol.28 , pp. 646-654
    • Schopfer, F.J.1    Baker, P.R.S.2    Freeman, B.A.3
  • 52
    • 0033214459 scopus 로고    scopus 로고
    • Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical
    • Goss SPA, Singh RJ, Kalyanaraman B: Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical. J Biol Chem 1999; 274: 28233-28239.
    • (1999) J Biol Chem , vol.274 , pp. 28233-28239
    • Goss, S.P.A.1    Singh, R.J.2    Kalyanaraman, B.3


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