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Volumn , Issue SUPPL. 49, 2011, Pages

Measurement of peroxiredoxin activity

Author keywords

Antioxidant enzymes; Antioxidants; Cysteine oxidation; FOX; HRP; Hydrogen peroxide; Hydroperoxides; PRDX; Prx; Redox catalysis; Sulfenic acids; Thiol peroxidase

Indexed keywords

CUMENE HYDROPEROXIDE; CYSTEINE; DITHIOTHREITOL; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LINOLEIC ACID; PEROXIDE; PEROXIREDOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TERT BUTYL HYDROPEROXIDE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 84858283859     PISSN: 19349254     EISSN: 19349262     Source Type: Journal    
DOI: 10.1002/0471140856.tx0710s49     Document Type: Article
Times cited : (64)

References (66)
  • 1
    • 0037646517 scopus 로고    scopus 로고
    • Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61
    • Baker, L.M. and Poole, L.B. 2003. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. J. Biol. Chem. 278:9203-9211.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9203-9211
    • Baker, L.M.1    Poole, L.B.2
  • 2
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxindependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • Baker, L.M., Raudonikiene, A., Hoffman, P.S., and Poole, L.B. 2001. Essential thioredoxindependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization. J. Bacteriol. 183:1961-1973.
    • (2001) J. Bacteriol. , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 3
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk, R., Lima, C.D., Erdjument-Bromage, H., Tempst, P., and Nathan, C. 2002. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295:1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 4
    • 34548439447 scopus 로고    scopus 로고
    • Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: General properties and factors affecting PrxIII activity and oligomeric state
    • Cao, Z., Bhella, D., and Lindsay, J.G. 2007. Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: General properties and factors affecting PrxIII activity and oligomeric state. J. Mol. Biol. 372:1022-1033.
    • (2007) J. Mol. Biol. , vol.372 , pp. 1022-1033
    • Cao, Z.1    Bhella, D.2    Lindsay, J.G.3
  • 5
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha, M.K., Kim, W.C., Lim, C.J., Kim, K., and Kim, I.H. 2004. Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J. Biol. Chem. 279:8769-8778.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8769-8778
    • Cha, M.K.1    Kim, W.C.2    Lim, C.J.3    Kim, K.4    Kim, I.H.5
  • 9
    • 73849144014 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
    • Cox, A.G.,Winterbourn, C.C., and Hampton, M.B. 2010. Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 425:313-325.
    • (2010) Biochem. J. , vol.425 , pp. 313-325
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 11
    • 0016500533 scopus 로고
    • A kinetic study of the reaction of horseradish peroxidase with hydrogen peroxide
    • Dolman, D., Newell, G.A., and Thurlow, M.D. 1975. A kinetic study of the reaction of horseradish peroxidase with hydrogen peroxide. Can. J. Biochem. 53:495-501.
    • (1975) Can. J. Biochem. , vol.53 , pp. 495-501
    • Dolman, D.1    Newell, G.A.2    Thurlow, M.D.3
  • 12
    • 33845934366 scopus 로고    scopus 로고
    • Spectroscopy of horseradish peroxidase. I. Optical, resonance raman, magnetic circular dichroism, x-ray absorption, and diffraction
    • (Dunford, H. B. eds.), JohnWiley&Sons, Hoboken, N.J
    • Dunford, H.B. 1999. Spectroscopy of horseradish peroxidase. I. Optical, resonance raman, magnetic circular dichroism, x-ray absorption, and diffraction. In Heme peroxidases (Dunford, H.B. eds.) pp 135-174. JohnWiley&Sons, Hoboken, N.J.
    • (1999) Heme peroxidases , pp. 135-174
    • Dunford, H.B.1
  • 13
    • 0031888539 scopus 로고    scopus 로고
    • Toxicity of linoleic acid hydroperoxide to Saccharomyces cerevisiae: Involvement of a respiration-related process for maximal sensitivity and adaptive response
    • Evans, M.V., Turton, H.E.,Grant, C.M., andDawes, I.W. 1998. Toxicity of linoleic acid hydroperoxide to Saccharomyces cerevisiae: Involvement of a respiration-related process for maximal sensitivity and adaptive response. J. Bacteriol. 180:483-490.
    • (1998) J. Bacteriol. , vol.180 , pp. 483-490
    • Evans, M.V.1    Turton, H.E.2    Grant, C.M.3    Dawes, I.W.4
  • 14
    • 0018449709 scopus 로고
    • Rat liver cytosolic glutathione peroxidase: Reactivity with linoleic acid hydroperoxide and cumene hydroperoxide
    • Forstrom, J.W., Stults, F.H., and Tappel, A.L. 1979. Rat liver cytosolic glutathione peroxidase: Reactivity with linoleic acid hydroperoxide and cumene hydroperoxide. Arch. Biochem. Biophys. 193:51-55.
    • (1979) Arch. Biochem. Biophys. , vol.193 , pp. 51-55
    • Forstrom, J.W.1    Stults, F.H.2    Tappel, A.L.3
  • 15
    • 77956171017 scopus 로고    scopus 로고
    • Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
    • Hall, A., Nelson, K.J., Poole, L.B., and Karplus, P.A. 2010. Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid. Redox Signal. 402:194-209.
    • (2010) Antioxid. Redox Signal. , vol.402 , pp. 194-209
    • Hall, A.1    Nelson, K.J.2    Poole, L.B.3    Karplus, P.A.4
  • 16
    • 0014132523 scopus 로고
    • Thioredoxin 2: Cleavage with cyanogen bromide
    • Holmgren, A. and Reichard, P. 1967. Thioredoxin 2: Cleavage with cyanogen bromide. Eur. J. Biochem. 2:187-196.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 187-196
    • Holmgren, A.1    Reichard, P.2
  • 17
    • 77952396492 scopus 로고    scopus 로고
    • Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: Catalytic mechanism and high reactivity
    • Horta, B.B., de Oliveira, M.A., Discola, K.F., Cussiol, J.R., and Netto, L.E. 2010. Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: Catalytic mechanism and high reactivity. J. Biol. Chem. 285:16051-16065.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16051-16065
    • Horta, B.B.1    de Oliveira, M.A.2    Discola, K.F.3    Cussiol, J.R.4    Netto, L.E.5
  • 18
    • 70350050576 scopus 로고    scopus 로고
    • Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics
    • Hugo, M., Turell, L.,Manta,B., Botti, H.,Monteiro, G., Netto, L.E., Alvarez, B., Radi, R., and Trujillo, M. 2009. Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics. Biochemistry 48:9416-9426.
    • (2009) Biochemistry , vol.48 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.E.6    Alvarez, B.7    Radi, R.8    Trujillo, M.9
  • 19
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger, T., Budde, H., Flohe, L., Menge, U., Singh, M., Trujillo, M., and Radi, R. 2004. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423:182-191.
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 182-191
    • Jaeger, T.1    Budde, H.2    Flohe, L.3    Menge, U.4    Singh, M.5    Trujillo, M.6    Radi, R.7
  • 20
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a newmember of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family
    • Jeong, W., Cha, M.K., and Kim, I.H. 2000. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a newmember of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family. J. Biol. Chem. 275:2924-2930.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 21
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • Kang, S.W., Baines, I.C., and Rhee, S.G. 1998. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273:6303-6311.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 22
    • 28244495868 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxin function in intracellular signal transduction: Therapeutic implications
    • Kang, S.W., Rhee, S.G., Chang, T.S., Jeong,W., and Choi,M.H. 2005. 2-Cys peroxiredoxin function in intracellular signal transduction: Therapeutic implications. Trends Mol. Med. 11:571-578.
    • (2005) Trends Mol. Med. , vol.11 , pp. 571-578
    • Kang, S.W.1    Rhee, S.G.2    Chang, T.S.3    Jeong, W.4    Choi, M.H.5
  • 23
    • 17644426975 scopus 로고    scopus 로고
    • Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide
    • Klomsiri, C., Panmanee, W., Dharmsthiti, S., Vattanaviboon, P., and Mongkolsuk, S. 2005. Novel roles of ohrR-ohr in Xanthomonas sensing, metabolism, and physiological adaptive response to lipid hydroperoxide. J. Bacteriol. 187:3277-3281.
    • (2005) J. Bacteriol. , vol.187 , pp. 3277-3281
    • Klomsiri, C.1    Panmanee, W.2    Dharmsthiti, S.3    Vattanaviboon, P.4    Mongkolsuk, S.5
  • 24
    • 38749091365 scopus 로고    scopus 로고
    • Evolution of the peroxiredoxins
    • (Flohé, L. and Harris, J. R. eds.), Springer, New York
    • Knoops, B., Loumaye, E., and Van Der Eecken, V. 2007. Evolution of the peroxiredoxins. In Peroxiredoxin Systems (Flohé, L. and Harris, J.R. eds.) pp. 27-40. Springer, New York.
    • (2007) Peroxiredoxin Systems , pp. 27-40
    • Knoops, B.1    Loumaye, E.2    Van Der Eecken, V.3
  • 25
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause, G. and Holmgren, A. 1991. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J. Biol. Chem. 266:4056-4066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 27
    • 0028946279 scopus 로고
    • Effect of pyridine nucleotide on the oxidative halfreaction of Escherichia coli thioredoxin reductase
    • Lennon, B.W. and Williams, C.H. Jr. 1995. Effect of pyridine nucleotide on the oxidative halfreaction of Escherichia coli thioredoxin reductase. Biochemistry 34:3670-3677.
    • (1995) Biochemistry , vol.34 , pp. 3670-3677
    • Lennon, B.W.1    Williams Jr., C.H.2
  • 28
    • 79251550085 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin
    • Lowther, W.T. and Haynes, A.C. 2010. Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin. Antioxid. Redox Signal. 15:99-109.
    • (2010) Antioxid. Redox Signal. , vol.15 , pp. 99-109
    • Lowther, W.T.1    Haynes, A.C.2
  • 29
    • 1642326559 scopus 로고    scopus 로고
    • Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST
    • Manevich,Y., Feinstein, S.I., and Fisher,A.B. 2004. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 31
    • 34247604468 scopus 로고    scopus 로고
    • Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiolspecific antioxidant paradigm, revealing another function of vitamin C
    • Monteiro, G., Horta, B.B., Pimenta, D.C., Augusto, O., and Netto, L.E. 2007. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiolspecific antioxidant paradigm, revealing another function of vitamin C. Proc. Natl. Acad. Sci. U. S. A. 104:4886-4891.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 4886-4891
    • Monteiro, G.1    Horta, B.B.2    Pimenta, D.C.3    Augusto, O.4    Netto, L.E.5
  • 32
  • 33
    • 79551493261 scopus 로고    scopus 로고
    • Analysis of the peroxiredoxin family: Using active site structure and sequence information for global classification and residue analysis
    • Nelson, K.J., Knutson, S.T., Soito, L., Klomsiri, C., Poole, L.B., and Fetrow, J.S. 2011. Analysis of the peroxiredoxin family: Using active site structure and sequence information for global classification and residue analysis. Proteins 79:947-964.
    • (2011) Proteins , vol.79 , pp. 947-964
    • Nelson, K.J.1    Knutson, S.T.2    Soito, L.3    Klomsiri, C.4    Poole, L.B.5    Fetrow, J.S.6
  • 35
    • 33845917628 scopus 로고    scopus 로고
    • Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics
    • Ogusucu, R., Rettori, D., Munhoz, D.C., Soares Netto, L.E., and Augusto, O. 2007. Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics. Free Radic. Biol. Med. 42:326-334.
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 326-334
    • Ogusucu, R.1    Rettori, D.2    Munhoz, D.C.3    Soares Netto, L.E.4    Augusto, O.5
  • 36
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • Parsonage, D., Youngblood, D.S., Sarma, G.N., Wood, Z.A., Karplus, P.A., and Poole, L.B. 2005. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44:10583-10592.
    • (2005) Biochemistry , vol.44 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Sarma, G.N.3    Wood, Z.A.4    Karplus, P.A.5    Poole, L.B.6
  • 37
    • 40849136587 scopus 로고    scopus 로고
    • Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
    • Parsonage, D., Karplus, P.A., and Poole, L.B. 2008. Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc. Natl. Acad. Sci. U.S.A. 105:8209-8214.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8209-8214
    • Parsonage, D.1    Karplus, P.A.2    Poole, L.B.3
  • 38
    • 77950870461 scopus 로고    scopus 로고
    • Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum
    • Parsonage,D., Desrosiers, D.C., Hazlett, K.R., Sun, Y., Nelson, K.J., Cox, D.L., Radolf, J.D., and Poole, L.B. 2010a. Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum. Proc. Natl. Acad. Sci. U.S.A. 107:6240-6245.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 6240-6245
    • Parsonage, D.1    Desrosiers, D.C.2    Hazlett, K.R.3    Sun, Y.4    Nelson, K.J.5    Cox, D.L.6    Radolf, J.D.7    Poole, L.B.8
  • 39
    • 79958067312 scopus 로고    scopus 로고
    • Engineering of fluorescent reporters into redox domains to monitor electron transfers
    • Parsonage, D., Reeves, S.A., Karplus, P.A., and Poole, L.B. 2010b. Engineering of fluorescent reporters into redox domains to monitor electron transfers. Methods Enzymol. 474:1-21.
    • (2010) Methods Enzymol , vol.474 , pp. 1-21
    • Parsonage, D.1    Reeves, S.A.2    Karplus, P.A.3    Poole, L.B.4
  • 40
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • Pedrajas, J.R., Miranda-Vizuete, A., Javanmardy, N., Gustafsson, J.A., and Spyrou, G. 2000. Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J. Biol. Chem. 275:16296-16301.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 41
    • 77954140186 scopus 로고    scopus 로고
    • Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae
    • Pedrajas, J.R., Padilla, C.A., McDonagh, B., and Barcena, J.A. 2010. Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae. Antioxid. Redox Signal. 13:249-258.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 249-258
    • Pedrajas, J.R.1    Padilla, C.A.2    McDonagh, B.3    Barcena, J.A.4
  • 43
    • 9744232974 scopus 로고    scopus 로고
    • Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
    • Poole, L.B. 2005. Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 433:240-254.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 240-254
    • Poole, L.B.1
  • 44
    • 38749094500 scopus 로고    scopus 로고
    • The catalytic mechanism of peroxiredoxins
    • (L. Flohé, and J. R. Harris, eds.), Springer, New York
    • Poole, L.B. 2007. The catalytic mechanism of peroxiredoxins. In Peroxiredoxin Systems (L. Flohé, and J.R. Harris, eds.) pp. 61-81. Springer, New York.
    • (2007) Peroxiredoxin Systems , pp. 61-81
    • Poole, L.B.1
  • 45
    • 0030032612 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins
    • Poole, L.B. and Ellis, H.R. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35:56-64.
    • (1996) Biochemistry , vol.35 , pp. 56-64
    • Poole, L.B.1    Ellis, H.R.2
  • 46
    • 0036371370 scopus 로고    scopus 로고
    • Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase
    • Poole, L.B. and Ellis, H.R. 2002. Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. Methods Enzymol. 348:122-136.
    • (2002) Methods Enzymol , vol.348 , pp. 122-136
    • Poole, L.B.1    Ellis, H.R.2
  • 47
    • 0034612366 scopus 로고    scopus 로고
    • AhpF can be dissected into two functional units: Tandem repeats of two thioredoxinlike folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like Cterminus to AhpC
    • Poole, L.B., Godzik, A., Nayeem, A., and Schmitt, J.D. 2000. AhpF can be dissected into two functional units: Tandem repeats of two thioredoxinlike folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like Cterminus to AhpC. Biochemistry 39:6602-6615.
    • (2000) Biochemistry , vol.39 , pp. 6602-6615
    • Poole, L.B.1    Godzik, A.2    Nayeem, A.3    Schmitt, J.D.4
  • 48
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., and Lunardi, J. 2002. 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) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 49
    • 61449217799 scopus 로고    scopus 로고
    • Highly active dimeric and lowactivity tetrameric forms of selenium-containing rat thioredoxin reductase 1
    • Rengby, O., Cheng, Q.,Vahter, M., Jörnvall, H., and Arnér,E.S. 2009. Highly active dimeric and lowactivity tetrameric forms of selenium-containing rat thioredoxin reductase 1. Free Radic. Biol. Med. 46:893-904.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 893-904
    • Rengby, O.1    Cheng, Q.2    Vahter, M.3    Jörnvall, H.4    Arnér, E.S.5
  • 51
    • 2942532835 scopus 로고    scopus 로고
    • Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni
    • Sayed, A.A. and Williams, D.L. 2004. Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni. J. Biol. Chem. 279:26159-26166.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26159-26166
    • Sayed, A.A.1    Williams, D.L.2
  • 52
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L.C. and Imlay, J.A. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 54
    • 78651278810 scopus 로고    scopus 로고
    • PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family
    • Soito, L., Williamson, C., Knutson, S.T., Fetrow, J.S., Poole, L.B., and Nelson, K.J. 2010. PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family. Nucleic Acids Res. 39:D332- D337.
    • (2010) Nucleic Acids Res , vol.39
    • Soito, L.1    Williamson, C.2    Knutson, S.T.3    Fetrow, J.S.4    Poole, L.B.5    Nelson, K.J.6
  • 55
    • 35448954324 scopus 로고    scopus 로고
    • Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation
    • Trujillo, M., Clippe, A., Manta, B., Ferrer-Sueta, G., Smeets, A., Declercq, J.P., Knoops, B., and Radi, R. 2007. Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation. Arch. Biochem. Biophys. 467:95-106.
    • (2007) Arch. Biochem. Biophys. , vol.467 , pp. 95-106
    • Trujillo, M.1    Clippe, A.2    Manta, B.3    Ferrer-Sueta, G.4    Smeets, A.5    Declercq, J.P.6    Knoops, B.7    Radi, R.8
  • 56
    • 52049096372 scopus 로고    scopus 로고
    • Kinetic studies on peroxynitrite reduction by peroxiredoxins
    • Trujillo, M., Ferrer-Sueta, G., and Radi, R. 2008. Kinetic studies on peroxynitrite reduction by peroxiredoxins. Methods Enzymol. 441:173-196.
    • (2008) Methods Enzymol , vol.441 , pp. 173-196
    • Trujillo, M.1    Ferrer-Sueta, G.2    Radi, R.3
  • 57
    • 0036436682 scopus 로고    scopus 로고
    • Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxide-induced gene expression and protection against organic peroxides in Xanthomonas campestris
    • Vattanaviboon, P., Whangsuk, W., Panmanee, W., Klomsiri, C., Dharmsthiti, S., and Mongkolsuk, S. 2002. Evaluation of the roles that alkyl hydroperoxide reductase and Ohr play in organic peroxide-induced gene expression and protection against organic peroxides in Xanthomonas campestris. Biochem. Biophys. Res. Commun. 299:177-182.
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 177-182
    • Vattanaviboon, P.1    Whangsuk, W.2    Panmanee, W.3    Klomsiri, C.4    Dharmsthiti, S.5    Mongkolsuk, S.6
  • 58
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Veal, E.A., Day, A.M., and Morgan, B.A. 2007. Hydrogen peroxide sensing and signaling. Mol. Cell 26:1-14.
    • (2007) Mol. Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 59
    • 0023085803 scopus 로고
    • The ability of scavengers to distinguish OH·production in the ironcatalyzed Haber-Weiss reaction: Comparison of four assays forOH·
    • Winterbourn, C.C. 1987. The ability of scavengers to distinguish OH·production in the ironcatalyzed Haber-Weiss reaction: Comparison of four assays forOH·.Free Radic. Biol.Med. 3:33-39.
    • (1987) Free Radic. Biol.Med. , vol.3 , pp. 33-39
    • Winterbourn, C.C.1
  • 60
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • Winterbourn, C.C. 2008. Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4:278-286.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 61
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff, S.P. 1994. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Methods Enzymol. 233:182-189.
    • (1994) Methods Enzymol , vol.233 , pp. 182-189
    • Wolff, S.P.1
  • 63
    • 0035799315 scopus 로고    scopus 로고
    • Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis
    • Wood, Z.A., Poole, L.B., and Karplus, P.A. 2001. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis. Biochemistry 40:3900-3911.
    • (2001) Biochemistry , vol.40 , pp. 3900-3911
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 64
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z.A., Poole, L.B., and Karplus, P.A. 2003. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300:650-653.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 65
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang, K.S., Kang, S.W., Woo, H.A., Hwang, S.C., Chae, H.Z., Kim, K., and Rhee, S.G. 2002. 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) J. Biol. Chem. , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 66
    • 27744456655 scopus 로고    scopus 로고
    • Involvement of peroxiredoxin I in protecting cells from radiation-induced death
    • Zhang, B., Su, Y., Ai, G., Wang, Y., Wang, T., and Wang, F. 2005. Involvement of peroxiredoxin I in protecting cells from radiation-induced death. J. Radiat. Res. (Tokyo) 46:305-312.
    • (2005) J. Radiat. Res. (Tokyo) , vol.46 , pp. 305-312
    • Zhang, B.1    Su, Y.2    Ai, G.3    Wang, Y.4    Wang, T.5    Wang, F.6


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