Skip to main content

The Peroxiredoxin Repair Proteins

  • Chapter
Book cover Peroxiredoxin Systems

Part of the book series: Subcellular Biochemistry ((SCBI,volume 44))

Abstract

Sulfiredoxin and sestrin are cysteine sulfinic acid reductases that selectively reduce or repair the hyperoxidized forms of typical 2-Cys peroxiredoxins within eukaryotes. As such these enzymes play key roles in the modulation of peroxide-mediated cell signaling and cellular defense mechanisms. The unique structure of sulfiredoxin facilitates access to the peroxiredoxin active site and novel sulfur chemistry

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Apel, K., and Hirt, H., 2004, Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu. Rev. Plant Biol. 55: 373–399.

    Article  CAS  PubMed  Google Scholar 

  • Baker, L. M., Raudonikiene, A., Hoffman, P. S., and Poole, L. B., 2001, Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183: 1961–1973.

    Article  CAS  PubMed  Google Scholar 

  • Basu, M. K., and Koonin, E. V., 2005, Evolution of eukaryotic cysteine sulfinic acid reductase, sulfiredoxin (Srx), from bacterial chromosome partitioning protein ParB. Cell Cycle. 4: 947–952.

    CAS  PubMed  Google Scholar 

  • Biteau, B., Labarre, J., and Toledano, M. B., 2003, ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature. 425: 980–984.

    Article  CAS  PubMed  Google Scholar 

  • Bozonet, S. M., Findlay, V. J., Day, A. M., Cameron, J., Veal, E. A., and Morgan, B. A., 2005, Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide. J. Biol. Chem. 280: 23319–23327.

    Article  CAS  PubMed  Google Scholar 

  • Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., and Chumakov, P. M., 2004, Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science. 304: 596–600.

    Article  CAS  PubMed  Google Scholar 

  • Budanov, A. V., Shoshani, T., Faerman, A., Zelin, E., Kamer, I., Kalinski, H., Gorodin, S., Fishman, A., Chajut, A., Einat, P., Skaliter, R., Gudkov, A. V., Chumakov, P. M., and Feinstein, E., 2002, Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability. Oncogene. 21: 6017–6031.

    Article  CAS  PubMed  Google Scholar 

  • Budde, H., Flohé, L., Hecht, H. J., Hofmann, B., Stehr, M., Wissing, J., and Lünsdorf, H., 2003, Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei. Biol. Chem. 384: 619–633.

    Article  CAS  PubMed  Google Scholar 

  • Castillo, E. A., Ayte, J., Chiva, C., Moldon, A., Carrascal, M., Abian, J., Jones, N., and Hidalgo, E., 2002, Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues. Mol. Microbiol. 45: 243–254.

    Article  CAS  PubMed  Google Scholar 

  • Castro, H., Budde, H., Flohé, L., Hofmann, B., Lünsdorf, H., Wissing, J., and Tomas, A. M., 2002, Specificity and kinetics of a mitochondrial peroxiredoxin of Leishmania infantum. Free Radic. Biol. Med. 33: 1563–1574.

    Article  CAS  PubMed  Google Scholar 

  • Cesaratto, L., Vascotto, C., D’Ambrosio, C., Scaloni, A., Baccarani, U., Paron, I., Damante, G., Calligaris, S., Quadrifoglio, F., Tiribelli, C., and Tell, G., 2005, Overoxidation of peroxiredoxins as an immediate and sensitive marker of oxidative stress in HepG2 cells and its application to the redox effects induced by ischemia/reperfusion in human liver. Free Radic. Res. 39: 255–268.

    Article  CAS  PubMed  Google Scholar 

  • Chae, H. J., Kim, K., and Kim, I. H., 1999, Redox Regulation of cell signaling and its clinical application, Marcel Dekker, Inc., New York, pp. 85–92.

    Google Scholar 

  • Chae, H. Z., Chung, S. J., and Rhee, S. G., 1994, Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269: 27670–27678.

    CAS  PubMed  Google Scholar 

  • Chae, H. Z., Kang, S. W., and Rhee, S. G., 1999,. Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods Enzymol. 300: 219–226.

    Article  CAS  PubMed  Google Scholar 

  • Chae, H. Z., Kim, H. J., Kang, S. W., and Rhee, S. G., 1999, Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45: 101–112.

    Article  CAS  PubMed  Google Scholar 

  • Chae, H. Z., Robison, K., Poole, L. B., Church, G., Storz, G., and Rhee, S. G., 1994, Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. U.S.A. 91: 7017–7021.

    Article  CAS  PubMed  Google Scholar 

  • Chang, T. S., Jeong, W., Choi, S. Y., Yu, S., Kang, S. W., and Rhee, S. G., 2002, Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. J. Biol. Chem. 277: 25370–25376.

    Article  CAS  PubMed  Google Scholar 

  • Chang, T. S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., and Rhee, S. G., 2004, Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J. Biol. Chem. 279: 50994–51001.

    Article  CAS  PubMed  Google Scholar 

  • Chevallet, M., Wagner, E., Luche, S., van Dorsselaer, A., Leize-Wagner, E., and Rabilloud, T., 2003, Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress. J. Biol. Chem. 278: 37146–37153.

    Article  CAS  PubMed  Google Scholar 

  • Christman, M. F., Morgan, R. W., Jacobson, F. S., and Ames, B. N., 1985, Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 41: 753–762.

    Article  CAS  PubMed  Google Scholar 

  • Chuang, M. H., Wu, M. S., Lo, W. L., Lin, J. T., Wong, C. H., and Chiou, S. H., 2006, The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function. Proc. Natl. Acad. Sci. U.S.A. 103: 2552–2557.

    Article  CAS  PubMed  Google Scholar 

  • Claiborne, A., Yeh, J. I., Mallett, T. C., Luba, J., Crane, E. J., 3rd, Charrier, V., and Parsonage, D., 1999, Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry. 38: 15407–15416.

    Article  CAS  PubMed  Google Scholar 

  • Degols, G., Shiozaki, K., and Russell, P., 1996, Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe. Mol. Cell Biol. 16: 2870–2877.

    CAS  Google Scholar 

  • Dietz, K. J., Horling, F., König, J., and Baier, M., 2002, The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J. Exp. Bot. 53: 1321–1329.

    Article  CAS  PubMed  Google Scholar 

  • Dietz, K. J., Jacob, S., Oelze, M. L., Laxa, M., Tognetti, V., de Miranda, S. M., Baier, M., and Finkemeier, I., 2006, The function of peroxiredoxins in plant organelle redox metabolism. J. Exp. Bot. 57: 1697–1709.

    Article  CAS  PubMed  Google Scholar 

  • Eichhorn, E., van der Ploeg, J. R., and Leisinger, T., 1999, Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274: 26639–26646.

    Article  CAS  PubMed  Google Scholar 

  • Findlay, V. J., Tapiero, H., and Townsend, D. M., 2005, Sulfiredoxin: a potential therapeutic agent? Biomed. Pharmacother. 59: 374–379.

    Article  CAS  PubMed  Google Scholar 

  • Findlay, V. J., Townsend, D. M., Morris, T. E., Fraser, J. P., He, L., and Tew, K. D., 2006, A novel role for human sulfiredoxin in the reversal of glutathionylation. Cancer Res. 66: 6800–6806.

    Article  CAS  PubMed  Google Scholar 

  • Finlayson, A. J., MacKenzie, S. L., and Finley, F. W., 1979, Reaction of alanine-3-sulfinic acid with 2-mercaptoethanol. Can. J. Chem. 57: 2073–2077.

    Article  CAS  Google Scholar 

  • Flohé, L., Budde, H., Bruns, K., Castro, H., Clos, J., Hofmann, B., Kansal-Kalavar, S., Krumme, D., Menge, U., Plank-Schumacher, K., Sztajer, H., Wissing, J., Wylegalla, C., and Hecht, H. J., 2002, Tryparedoxin peroxidase of Leishmania donovani: molecular cloning, heterologous expression, specificity, and catalytic mechanism. Arch. Biochem. Biophys. 397: 324–335.

    Article  PubMed  Google Scholar 

  • Hamann, M., Zhang, T., Hendrich, S., and Thomas, J. A., 2002, Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol. 348: 146–156.

    Article  CAS  PubMed  Google Scholar 

  • Hofmann, B., Hecht, H.-J., and Flohé, L., 2002, Peroxiredoxins. Biol. Chem. 383: 347–364.

    Article  CAS  PubMed  Google Scholar 

  • Isermann, K., Liebau, E., Roeder, T., and Bruchhaus, I., 2004, A peroxiredoxin specifically expressed in two types of pharyngeal neurons is required for normal growth and egg production in Caenorhabditis elegans. J. Mol. Biol. 338: 745–755.

    Article  CAS  PubMed  Google Scholar 

  • Jacob, C., Holme, A. L., and Fry, F. H., 2004, The sulfinic acid switch in proteins. Org. Biomol. Chem. 2: 1953–1956.

    Article  CAS  PubMed  Google Scholar 

  • Jang, H. H., Kim, S. Y., Park, S. K., Jeon, H. S., Lee, Y. M., Jung, J. H., Lee, S. Y., Chae, H. B., Jung, Y. J., Lee, K. O., Lim, C. O., Chung, W. S., Bahk, J. D., Yun, D. J., and Cho, M. J., 2006, Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions. FEBS Lett. 580: 351–355.

    Article  CAS  PubMed  Google Scholar 

  • Jang, H. H., Lee, K. O., Chi, Y. H., Jung, B. G., Park, S. K., Park, J. H., Lee, J. R., Lee, S. S., Moon, J. C., Yun, J. W., Choi, Y. O., Kim, W. Y., Kang, J. S., Cheong, G. W., Yun, D. J., Rhee, S. G., Cho, M. J., and Lee, S. Y., 2004, Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell. 117: 625–635.

    Article  CAS  PubMed  Google Scholar 

  • Jeong, W., Park, S. J., Chang, T. S., Lee, D. Y., and Rhee, S. G., 2006, Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J. Biol. Chem. 281: 14400–14407.

    Article  CAS  PubMed  Google Scholar 

  • Jönsson, T. J., Murray, M. S., Johnson, L. C., Poole, L. B., and Lowther, W. T., 2005, Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin. Biochemistry. 44: 8634–8642.

    Article  PubMed  Google Scholar 

  • Kim, K., Rhee, S. G., and Stadtman, E. R., 1985, Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron. J. Biol. Chem. 260: 15394–15397.

    CAS  PubMed  Google Scholar 

  • König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schürmann, P., and Dietz, K. J., 2002, The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. Proc. Natl. Acad. Sci. U.S.A. 99: 5738–5743.

    Article  PubMed  Google Scholar 

  • Koo, K. H., Lee, S., Jeong, S. Y., Kim, E. T., Kim, H. J., Kim, K., Song, K., and Chae, H. Z., 2002, Regulation of thioredoxin peroxidase activity by C-terminal truncation. Arch. Biochem. Biophys. 397: 312–318.

    Article  CAS  PubMed  Google Scholar 

  • Kudo, N., Taoka, H., Yoshida, M., and Horinouchi, S., 1999, Identification of a novel nuclear export signal sensitive to oxidative stress in yeast AP-1-like transcription factor. Ann. N. Y. Acad. Sci. 886: 204–207.

    Article  CAS  PubMed  Google Scholar 

  • Lee, D. Y., Rhee, S. G., Ferretti, J., and Gruschus, J. M., 2005, 1H, 15N, 13C chemical shift assignments of the human Sulfiredoxin (hSrx). J. Biomol. NMR. 32: 339.

    Article  CAS  PubMed  Google Scholar 

  • Liu, X. P., Liu, X. Y., Zhang, J., Xia, Z. L., Liu, X., Qin, H. J., and Wang, D. W., 2006, Molecular and functional characterization of sulfiredoxin homologs from higher plants. Cell Res. 16: 287–296.

    Article  CAS  PubMed  Google Scholar 

  • Martin, I. V., and MacNeill, S. A., 2002, ATP-dependent DNA ligases. Genome Biol. 3: REVIEWS3005.

    Google Scholar 

  • Mitsumoto, A., Nakagawa, Y., Takeuchi, A., Okawa, K., Iwamatsu, A., and Takanezawa, Y., 2001, Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat. Free Radic. Res. 35: 301–310.

    Article  CAS  PubMed  Google Scholar 

  • Mitsumoto, A., Takanezawa, Y., Okawa, K., Iwamatsu, A., and Nakagawa, Y. (2001). Variants of peroxiredoxins expression in response to hydroperoxide stress. Free Radic. Biol. Med. 30: 625–635.

    Article  CAS  PubMed  Google Scholar 

  • Moon, J. C., Hah, Y. S., Kim, W. Y., Jung, B. G., Jang, H. H., Lee, J. R., Kim, S. Y., Lee, Y. M., Jeon, M. G., Kim, C. W., Cho, M. J., and Lee, S. Y. (2005). Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. J. Biol. Chem. 280: 28775–28784.

    Article  CAS  PubMed  Google Scholar 

  • Moore, R. B., Mankad, M. V., Shriver, S. K., Mankad, V. N., and Plishker, G. A. (1991). Reconstitution of Ca(2+)-dependent K+transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J. Biol. Chem. 266: 18964–18968.

    CAS  PubMed  Google Scholar 

  • Morgan, R. W., Christman, M. F., Jacobson, F. S., Storz, G., and Ames, B. N., 1986, Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc. Natl. Acad. Sci. U.S.A. 83: 8059–8063.

    Article  CAS  PubMed  Google Scholar 

  • Niimura, Y., Poole, L. B., and Massey, V., 1995, Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component. J. Biol. Chem. 270: 25645–25650.

    Article  CAS  PubMed  Google Scholar 

  • Nogoceke, E., Gommel, D. U., Kiess, M., Kalisz, H. M., and Flohé, L., 1997, A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378: 827–836.

    Article  CAS  PubMed  Google Scholar 

  • Pannifer, A. D., Flint, A. J., Tonks, N. K., and Barford, D., 1998, Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography. J. Biol. Chem. 273: 10454–10462.

    Article  CAS  PubMed  Google Scholar 

  • Poole, L. B., 1996, Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry. 35: 65–75.

    Article  CAS  PubMed  Google Scholar 

  • Quinn, J., Findlay, V. J., Dawson, K., Millar, J. B., Jones, N., Morgan, B. A., and Toone, W. M., 2002, Distinct regulatory proteins control the graded transcriptional response to increasing H(2)O(2) levels in fission yeast Schizosaccharomyces pombe. Mol. Biol. Cell. 13: 805–816.

    Article  CAS  PubMed  Google Scholar 

  • Rhee, S. G., 2006, Cell signaling. H2O2, a necessary evil for cell signaling. Science. 312: 1882–1883.

    Article  PubMed  Google Scholar 

  • Schröder, E., Littlechild, J. A., Lebedev, A. A., Errington, N., Vagin, A. A., and Isupov, M. N., 2000, Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7Å resolution. Structure Fold Des. 8: 605–615.

    Article  PubMed  Google Scholar 

  • Seaver, L. C., and Imlay, J. A., 2001, Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183: 7182–7189.

    Article  CAS  PubMed  Google Scholar 

  • Shiozaki, K., and Russell, P., 1995, Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature. 378: 739–743.

    Article  CAS  PubMed  Google Scholar 

  • Shiozaki, K., and Russell, P., 1996, Conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast. Genes Dev. 10: 2276–2288.

    Article  CAS  PubMed  Google Scholar 

  • Timson, D. J., Singleton, M. R., and Wigley, D. B., 2000, DNA ligases in the repair and replication of DNA. Mutat. Res. 460: 301–318.

    CAS  PubMed  Google Scholar 

  • Toone, W. M., Kuge, S., Samuels, M., Morgan, B. A., Toda, T., and Jones, N., 1998, Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (Exportin) and the stress-activated MAP kinase Sty1/Spc1. Genes Dev. 12: 1453–1463.

    Article  CAS  PubMed  Google Scholar 

  • Traut, T. W., 1994, The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. Eur. J. Biochem. 222: 9–19.

    Article  CAS  PubMed  Google Scholar 

  • Veal, E. A., Findlay, V. J., Day, A. M., Bozonet, S. M., Evans, J. M., Quinn, J., and Morgan, B. A., 2004, A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. Mol. Cell. 15: 129–139.

    Article  CAS  PubMed  Google Scholar 

  • Velasco-Miguel, S., Buckbinder, L., Jean, P., Gelbert, L., Talbott, R., Laidlaw, J., Seizinger, B., and Kley, N., 1999, PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes. Oncogene. 18: 127–137.

    Article  CAS  PubMed  Google Scholar 

  • Vivancos, A. P., Castillo, E. A., Biteau, B., Nicot, C., Ayte, J., Toledano, M. B., and Hidalgo, E., 2005, A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc. Natl. Acad. Sci U.S.A. 102: 8875–8880.

    Article  CAS  PubMed  Google Scholar 

  • Vivancos, A. P., Castillo, E. A., Jones, N., Ayte, J., and Hidalgo, E., 2004, Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration. Mol. Microbiol. 52: 1427–1435.

    Article  CAS  PubMed  Google Scholar 

  • Wilkinson, M. G., Samuels, M., Takeda, T., Toone, W. M., Shieh, J. C., Toda, T., Millar, J. B., and Jones, N., 1996, The Atf1 transcription factor is a target for the Sty1 stress-activated MAP kinase pathway in fission yeast. Genes Dev. 10: 2289–2301.

    Article  CAS  PubMed  Google Scholar 

  • Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K. S., Kang, S. W., Kim, K., and Rhee, S. G., 2003, Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science. 300: 653–656.

    Article  CAS  PubMed  Google Scholar 

  • Woo, H. A., Jeong, W., Chang, T. S., Park, K. J., Park, S. J., Yang, J. S., and Rhee, S. G., 2005, Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. J. Biol. Chem. 280: 3125–3128.

    Article  CAS  PubMed  Google Scholar 

  • Woo, H. A., Kang, S. W., Kim, H. K., Yang, K. S., Chae, H. Z., and Rhee, S. G., 2003, Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J. Biol. Chem. 278: 47361–47364.

    Article  CAS  PubMed  Google Scholar 

  • Wood, Z. A., Poole, L. B., and Karplus, P. A., 2003, Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science. 300: 650–653.

    Article  CAS  PubMed  Google Scholar 

  • Wood, Z. A., Schröder, E., Harris, R. J., and Poole, L. B., 2003, Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28: 32–40.

    Article  CAS  PubMed  Google Scholar 

  • 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.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2007 Springer

About this chapter

Cite this chapter

Jönsson, T.J., Lowther, W.T. (2007). The Peroxiredoxin Repair Proteins. In: Flohé, L., Harris, J.R. (eds) Peroxiredoxin Systems. Subcellular Biochemistry, vol 44. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6051-9_6

Download citation

Publish with us

Policies and ethics