Skip to main content

The Role of Peroxiredoxins in Oxygenic Photosynthesis of Cyanobacteria and Higher Plants: Peroxide Detoxification or Redox Sensing?

  • Chapter
Photoprotection, Photoinhibition, Gene Regulation, and Environment

Summary

Peroxiredoxins (Prx) constitute a group of recently identified peroxidases that detoxify a broad range of peroxides in distinct subcellular compartments, including chloroplasts. They are ubiquitously expressed in all organisms, i.e. bacteria, fungi, and animals, as well as in cyanobacteria and plants, in which they frequently represent a considerable fraction of total cellular and organellar protein. At least seven prxgenes are expressed in leaves of Arabidopsis. The gene products of four of them are targeted to chloroplasts. Five genes encoding (putative) Prx are found in Synechocystissp. PCC 6803. Based on such circumstantial evidence, as well as biochemical analysis and observations on photosynthetic organisms with modified levels of Prx, it has been established that a subset of Prx plays a role in the context of photosynthesis. The conclusion is further strengthened by studies that showed a modulation of prxgene expression in response to photosynthetic activity. This chapter describes the properties of peroxiredoxins in general and focuses on the role of Prx in protecting the photosynthetic apparatus from oxidative damage and, possibly, in redox signaling in photooxygenic cells.

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

  • Alphey MS, Bond CS, Tedaud E, Fairlamb AH and Hunter WN (2000) The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2-Cys peroxiredoxins. J Mol Biol 300: 903–916

    Google Scholar 

  • Armstrong F, Leung J, Grabov A, Brearley J, Giraudat J and Blatt MR (1995) Sensitivity of abscisic acid of guard cell K+ channels is suppressed by abi1-1, a mutant Arabidopsis gene encoding a putative protein phosphatase. Proc Natl Acad Sci USA 92: 9520–9524

    Article  PubMed  CAS  Google Scholar 

  • Asada K (1999) The water-water cycle in chloroplasts: Scavenging of active oxygen and dissipation of excess photons. Annu Rev Plant Physiol Plant Mol Biol 50: 601–639

    Article  PubMed  CAS  Google Scholar 

  • Asada K (2000) The water-water cycle as alternative photon and electron sinks. Philos Trans Roy Soc Lond 355: 1419–1432

    Article  CAS  Google Scholar 

  • Baier M and Dietz K-J (1996) Primary structure and expression of plant homologues of animal and fungal thioredoxindependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol Biol 31: 553–564

    Article  PubMed  CAS  Google Scholar 

  • Baier M and Dietz K-J (1997) The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. Plant J 12: 179– 190

    Article  PubMed  CAS  Google Scholar 

  • Baier M and Dietz K-J (1998) The costs and benefits of oxygen for photosynthesizing cells. Prog Bot 60: 282–314

    Google Scholar 

  • Baier M and Dietz K-J (1999a) Alkylhydroperoxide reductases: the way out of oxidative breakdown of lipids in chloroplasts. Trends Plant Sci 4: 166–168

    Article  Google Scholar 

  • Baier M and Dietz K-J (1999b) Protective function of chloroplast 2-Cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis. Plant Physiol 119: 1407–1414

    Article  CAS  Google Scholar 

  • Baier M, Noctor G, Foyer CH and Dietz K-J (2000) Antisense suppression of 2-Cys peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism. Plant Physiol 124: 823–832

    Article  PubMed  CAS  Google Scholar 

  • Baier M, Ströher E and Dietz K-J (2004) The acceptor availability at photosystem I andABAcontrol nuclear expression of 2-Cys peroxiredoxin-A in Arabidopsis thaliana. Plant Cell Physiol 45: 997–1006

    Article  PubMed  CAS  Google Scholar 

  • Br’eh’elin C, Meyer EH, de Souris JP, Bonnard G and Meyer Y (2003) Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: Similar sequences for divergent gene expression, protein localization, and activity. Plant Physiol 132: 2045–2057

    Article  CAS  Google Scholar 

  • Broin M and Rey P (2003) Potato plants lacking the CDSP 32 plastidic thioredoxin exhibit overoxidation of the BAS1 2-Cysteine peroxiredoxin and increased lipid peroxidation in thylakoid under photooxidative stress. Plant Physiol 132: 1335–1343

    Article  PubMed  CAS  Google Scholar 

  • Broin M, Cuin’e S, Eymery F and Rey P (2002) The plastidic 2- Cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. Plant Cell 14: 1417–1432

    Article  PubMed  CAS  Google Scholar 

  • Bryk R, Griffin P and Nathan C (2000) Peroxinitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211–215

    Google Scholar 

  • Campbell WS and Laudenbach DE (1995) Characterization of four superoxide dismutase genes from a filamentous cyanobacterium. J Bacteriol 177: 964–972

    PubMed  CAS  Google Scholar 

  • Carr NG and Whitton BA (1982) The Biology of Cyanobacteria. Blackwell Scientific Publishers, Oxford, UK

    Google Scholar 

  • Cha M-K and Kim I-H (1996) Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductases in human red blood cell. Biochem Biophys Res Commun 217: 900–907

    Article  Google Scholar 

  • Chadd HE, Newman J, Mann NH and Carr NG (1996) Identification of iron superoxide dismutase and a copper/zinc superoxide dismutase enzyme activity within the marine cyanobacterium Synechococcus sp.WH7803. FEMS Microbiol Lett 138: 161– 165

    Article  PubMed  CAS  Google Scholar 

  • Chae HZ, Kim IH, Kim K and Rhee SG (1993) Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J Biol Chem 268: 16815–16821

    PubMed  CAS  Google Scholar 

  • Chae HZ, Chung SJ and Rhee SG (1994) Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269: 27670– 27678

    PubMed  CAS  Google Scholar 

  • Chae HZ, Kang SW and Rhee SG (1999) Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods Enzymol 300: 219–226

    Article  PubMed  CAS  Google Scholar 

  • Cheong NE, Choi YO, Lee KO, Kim WY, Jung BG, Chi YH, Jeong JS, Kim K, Cho MJ and Lee SY (1999) Molecular cloning, expression, and functional characterization of a 2- Cys-peroxiredoxin in Chinese cabbage. Plant Mol Biol 40: 825–834

    Google Scholar 

  • Choi YO, Cheong NE, Lee KO, Jung BG, Hong CH, Jeong JH, Chi YH, Kim K, Cho MJ and Lee SY (1999) Cloning and expression of a newisotype of the peroxiredoxin gene in Chinese cabbage and its comparison to 2-Cys peroxiredoxin isolated from the same plant. Biochem Biophys Res Commun 258: 768–771

    Article  PubMed  CAS  Google Scholar 

  • Collin V, Issakidis-Bourguet E, Marchand C, Hirasawa M, Lancelin J-M, Knaff DB and Miginiac-Maslow M (2003) The Arabidopsis plastidial thioredoxins: New functions and new insights into specificity. J Biol Chem 278: 23747–23752

    Article  PubMed  CAS  Google Scholar 

  • Dietz K-J (2003a) Plant peroxiredoxins. Annu Rev Plant Biol 54: 93–107

    Article  CAS  Google Scholar 

  • Dietz K-J (2003b) Redox regulation, redox signalling and redox homeostasis in plants. Int Rev Cytol 228, 111–193

    Google Scholar 

  • Dietz K-J and Heber U (1984) Rate-limiting factors in leaf photosynthesis. I. Carbon fluxes in the Calvin cycle. Biochim Biophys Acta 767: 432–443.

    Article  CAS  Google Scholar 

  • Dietz K-J, Horling F, Konig 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  PubMed  CAS  Google Scholar 

  • Elstner EF (1990) Der Sauerstoff. Biochemie, Biologie, Medizin. Spektrum Akademischer Verlag, Heidelberg, Germany

    Google Scholar 

  • Fay P (1983) The Blue-Greens. Edward Arnold, Baltimore, USA

    Google Scholar 

  • Foyer CH and Noctor G (2000) Oxygen processing in photosynthesis: regulation and signalling. New Phytol 146: 359–388

    Article  CAS  Google Scholar 

  • Foyer CH, Lelandais M and Kunert K-J (1994) Photooxidative stress in plants. Physiol Plant 92: 696–717

    Article  CAS  Google Scholar 

  • Frausto da Silva JJR and Williams RJP (1993) The Biological Chemistry of the Elements. The Inorganic Chemistry of Life. Clarendon Press, Oxford

    Google Scholar 

  • Fridlyand LE and Scheibe R (1999) Controlled distribution of electrons between acceptors in chloroplasts: a theoretical consideration. Biochim Biophys Acta 1413: 31–42

    Article  CAS  Google Scholar 

  • Genot G, Wintz H, Houln’e G and Jamet E (2001) Molecular characterization of a bean chloroplastic 2-Cys peroxiredoxin. Plant Physiol Biochem 39: 449–459

    Article  CAS  Google Scholar 

  • Goyer A, Haslekas C, Miginiac-Maslow M, Klein U, Le Marechal P, Jacquot JP and Decottignies P (2002) Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii. Eur J Biochem 269: 272– 282

    Google Scholar 

  • Guerinot ML and Yi Y (1994) Iron: Nutritious, noxious, and not readily available. Plant Physiol 104: 815–820

    Google Scholar 

  • Helman Y, Tchernov D, Reinhold L, Shibata M, Ogawa T and Kaplan A (2003) Genes encoding A-type flavoproteins are essential for photoreduction of O2 in cyanobacteria. Curr Biol 13: 230–235

    Article  PubMed  CAS  Google Scholar 

  • Herbert SK, Samson G, Fork DC and Laudenbach DE (1992) Characterization of damage to photosystems I and II in a cyanobacterium lacking detectable iron superoxide dismutase activity. Proc Natl Acad Sci USA 89: 8716–8720

    Article  PubMed  CAS  Google Scholar 

  • Hofmann B, Hecht HJ and Floh’e L (2002) Peroxiredoxins. Biol Chem 383: 347–364

    Article  PubMed  CAS  Google Scholar 

  • Horling F,König J and Dietz K-J (2002) Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: Its expression and activity in comparison with other peroxiredoxins. Plant Physiol Biochem 40: 491–499

    Article  CAS  Google Scholar 

  • Horling F, Lamkemeyer P,König J, Finkemeier I, Kandlbinder A, Baier M and Dietz K-J (2003) Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana. Plant Physiol 131: 317–325

    Article  PubMed  CAS  Google Scholar 

  • Jakopitsch C, Ruker F, Regelsberger G, Dockal M, Peschek GA and Obinger C (1999) Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization. Biol Chem 380: 1087–1096

    Article  PubMed  CAS  Google Scholar 

  • Janssen-Heininger YMW, Persinger RL, Korn SH, Pantano C, McElhinney B, Reynaert NL, Langen RCJ, Ckless K, Shrivastava P and Poynter ME (2002) Reactive nitrogen species and cell signaling – Implications for death or survival of lung epithelium. Am J Resp Crit Care Med 166: 9–16

    Google Scholar 

  • Jin D-Y and Jeang K-T (2000) Peroxiredoxins in cell signalling and HIV infection. In: Sen CK, Sies H and Baeuerle PA (eds) Antioxidants and Redox Regulation of Genes, pp 382–409. Academic Press, San Diego

    Google Scholar 

  • Kaim W and Schwederski B (1995) Bioanorganische Chemie. Teubner, Stuttgart

    Google Scholar 

  • Kandlbinder A, Finkemeier I, Wormuth D, Hanitzsch M and Dietz K-J (2004) The antioxidant status of photosynthesising leaves under nutrient deficiency: redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana. Physiol Plant 120: 63–73

    Article  PubMed  CAS  Google Scholar 

  • Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamoto S, Kimura T, Hosouchi T, Matsuno A, Muraki A, Nakazaki N, Naruo K, Okumura S, Shimpo S, Takeuchi C, Wada T, Watanabe A, Yamada M, YasudaMand Tabata S (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions (supplement). DNA Res 3: 185–209

    Google Scholar 

  • Karpinski S, Escoubar C, Karpinska B, Creissen G and Mullineaux PM (1997) Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress. Plant Cell 9: 627– 640

    Article  PubMed  CAS  Google Scholar 

  • Kashino Y, Koike H, Yoshio M, Egashira H, Ikeuchi M, Pakrasi HB and Satoh K (2002) Low-molecular-mass polypeptide components of a photosystem II preparation from the thermophilic cyanobacterium Thermosynechococcus vulcanus. Plant Cell Physiol 43: 1366–1373

    Article  PubMed  CAS  Google Scholar 

  • Klughammer B, Baier M and Dietz K-J (1998) Inactivation by gene disruption of 2-Cysteine-peroxiredoxin in Synechocystis sp.PCC6803 leads to increased stress sensitivity. Physiol Plant 104: 699–706

    Article  CAS  Google Scholar 

  • Kong W, Shiota S, Shi YX, Nakayama H and Nakayama K (2000). A novel peroxiredoxin of the plant Sedum lineare is a homologue of the Escherichia coli bacterioferritin comigratory protein (Bcp). Biochem J 351: 107–114

    Article  PubMed  CAS  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 USA 99: 5738–5743

    Google Scholar 

  • König J, Lotte K, Plessow R, Brockhinke A, Baier M and Dietz K-J (2003) Reaction mechanism of plant 2-Cys peroxredoxin: Role of the C terminus and the quaternary structure. J Biol Chem 278: 24409–24420

    Google Scholar 

  • Lee J, SpectorD, Godon C, Labarre J and ToledanoMB(1999)A new antioxidant with alkyl hydroperoxide defense properties in yeast. J Biol Chem 274: 4537–4544

    Google Scholar 

  • Lee SP, Hwang YS, KimYJ, Kwon KS, Kim HJ, Kim K and Chae HZ (2001) Cyclophylin-A binds to peroxiredoxins and activates its peroxidase activity. J Biol Chem 276: 29826– 29832

    Google Scholar 

  • Li H, Singh AK and Sherman LA (2003) Differential gene expression and the regulation of oxidative stress in the cyanobacterium Synechocystis sp. PCC 6803. In: Hagemann M, Herrmann RG, Omata O and Tabata S (eds) Functional Genomics in Cyanobacteria, pp 54–55. Benediktbeuren, Germany MeinhardMand Grill E (2001) Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis. FEBS Lett 508: 443–446

    Google Scholar 

  • Meinhard M, Rodriguez PL and Grill E (2002) The sensitivity of ABI2 to hydrogen peroxide links the abscisic acid-response regulator to redox signaling. Planta 214: 775–782

    Google Scholar 

  • Melis A (1999) Photosystem-II damage and repair cycle in chloroplasts:what modulates the rate of photodamage in vivo? Trends Plant Sci 4: 130–135

    Google Scholar 

  • Michel KP and Pistorius EK (2004) Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: The function of IdiA and IsiA. Physiol Plant 120: 36–50

    Google Scholar 

  • Mutsuda M, Ishikawa T, Takeda T and Shigeoka S (1996) The catalase-peroxidase of SynechococcusPCC7942: purification, nucleotide sequence analysis and expression in Escherichia coli. Biochem J 316: 251–257

    Google Scholar 

  • Neill SJ, Desikan R and Hancock JT (2003) Nitric oxide signalling in plants. New Phytol 159: 11–35 Neumann CA, Krause DS, Carman CV, Das S, Dubey DP, Abraham JL, Bronson RT, Fujiwara Y, Orkin SH and Van

    Google Scholar 

  • Etten RA (2003) Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 424: 561–565

    Google Scholar 

  • Nguyˆen-Nhu NT (2003) Characterization of human peroxiredoxin 5 and homologous Saccharomyces cerevisiae alkyl hydroperoxide reductase 1. PhD-thesis, Universit’e Catholique de Louvain, Facult’e des Sciences

    Google Scholar 

  • Nishiyama Y, Yamamoto H, Allakhverdiev SI, Inaba M, Yokota A and Murata N (2001) Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery. EMBO J 20: 5587–5594

    Google Scholar 

  • Nishiyama Y, Allakhverdiev SI and Murata N (2005) Regulation by environmental conditions of the repair of photosystem II in cyanobacteria. In: Demmig-Adams B, Adams WW III and MattooAK(eds) Photoprotection, Photoinhibition, Gene Regulation, and Environment, pp 193–203. Springer, Dordrecht NoctorGand FoyerCH(1998) Ascorbate and glutathione:Keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49: 249–279

    Google Scholar 

  • Obinger C, Regelsberger G, Strasser G, Burner U and Peschek GA(1997) Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans. Biochem Biophys Res Commun 235: 545–552

    Google Scholar 

  • Paerl HW (2000) Marine plankton. In: Whitton BA and Potts M (eds) The Ecology of Cyanobacteria: Their Diversity in Time and Space, pp 121–148. Kluwer Academic Publishers, Dordrecht, London, Boston Patel RP, McAndrew J, Sellak H, White CR, Jo HJ, Freeman BA and Darley-Usmar VM (1999) Biological aspects of reactive nitrogen species. Biochim Biophys Acta 1411: 385–400

    Google Scholar 

  • Peltier JB, Friso G, Kalume DE, Roepstorff P, Nilsson F, Adamska I and van Wijk KJ (2000) Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12: 319–341

    Google Scholar 

  • Pfannschmidt T (2003) Chloroplast redox signals: how photosynthesis controls its own genes. Trends Plant Sci 8: 33–41 Pfannschmidt T, Allen JE and Oelmüller R (2001) Principles of redox control in photosynthesis gene expression. Physiol Plant 112: 1–9

    Google Scholar 

  • Pruvot G, Massimino J, PeltierGand Rey P (1996) Effects of low temperature, high salinity and endogenousABAon the synthesis of two chloroplastic drought-induced proteins in Solanum tuberosum. Physiol Plant 97: 123–131

    Google Scholar 

  • Rawyler A, Arpagaus S and Braendle R (2002) Impact of oxygen stress and energy availability on membrane stability of plant cells. Ann Bot 90: 499–507

    Google Scholar 

  • Regelsberger G, Jakopitsch C, Plasser L, Schwaiger H, Furtmüller G, Peschek G, Zamocky M and Obinger C (2002) Occurrence and biochemistry of hydroperoxidases in oxygenic phototrophic prokaryotes (cyanobacteria). Plant Physiol Biochem 40: 479–490

    Google Scholar 

  • Rey P, Pruvot G, Becuwe N, Eymery F, Rumeau D and Peltier G (1998) A novel-thioredoxin-like protein located in the chloroplast is induced bywater deficit in Solanum tuberosum L. Plant J 13: 97–107

    Article  PubMed  CAS  Google Scholar 

  • Rhee SG, Kang SW, Chang TS, Jeong W, Kim K (2001) Peroxiredoxin, a novel family of peroxidases. IUBMB Life 52: 35–41

    Article  PubMed  CAS  Google Scholar 

  • Rouhier N and Jacquot JP (2002) Plant peroxiredoxins: alternative hydroperoxide scavenging enzymes. Photosynth Res 74: 259–268

    Article  PubMed  CAS  Google Scholar 

  • Rouhier N, Gelhaye E, Corbier C and Jacquot JP (2004) Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin. Physiol Plant 120: 57–62

    Article  PubMed  CAS  Google Scholar 

  • Sakamoto A, Okumura T, Kaminaka H, Sumi K and Tanaka K (1995) Structure and differential response to abscisic acid of two promoters for the cytosolic copper/zinc-superoxide dismutase genes, SpdCc1 and SodCc2, in rice protoplasts. FEBS Lett 358: 62–66

    Article  PubMed  CAS  Google Scholar 

  • Sakamoto A, Tsukamoto S, Yamamoto H, Ueda-Hashimoto M, Takahashi M, Suzuki H and Morikawa H (2003) Functional complementation in yeast reveals a protective role of chloroplast 2-Cys peroxiredoxin against reactive nitrogen species. Plant J 33: 841–851

    Google Scholar 

  • Samuilov VD (1997) Photosynthetic oxygen: the role of H2O2. A review. Biochemistry (Moscow) 62: 451–454

    CAS  Google Scholar 

  • Schmetterer G (1994) Cyanobacterial respiration. In: Bryant DA (ed) The Molecular Biology of Cyanobacteria, pp 409–435. Kluwer Academic Publishers, The Netherlands, Dordrecht, Boston, London

    Google Scholar 

  • Schopf JW (2000) The fossil record: Tracing the roots of the cyanobacterial lineage. In: Whitton BA, Potts M (eds) The Ecology of Cyanobacteria: Their Diversity in Time and Space. Kluwer Academic Publishers, Dordrecht, London, Boston, pp 13–35

    Google Scholar 

  • Schröder E and Ponting CP (1998) Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily. Protein Sci 7: 2465–2468

    Article  PubMed  Google Scholar 

  • Schröder E, Littlechild JA, Lebedev AA, Errington N, Vagin AA and Isupov MN (2000) Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution. Structure 8: 605–615

    Article  PubMed  Google Scholar 

  • Schwartz SH, L’eon-Kloosterziel KM, Koornneef M and Zeevaart JAD. (1997) Biochemical characterization of the aba2 and aba3 mutant in Arabidopsis thaliana. Plant Physiol 114: 161–166

    Google Scholar 

  • Singh AK, Li H and Sherman LA (2004) Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803. Physiol Plant 120:27–35

    Article  PubMed  CAS  Google Scholar 

  • Stacy RAP, Munthe E, Steinum T, Sharma B and AalenRB(1996) Aperoxiredoxin antioxidant is encoded by a dormancy-related gene, Per1, expressed during late development in the aleurone and embryo of barley grains. Plant Mol Biol 31: 1205–1216

    Article  PubMed  CAS  Google Scholar 

  • Stacy RAP, Nordeng TW, Culianez-Macia FA and Aalen RB (1999) The dormancy-related peroxiredoxin antioxidant, PER1, is localized to the nucleus of barley embryo and aleurone cells. Plant J 19: 1–8

    Article  PubMed  CAS  Google Scholar 

  • Swofford D L (2002) PAUP*. Phylogenetic Analysis Using Parsimony (*and other methods). Version 4. Sinauer Associates, Sunderland, Massachusetts

    Google Scholar 

  • Tel-Or E, HuflejtMand Packer L (1985) The role of glutathione and ascorbate in hydroperoxide removal in cyanobacteria. Biochem Biophys Res Commun 132: 533–539

    Article  PubMed  CAS  Google Scholar 

  • Tel-Or E, Huflejt ME and Packer L (1986) Hydroperoxide metabolism in cyanobacteria. Arch Biochem Biophys 246: 396–402

    Article  PubMed  CAS  Google Scholar 

  • Thomas DJ, Avenson TJ, Thomas JB and Herbert SK (1998) A cyanobacterium lacking iron superoxide dismutase is sensitized to oxidative stress induced with methyl viologen but is not sensitized to oxidative stress induced with norflurazon. Plant Physiol 116: 1593–1602

    Article  PubMed  CAS  Google Scholar 

  • Tichy M and Vermaas W (1999) In vivo role of catalaseperoxidase in Synechocystis sp. strain PCC 6803. J Bacteriol 181: 1875–1882

    Google Scholar 

  • Van Breusegem F, Vranova E, Dat JF and Inz’e D (2001) The role of active oxygen species in plant signal transduction. Plant Sci 161: 405–414

    Article  Google Scholar 

  • Vermaas WFJ (2001) Photosynthesis and respiration in cyanobacteria. In: Encyclopedia of Life Sciences, pp 1–7. Nature Publishing Group, London

    Google Scholar 

  • Vranova E, van Breusegem F, Dat J, Belles-Boix E and Inz’e D (2002) The role of active oxygen species in plant signal transduction. In: Scheel D and Wasternack C (eds) Plant Signal Transduction, pp 45–73. Oxford University Press, Oxford

    Google Scholar 

  • Welinder KG (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struct Biol 2: 388–393

    Article  CAS  Google Scholar 

  • Whitton BA and Potts M (2000) Introduction to the cyanobacteria. In: Whitton BA and Potts M (eds) The Ecology of Cyanobacteria: Their Diversity in Time and Space, pp 1–11. Kluwer Academic Publishers, Dordrecht, London, Boston

    Google Scholar 

  • Wood ZA, Poole LB, Hantgan RR and Karplus PA(2002) Dimers to oligomers: Redox-sensitive oligomerization of 2-Cysteine peroxiredoxins. Biochemistry 41: 5493–5504

    Article  PubMed  CAS  Google Scholar 

  • Wood ZA, Schröder E, Harris JR and Poole LB (2003) Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci 28: 32–40

    Article  PubMed  CAS  Google Scholar 

  • Wydrzynski T, Angström J and Vännegard T (1989) H2O2 formation by photosystem II. Biochim Biophys Acta 973: 23–28

    Article  CAS  Google Scholar 

  • Yamamoto H, Miyake C, Dietz K-J, Tomizawa K, Murata N and Yokota A (1999) Thioredoxin peroxidase in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett 447: 269–273

    Article  PubMed  CAS  Google Scholar 

  • Yousef N, Pistorius EK and Michel KP (2003) Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild type and selected mutants. Arch Microbiol 180: 471– 483

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2008 Springer Science+Business Media B.V.

About this chapter

Cite this chapter

Dietz, KJ. et al. (2008). The Role of Peroxiredoxins in Oxygenic Photosynthesis of Cyanobacteria and Higher Plants: Peroxide Detoxification or Redox Sensing?. In: Demmig-Adams, B., Adams, W.W., Mattoo, A.K. (eds) Photoprotection, Photoinhibition, Gene Regulation, and Environment. Advances in Photosynthesis and Respiration, vol 21. Springer, Dordrecht. https://doi.org/10.1007/1-4020-3579-9_19

Download citation

Publish with us

Policies and ethics