• 1
    Asada, K. (1999) The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons. Annu Rev Plant Physiol Plant Mol Biol. 50, 601639.
  • 2
    Asada, K. (2006) Production and scavenging of reactive oxygen species in chloroplasts and their functions. Plant Physiol. 141, 391396.
  • 3
    Dietz, K. J., S. Jacob, M. L. Oelze, M. Laxa, V. Tognetti, S. M. De Miranda, M. Baier and I. Finkemeier (2006) The function of peroxiredoxins in plant organelle redox metabolism. J Exp Bot. 57, 16971709.
  • 4
    Heber, U. (2002) Irrungen, Wirrungen? The Mehler reaction in relation to cyclic electron transport in C3 plants. Photosynth. Res. 73, 223231.
  • 5
    Miyake, C. and A. Yokota (2000) Determination of the rate of photoreduction of O2 in the water-water cycle in watermelon leaves and enhancement of the rate by limitation of photosynthesis. Plant Cell Physiol. 41, 335343.
  • 6
    Hirotsu, N., A. Makino, A. Ushio and T. Mae (2004) Changes in the thermal dissipation and the electron flow in the water-water cycle in rice grown under conditions of physiologically low temperature. Plant Cell Physiol. 45, 635644.
  • 7
    Li, X. G., Y. P. Bi, S. J. Zhao, Q. W. Meng, Q. Zou and Q. W. He (2005) Cooperation of xanthophyll cycle with water-water cycle in the protection of photosystems 1 and 2 against inactivation during chilling stress under low irradiance. Photosynthetica 43, 261266.
  • 8
    Chen, H. X., H. Y. Gao, S. Z. An and W. J. Li (2004) Dissipation of excess energy in Mehler-peroxidase reaction in Rumex leaves during salt shock. Photosynthetica 42, 117122.
  • 9
    Makino, A., C. Miyake and A. Yokota (2002) Physiological functions of the water-water cycle (Mehler reaction) and the cyclic electron flow around PSI in rice leaves. Plant Cell Physiol. 43, 10171026.
  • 10
    Kitajima, S., K. Tomizawa, S. Shigeoka and A. Yokota (2006) An inserted loop region of stromal ascorbate peroxidase is involved in its hydrogen peroxide-mediated inactivation. FEBS J. 273, 27042710.
  • 11
    Kitajima, S., T. Shimaoka, M. Kurioka and A. Yokota (2007) Irreversible cross-linking of heme to the distal tryptophan of stromal ascorbate peroxidase in response to rapid inactivation by H2O2. FEBS J. 274, 30133020.
  • 12
    Hiner, A. N., J. N. Rodriguez-Lopez, M. B. Arnao, E. L. Raven, F. Garcia-Canovas and M. Acosta (2000) Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide. Biochem. J. 348, 321328.
  • 13
    Fox, T., G. Tsaprailis and A. M. English (1994) Fluorescence investigation of yeast cytochrome c peroxidase oxidation by hydrogen peroxide and enzyme activities of the oxidized enzyme. Biochemistry 33, 186191.
  • 14
    Tsaprailis, G. and A. M. English (2003) Different pathways of radical translocation in yeast cytochrome c peroxidase and its W191F mutant on reaction with H(2)O(2) suggest an antioxidant role. J. Biol. Inorg. Chem. 8, 248255.
  • 15
    König, J., M. Baier, F. Horling, U. Kahmann, G. Harris, P. Schürmann and K. J. Dietz (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, 57385743.
  • 16
    Wood, Z. A., L. B. Poole and P. A. Karplus (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650653.
  • 17
    Welinder, K. G. (1992) Superfamily of plant, fungal and bacterial peroxidases. Cur. Opin. Struc. Biol. 2, 388393.
  • 18
    Shigeoka, S., T. Ishikawa, M. Tamoi, Y. Miyagawa, T. Takeda, Y. Yabuta and K. Yoshimura (2002) Regulation and function of ascorbate peroxidase isoenzymes. J. Exp. Bot., 53, 13051319.
  • 19
    Mittler, R. and B. A. Zilinskas (1991) Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol. 97, 962968.
  • 20
    Preger, V., A. Pesaresi, P. Pupillo and P. Trost (2001) Ascorbate-independent electron transfer between cytochrome b561 and a 27 kDa ascorbate peroxidase of bean hypocotyls. Protoplasma, 217, 137145.
  • 21
    Ishikawa T., T. Takeda and S. Shigeoka (1996) Purification and characterization of cytosolic ascorbate peroxidase from komatsuna (Brassica rapa). Plant Sci. 120, 1118.
  • 22
    Yoshimura, K., T. Ishikawa, Y. Nakamura, M. Tamoi, T. Takeda, T. Tada, K. Nishimura and S. Shigeoka (1998) Comparative study on recombinant chloroplastic and cytosolic ascorbate peroxidase isozymes of spinach. Arch. Biochem. Biophys. 353, 5563.
  • 23
    Sano, S., M. Ueda, S. Kitajima, T. Takeda, S. Shigeoka, N. Kurano, S. Miyachi, C. Miyake and A. Yokota (2001) Characterization of ascorbate peroxidases from unicellular red alga Galdieria partita. Plant Cell Physiol. 42, 433440.
  • 24
    Chen, G. X. and K. Asada (1989) Ascorbate peroxidase in tea leaves: Occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol. 30, 987998.
  • 25
    Miyake, C., W. H. Cao and K. Asada (1993) Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol., 34, 881889.
  • 26
    Madhusudhan, R., T. Ishikawa, Y. Sawa, S. Shigeoka and H. Shibata (2003) Characterization of an ascorbate peroxidase in plastids of tobacco BY-2 cells. Physiol. Plant. 117, 550557.
  • 27
    Miyake, C. and K. Asada (1996) Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: Hydrogen peroxide decomposes compound I of ascorbate peroxidase. Plant Cell Physiol. 37, 423430.
  • 28
    Wada, K., T. Tada, Y. Nakamura, T. Ishikawa, Y. Yabuta, K. Yoshimura, S. Shigeoka and K. Nishimura (2003) Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability. J. Biochem. 134, 239244.
  • 29
    Sharp, K. H., M. Mewies, P. C. Moody and E. L. Raven (2003) Crystal structure of the ascorbate peroxidase-ascorbate complex. Nat. Struct. Biol. 10, 303307.
  • 30
    Kitajima, S., M. Kurioka, T. Yoshimoto, M. Shindo, K. Kanaori, K. Tajima and K. Oda (2008) A cysteine residue near the propionate side-chain of heme is the radical site in ascorbate peroxidase. FEBS J. 275, 470480.
  • 31
    Borisenko, G. G., I. Martin, Q. Zhao, A. A. Amoscato and V. E. Kagan (2004) Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells. J. Am. Chem. Soc. 126, 92219232.
  • 32
    Spickett, C. M., A. R. Pitt, N. Morrice and W. Kolch (2006) Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction. Biochim. Biophys. Acta 1764, 18231841.
  • 33
    Pipirou, Z., A. R. Bottrill, C. M. Metcalfe, S. C. Mistry, S. K. Badyal, B. J. Rawlings and E. L. Raven (2007) Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase. Biochemistry 46, 21742180.
  • 34
    Wright, P. J. and A. M. English (2003) Scavenging with TEMPO* to identify peptide- and protein-based radicals by mass spectrometry: Advantages of spin scavenging over spin trapping. J. Am. Chem. Soc. 125, 86558665.
  • 35
    Piontek, K., A. T. Smith and W. Blodig (2001) Lignin peroxidase structure and function. Biochem. Soc. Trans. 29, 111116.
  • 36
    Guallar, V. and B. Olsen (2006) The role of the heme propionates in heme biochemistry. J. Inorg. Biochem. 100, 755760.
  • 37
    Jakopitsch, C., C. Obinger, S. Una and A. Ivancich (2006) Identification of Trp106 as the tryptophanyl radical intermediate in Synechocystis PCC6803 catalase-peroxidase by multifrequency electron paramagnetic resonance spectroscopy. J. Inorg. Biochem. 100, 10911099.
  • 38
    Hillar, A., B. Peters, R. Pauls, A. Loboda, H. Zhang, A. G. Mauk and P. C. Loewen (2000) Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry 39, 58685875.
  • 39
    Regelsberger, G., C. Jakopitsch, F. Ruker, D. Krois, G. A. Peschek and C. Obinger (2000) Effect of distal cavity mutations on the formation of compound I in catalase-peroxidases. J. Biol. Chem. 275, 2285422861.
  • 40
    Goodin, D. B., M. G. Davidson, J. A. Roe, A. G. Mauk and M. Smith (1991) Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: Effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry 30, 49534962.
  • 41
    Edwards, S. L., R. Raag, H. Wariishi, M. H. Gold and T. L. Poulos (1993) Structure of lignin peroxidase. Proc. Natl Acad. Sci. USA 90, 750754.
  • 42
    Sundaramoorthy, M, K. Kishi, M. H. Gold and T. L. Poulos (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J. Biol. Chem. 269, 3275932767.
  • 43
    Noctor, G. and C. Foyer (1998) Ascorbate and glutathione: Keeping active oxygen under control. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 249279.
  • 44
    Passardi, F., G. Theiler, M. Zamocky, C. Cosio, N. Rouhier, F. Teixera, M. Margis-Pinheiro, V. Ioannidis, C. Penel, L. Falquet and C. Dunand. (2007) PeroxiBase: The peroxidase database. Phytochemistry, 68, 16051611.
  • 45
    Obara, K., K. Sumi and H. Fukuda (2001) The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts. Plant Cell Physiol. 43, 697705.
  • 46
    Chew, O., J. Whelan and A. H. Millar (2003) Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278, 4686946877.
  • 47
    Wood, Z. A., E. Schröder, J. Robin Harris and L. B. Poole (2003) Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28, 3240.
  • 48
    Rouhier, N. and J. P. Jacquot (2005) The plant multigenic family of thiol peroxidases. Free Radic. Biol. Med. 38, 14131421.
  • 49
    Stork, T., K. P. Michel, E. K. Pistorius and K. J. Dietz (2005) Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942 for the presence of peroxiredoxins and their transcript regulation under stress. J. Exp. Bot. 56, 31933206.
  • 50
    König, J., K. Lotte, R. Plessow, A. Brockhinke, M. Baier and K. J. Dietz (2003) Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure. J. Biol. Chem. 278, 2440924420.
  • 51
    Lamkemeyer, P., M. Laxa, V. Collin, W. Li, I. Finkemeier, M. A. Schöttler, V. Holtkamp, V. B. Tognetti, E. Issakidis-Bourguet, A. Kandlbinder, E. Weis, M. Miginiac-Maslow and K. J. Dietz (2006) Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis. Plant J. 45, 968981.
  • 52
    Pérez-Ruiz, J. M., M. C. Spínola, K. Kirchsteiger, J. Moreno, M. Sahrawy and F. J. Cejudo (2006) Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell, 18, 23562368.
  • 53
    Schröder, E., J. Littlechil, A. Lebedev, N. Errington, A. Vagin and M. Isupov (2000) Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7Å resolution. Structure, 8, 605615.
  • 54
    Chang, T. S., W. Jeong, H. Woo, S. M. Lee, S. Park and S. G. Rhee (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, 5099451001.
  • 55
    Jönsson, T. J., L. C. Johnson and W. T. Lowther (2008) Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. Nature, 451, 98101.
  • 56
    Veal, E. A., V. J. Findlay, A. M. Day, S. M. Bozonet, J. M. Evans, J. Quinn and B. A. Morgan (2004) A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. Mol. Cell 15, 129139.
  • 57
    Vivancos, A. P., E. A. Castillo, B. Biteau, C. Nicot, J. Ayté, M. B. Toledano and E. Hidalgo (2005) A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc. Natl Acad. Sci. USA 102, 88758880.
  • 58
    Rey, P., N. Bécuwe, M. B. Barrault, D. Rumeau, M. Havaux, B. Biteau and M. B. Toledano (2007) The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response. Plant J. 49, 505514.
  • 59
    Jang, H. H., K. O. Lee, Y. H. Chi, B. G. Jung, S. K. Park, J. H. Park, J. R. Lee, S. S. Lee, J. C. Moon, J. W. Yun, Y. O. Choi, W. Y. Kim, J. S. Kang, G. W. Cheong, D. J. Yun, S. G. Rhee, M. J. Cho and S. Y. Lee (2004) Two enzymes in one: Two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 117, 625635.
  • 60
    Moon, J. C., Y. S. Hah, W. Y. Kim, B. G. Jung, H. H. Jang, J. R. Lee, S. Y. Kim, Y. M. Lee, M. G. Jeon, C. W. Kim, M. J. Cho and S. Y. Lee (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, 2877528784.
  • 61
    Jang, H. H., Y. H. Chi, S. K. Park, S. S. Lee, J. R. Lee, J. H. Park, J. C. Moon, Y. M. Lee, S. Y. Kim, K. O. Lee and S. Y. Lee (2006) Structural and functional regulation of eukaryotic 2-Cys peroxiredoxins including the plant ones in cellular defense-signaling mechanisms against oxidative stress. Physiol. Plant. 126, 549559.