Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms

Tripathi BN, Bhatt I, Dietz K-J (2009)
PROTOPLASMA 235(1-4): 3-15.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Tripathi, Bhumi Nath; Bhatt, Indu; Dietz, Karl-JosefUniBi
Abstract / Bemerkung
Peroxiredoxins (Prx) are ubiquitous thiol-dependent peroxidases capable of reducing a broad range of toxic peroxides and peroxinitrites. A cysteinyl residue of peroxiredoxins reacts with the peroxides as primary catalytic center and oxidizes to sulfenic acid. The regeneration of the reduced form of Prx is required as a next step to allow its entry into next catalytic cycle. Several proteins, such as thioredoxin, glutaredoxin, cyclophilin, among others, are known to facilitate the regeneration of the reduced (catalytically active) form of Prx in plants. Based on the cysteine residues conserved in the deduced amino acid sequence and their catalytic mechanisms, four groups of peroxiredoxins have been distinguished in plants, namely, 1-Cys Prx, 2-Cys Prx, Type II Prx and Prx Q. Peroxiredoxins are known to play an important role in combating the reactive oxygen species generated at the level of electron transport activities in the plant exposed to different types of biotic and abiotic stresses. In addition to their role in antioxidant defense mechanisms in plants, they also modulate redox signaling during development and adaptation. Besides these general properties, peroxiredoxins have been shown to protect DNA from damage in vitro and in vivo. They also regulate metabolism in thylakoids and mitochondria. The present review summarizes the most updated information on the structure and catalysis of Prx and their functional importance in plant metabolism.
Hydrogen peroxides; Antioxidant; Nutrient deficiency; Oxidative stress; Peroxiredoxin; Reactive oxygen species
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Tripathi BN, Bhatt I, Dietz K-J. Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. PROTOPLASMA. 2009;235(1-4):3-15.
Tripathi, B. N., Bhatt, I., & Dietz, K. - J. (2009). Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. PROTOPLASMA, 235(1-4), 3-15.
Tripathi, Bhumi Nath, Bhatt, Indu, and Dietz, Karl-Josef. 2009. “Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms”. PROTOPLASMA 235 (1-4): 3-15.
Tripathi, B. N., Bhatt, I., and Dietz, K. - J. (2009). Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. PROTOPLASMA 235, 3-15.
Tripathi, B.N., Bhatt, I., & Dietz, K.-J., 2009. Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. PROTOPLASMA, 235(1-4), p 3-15.
B.N. Tripathi, I. Bhatt, and K.-J. Dietz, “Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms”, PROTOPLASMA, vol. 235, 2009, pp. 3-15.
Tripathi, B.N., Bhatt, I., Dietz, K.-J.: Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms. PROTOPLASMA. 235, 3-15 (2009).
Tripathi, Bhumi Nath, Bhatt, Indu, and Dietz, Karl-Josef. “Peroxiredoxins: a less studied component of hydrogen peroxide detoxification in photosynthetic organisms”. PROTOPLASMA 235.1-4 (2009): 3-15.

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Daten bereitgestellt von Europe PubMed Central.

Novel Plastid-Nuclear Genome Combinations Enhance Resistance to Citrus Canker in Cybrid Grapefruit.
Murata MM, Omar AA, Mou Z, Chase CD, Grosser JW, Graham JH., Front Plant Sci 9(), 2018
PMID: 30666259
Comparative Membrane-Associated Proteomics of Three Different Immune Reactions in Potato.
Burra DD, Lenman M, Levander F, Resjö S, Andreasson E., Int J Mol Sci 19(2), 2018
PMID: 29439444
Cytosolic and Chloroplastic DHARs Cooperate in Oxidative Stress-Driven Activation of the Salicylic Acid Pathway.
Rahantaniaina MS, Li S, Chatel-Innocenti G, Tuzet A, Issakidis-Bourguet E, Mhamdi A, Noctor G., Plant Physiol 174(2), 2017
PMID: 28381499
Interactions between 2-Cys peroxiredoxins and ascorbate in autophagosome formation during the heat stress response in Solanum lycopersicum.
Cheng F, Yin LL, Zhou J, Xia XJ, Shi K, Yu JQ, Zhou YH, Foyer CH., J Exp Bot 67(6), 2016
PMID: 26834179
Hydrogen Peroxide, Signaling in Disguise during Metal Phytotoxicity.
Cuypers A, Hendrix S, Amaral Dos Reis R, De Smet S, Deckers J, Gielen H, Jozefczak M, Loix C, Vercampt H, Vangronsveld J, Keunen E., Front Plant Sci 7(), 2016
PMID: 27199999
Selective silencing of 2Cys and type-IIB Peroxiredoxins discloses their roles in cell redox state and stress signaling.
Vidigal P, Martin-Hernandez AM, Guiu-Aragonés C, Amâncio S, Carvalho L., J Integr Plant Biol 57(6), 2015
PMID: 25319151
Functional and structural changes in plant mitochondrial PrxII F caused by NO.
Camejo D, Ortiz-Espín A, Lázaro JJ, Romero-Puertas MC, Lázaro-Payo A, Sevilla F, Jiménez A., J Proteomics 119(), 2015
PMID: 25682994
Phytotoxic metabolites from Neofusicoccum parvum, a pathogen of Botryosphaeria dieback of grapevine.
Abou-Mansour E, Débieux JL, Ramírez-Suero M, Bénard-Gellon M, Magnin-Robert M, Spagnolo A, Chong J, Farine S, Bertsch C, L'Haridon F, Serrano M, Fontaine F, Rego C, Larignon P., Phytochemistry 115(), 2015
PMID: 25747381
Label-free quantitative proteomics to investigate strawberry fruit proteome changes under controlled atmosphere and low temperature storage.
Li L, Luo Z, Huang X, Zhang L, Zhao P, Ma H, Li X, Ban Z, Liu X., J Proteomics 120(), 2015
PMID: 25753123
Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) of Arabidopsis thaliana effectively improves its peroxidase and chaperone functions.
Lee EM, Lee SS, Tripathi BN, Jung HS, Cao GP, Lee Y, Singh S, Hong SH, Lee KW, Lee SY, Cho JY, Chung BY., Ann Bot 116(4), 2015
PMID: 26141131
Fine genetic mapping of the white immature fruit color gene w to a 33.0-kb region in cucumber (Cucumis sativus L.).
Liu H, Meng H, Pan Y, Liang X, Jiao J, Li Y, Chen S, Cheng Z., Theor Appl Genet 128(12), 2015
PMID: 26239410
An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone.
An BC, Lee SS, Jung HS, Kim JY, Lee Y, Lee KW, Lee SY, Tripathi BN, Chung BY., FEBS Lett 589(19 pt b), 2015
PMID: 26278368
Antioxidative and proteolytic systems protect mitochondria from oxidative damage in S-deficient Arabidopsis thaliana.
Ostaszewska-Bugajska M, Rychter AM, Juszczuk IM., J Plant Physiol 186-187(), 2015
PMID: 26339750
The roles of reactive oxygen metabolism in drought: not so cut and dried.
Noctor G, Mhamdi A, Foyer CH., Plant Physiol 164(4), 2014
PMID: 24715539
Extracellular proteome analysis of Leptospira interrogans serovar Lai.
Zeng L, Zhang Y, Zhu Y, Yin H, Zhuang X, Zhu W, Guo X, Qin J., OMICS 17(10), 2013
PMID: 23895271
Oxidative protein-folding systems in plant cells.
Onda Y., Int J Cell Biol 2013(), 2013
PMID: 24187554
Phytoextraction of toxic metals: a central role for glutathione.
Seth CS, Remans T, Keunen E, Jozefczak M, Gielen H, Opdenakker K, Weyens N, Vangronsveld J, Cuypers A., Plant Cell Environ 35(2), 2012
PMID: 21486307
Glutathione in plants: an integrated overview.
Noctor G, Mhamdi A, Chaouch S, Han Y, Neukermans J, Marquez-Garcia B, Queval G, Foyer CH., Plant Cell Environ 35(2), 2012
PMID: 21777251
Multiple strategies to prevent oxidative stress in Arabidopsis plants lacking the malate valve enzyme NADP-malate dehydrogenase.
Hebbelmann I, Selinski J, Wehmeyer C, Goss T, Voss I, Mulo P, Kangasjärvi S, Aro EM, Oelze ML, Dietz KJ, Nunes-Nesi A, Do PT, Fernie AR, Talla SK, Raghavendra AS, Linke V, Scheibe R., J Exp Bot 63(3), 2012
PMID: 22140244
The biology of reactive sulfur species (RSS).
Gruhlke MC, Slusarenko AJ., Plant Physiol Biochem 59(), 2012
PMID: 22541352
Effect of calcium and potassium on antioxidant system of Vicia faba L. Under cadmium stress.
Siddiqui MH, Al-Whaibi MH, Sakran AM, Basalah MO, Ali HM., Int J Mol Sci 13(6), 2012
PMID: 22837652
Understanding the mechanisms of chilling injury in bell pepper fruits using the proteomic approach.
Sánchez-Bel P, Egea I, Sánchez-Ballesta MT, Martinez-Madrid C, Fernandez-Garcia N, Romojaro F, Olmos E, Estrella E, Bolarín MC, Flores FB., J Proteomics 75(17), 2012
PMID: 22796354
Expression of ROS-responsive genes and transcription factors after metabolic formation of H(2)O(2) in chloroplasts.
Balazadeh S, Jaspert N, Arif M, Mueller-Roeber B, Maurino VG., Front Plant Sci 3(), 2012
PMID: 23125844
Tolerance to oxidative stress induced by desiccation in Porphyra columbina (Bangiales, Rhodophyta).
Contreras-Porcia L, Thomas D, Flores V, Correa JA., J Exp Bot 62(6), 2011
PMID: 21196477
Comparative metagenomics of microbial traits within oceanic viral communities.
Sharon I, Battchikova N, Aro EM, Giglione C, Meinnel T, Glaser F, Pinter RY, Breitbart M, Rohwer F, Béjà O., ISME J 5(7), 2011
PMID: 21307954
Unravelling the regulatory function of FurA in Anabaena sp. PCC 7120 through 2-D DIGE proteomic analysis.
González A, Bes MT, Peleato ML, Fillat MF., J Proteomics 74(5), 2011
PMID: 21315197
Response of mitochondrial thioredoxin PsTrxo1, antioxidant enzymes, and respiration to salinity in pea (Pisum sativum L.) leaves.
Martí MC, Florez-Sarasa I, Camejo D, Ribas-Carbó M, Lázaro JJ, Sevilla F, Jiménez A., J Exp Bot 62(11), 2011
PMID: 21460385
Peroxiredoxins and NADPH-dependent thioredoxin systems in the model legume Lotus japonicus.
Tovar-Méndez A, Matamoros MA, Bustos-Sanmamed P, Dietz KJ, Cejudo FJ, Rouhier N, Sato S, Tabata S, Becana M., Plant Physiol 156(3), 2011
PMID: 21562331
Proteome analysis of Fusarium infection in emmer grains (Triticum dicoccum)
Eggert K, Zörb C, Mühling KH, Pawelzik E., Plant Pathol 60(5), 2011
PMID: IND44682812
Oxidative protein folding: selective pressure for prolamin evolution in rice.
Onda Y, Kawagoe Y., Plant Signal Behav 6(12), 2011
PMID: 22112460
Proline improves copper tolerance in chickpea (Cicer arietinum).
Singh V, Bhatt I, Aggarwal A, Tripathi BN, Munjal AK, Sharma V., Protoplasma 245(1-4), 2010
PMID: 20625778

93 References

Daten bereitgestellt von Europe PubMed Central.

K, Philos Trans R Soc 355(), 2000
Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide.
Banmeyer I, Marchand C, Clippe A, Knoops B., FEBS Lett. 579(11), 2005
PMID: 15848167

S, Acta Crystall F 62(), 2006
Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.
Barranco-Medina S, Krell T, Finkemeier I, Sevilla F, Lazaro JJ, Dietz KJ., Plant Physiol. Biochem. 45(10-11), 2007
PMID: 17881238
Thermodynamics of the dimer-decamer transition of reduced human and plant 2-cys peroxiredoxin.
Barranco-Medina S, Kakorin S, Lazaro JJ, Dietz KJ., Biochemistry 47(27), 2008
PMID: 18553980

T, AF076920). Plant Physiol Plant Gene Reg 118(), 1998
Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae.
Chae HZ, Kim IH, Kim K, Rhee SG., J. Biol. Chem. 268(22), 1993
PMID: 8344960
Thioredoxin-dependent peroxide reductase from yeast.
Chae HZ, Chung SJ, Rhee SG., J. Biol. Chem. 269(44), 1994
PMID: 7961686
Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin.
Chae HZ, Kang SW, Rhee SG., Meth. Enzymol. 300(), 1999
PMID: 9919524
Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage.
Cheong NE, Choi YO, Lee KO, Kim WY, Jung BG, Chi YH, Jeong JS, Kim K, Cho MJ, Lee SY., Plant Mol. Biol. 40(5), 1999
PMID: 10487217
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE., Nat. Struct. Biol. 5(5), 1998
PMID: 9587003
Cloning and expression of a new isotype of the peroxiredoxin gene of Chinese cabbage and its comparison to 2Cys-peroxiredoxin isolated from the same plant.
Choi YO, Cheong NE, Lee KO, Jung BG, Hong CH, Jeong JH, Chi YH, Kim K, Cho MJ, Lee SY., Biochem. Biophys. Res. Commun. 258(3), 1999
PMID: 10329461
The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity.
Collin V, Issakidis-Bourguet E, Marchand C, Hirasawa M, Lancelin JM, Knaff DB, Miginiac-Maslow M., J. Biol. Chem. 278(26), 2003
PMID: 12707279
Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type.
Collin V, Lamkemeyer P, Miginiac-Maslow M, Hirasawa M, Knaff DB, Dietz KJ, Issakidis-Bourguet E., Plant Physiol. 136(4), 2004
PMID: 15531707
Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution.
Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B., J. Mol. Biol. 311(4), 2001
PMID: 11518528
Plant peroxiredoxins.
Dietz KJ., Annu Rev Plant Biol 54(), 2003
PMID: 14502986
The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation.
Dietz KJ, Horling F, Konig J, Baier M., J. Exp. Bot. 53(372), 2002
PMID: 11997378

K-J, 2005
The function of peroxiredoxins in plant organelle redox metabolism.
Dietz KJ, Jacob S, Oelze ML, Laxa M, Tognetti V, de Miranda SM, Baier M, Finkemeier I., J. Exp. Bot. 57(8), 2006
PMID: 16606633
The lipoxygenase pathway.
Feussner I, Wasternack C., Annu Rev Plant Biol 53(), 2002
PMID: 12221977
The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress.
Finkemeier I, Goodman M, Lamkemeyer P, Kandlbinder A, Sweetlove LJ, Dietz KJ., J. Biol. Chem. 280(13), 2005
PMID: 15632145
The mitochondrial type II peroxiredoxin from poplar
Gama F, Keech O, Eymery F, Finkemeier I, Gelhaye E, Gardestrom P, Dietz KJ, Rey P, Jacquot JP, Rouhier N., Physiol Plant 129(1), 2007
PMID: IND43860515

Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii.
Goyer A, Haslekas C, Miginiac-Maslow M, Klein U, Le Marechal P, Jacquot JP, Decottignies P., Eur. J. Biochem. 269(1), 2002
PMID: 11784321
The expression of a peroxiredoxin antioxidant gene, AtPer1, in Arabidopsis thaliana is seed-specific and related to dormancy.
Haslekas C, Stacy RA, Nygaard V, Culianez-Macia FA, Aalen RB., Plant Mol. Biol. 36(6), 1998
PMID: 9580097

S, Proc Natl Acad Sci USA 96(), 1999
Hofmann B, Hecht HJ, Flohe L., Biol. Chem. 383(3-4), 2002
PMID: 12033427

F, Plant Physiol Biochem 40(), 2002
Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis.
Horling F, Lamkemeyer P, Konig J, Finkemeier I, Kandlbinder A, Baier M, Dietz KJ., Plant Physiol. 131(1), 2003
PMID: 12529539
Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803.
Hosoya-Matsuda N, Motohashi K, Yoshimura H, Nozaki A, Inoue K, Ohmori M, Hisabori T., J. Biol. Chem. 280(1), 2004
PMID: 15509585

J, J Exp Bot 44(), 1993
A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress.
Kiba A, Nishihara M, Tsukatani N, Nakatsuka T, Kato Y, Yamamura S., Plant Cell Physiol. 46(6), 2005
PMID: 15840643

B, Physiol Plant 104(), 1998
Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.
Knoops B, Clippe A, Bogard C, Arsalane K, Wattiez R, Hermans C, Duconseille E, Falmagne P, Bernard A., J. Biol. Chem. 274(43), 1999
PMID: 10521424
Response to oxidative stress involves a novel peroxiredoxin gene in the unicellular cyanobacterium Synechocystis sp. PCC 6803.
Kobayashi M, Ishizuka T, Katayama M, Kanehisa M, Bhattacharyya-Pakrasi M, Pakrasi HB, Ikeuchi M., Plant Cell Physiol. 45(3), 2004
PMID: 15047877

J, Proc Natl Acad Sci USA 99(), 2002
Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.
Konig J, Lotte K, Plessow R, Brockhinke A, Baier M, Dietz KJ., J. Biol. Chem. 278(27), 2003
PMID: 12702727
Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis.
Lamkemeyer P, Laxa M, Collin V, Li W, Finkemeier I, Schottler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, Miginiac-Maslow M, Dietz KJ., Plant J. 45(6), 2006
PMID: 16507087
Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.
Lee SP, Hwang YS, Kim YJ, Kwon KS, Kim HJ, Kim K, Chae HZ., J. Biol. Chem. 276(32), 2001
PMID: 11390385

K, Proc Natl Acad Sci USA 98(), 2001

B, Proteomics 21(), 2007
Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
Navrot N, Collin V, Gualberto J, Gelhaye E, Hirasawa M, Rey P, Knaff DB, Issakidis E, Jacquot JP, Rouhier N., Plant Physiol. 142(4), 2006
PMID: 17071643

G, Philos Trans R Soc Lond Ser B 355(), 2000
Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity.
Pedrajas JR, Miranda-Vizuete A, Javanmardy N, Gustafsson JA, Spyrou G., J. Biol. Chem. 275(21), 2000
PMID: 10821871
Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage.
Perez-Ruiz JM, Spinola MC, Kirchsteiger K, Moreno J, Sahrawy M, Cejudo FJ., Plant Cell 18(9), 2006
PMID: 16891402
The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome.
Petersson UA, Kieselbach T, Garcia-Cerdan JG, Schroder WP., FEBS Lett. 580(26), 2006
PMID: 17054949
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, Lunardi J., J. Biol. Chem. 277(22), 2002
PMID: 11904290
The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.
Rey P, Becuwe N, Barrault MB, Rumeau D, Havaux M, Biteau B, Toledano MB., Plant J. 49(3), 2007
PMID: 17217469
S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
Romero-Puertas MC, Laxa M, Matte A, Zaninotto F, Finkemeier I, Jones AM, Perazzolli M, Vandelle E, Dietz KJ, Delledonne M., Plant Cell 19(12), 2007
PMID: 18165327
Plant peroxiredoxins: alternative hydroperoxide scavenging enzymes.
Rouhier N, Jacquot JP., Photosyn. Res. 74(3), 2002
PMID: 16245137
Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.
Rouhier N, Gelhaye E, Gualberto JM, Jordy MN, De Fay E, Hirasawa M, Duplessis S, Lemaire SD, Frey P, Martin F, Manieri W, Knaff DB, Jacquot JP., Plant Physiol. 134(3), 2004
PMID: 14976238
Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution.
Schroder E, Littlechild JA, Lebedev AA, Errington N, Vagin AA, Isupov MN., Structure 8(6), 2000
PMID: 10873855

R, Mol Microbiol 151(), 2005
Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate.
Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG., J. Biol. Chem. 275(27), 2000
PMID: 10751410
Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts.
Shikanai T, Takeda T, Yamauchi H, Sano S, Tomizawa KI, Yokota A, Shigeoka S., FEBS Lett. 428(1-2), 1998
PMID: 9645472

R, Proc Natl Acad Sci USA 101(), 2004
Signs of oxidative stress in the chlorotic leaves of iron starved plants.
Tewari RK, Kumar P, Neetu , Sharma PN., Plant Sci. 169(6), 2005
PMID: IND43762711
Oxidative stress in Scenedesmus sp. during short- and long-term exposure to Cu2+ and Zn2+.
Tripathi BN, Mehta SK, Amar A, Gaur JP., Chemosphere 62(4), 2005
PMID: 16084572
In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family.
Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y., J. Biol. Chem. 274(28), 1999
PMID: 10391912
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.
Wood ZA, Poole LB, Karplus PA., Science 300(5619), 2003
PMID: 12714747
Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803.
Yamamoto H, Miyake C, Dietz KJ, Tomizawa K, Murata N, Yokota A., FEBS Lett. 447(2-3), 1999
PMID: 10214959
Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis.
Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY., Biochem. Biophys. Res. Commun. 268(3), 2000
PMID: 10679306

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