Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure

König J, Lotte K, Plessow R, Brockhinke A, Baier M, Dietz K-J (2003)

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König, JanineUniBi; Lotte, Kirsten; Plessow, Regina; Brockhinke, AndreasUniBi; Baier, Margarete; Dietz, Karl-JosefUniBi
Abstract / Bemerkung
Barley 2-cysteine peroxiredoxin (2-Cys Prx) was analyzed for peroxide reduction, quaternary structure, thylakoid attachment, and function as well as in vivo occurrence of the inactivated form, with emphasis on the role of specific amino acid residues. Data presented show the following. 1) 2-Cys Prx has a broad substrate specificity and reduces even complex lipid peroxides such as phosphatidylcholine dilineoyl hydroperoxide, although at low rates. 2) 2-Cys Prx partly becomes irreversibly oxidized by peroxide substrates during the catalytic cycle in a concentration-dependent manner, particularly by bulky hydroperoxides. 3) Using dithiothreitol and thioredoxin (Trx) as reductants, amino acids were identified that are important for peroxide reduction (Cys(64), Arg(140), and Arg(163)), regeneration by Trx (Cys(185)), and conformation changes from dimer to oligomer (Thr(66), Trp(99), and Trp(189)). 4) Oligomerization decreased the rate of Trx-dependent peroxide detoxification. 5) Comparison of Prx(WT), W99L, and W189L using static and time-resolved LIF techniques demonstrated the contributions of the tryptophan residues and yielded information about their local environment. Data indicated protein dynamics in the catalytic site and the carboxyl terminus during the reduction-oxidation cycle. 6) Reduced and inactivated barley 2-Cys Prx oligomerized and attached to the thylakoid membrane in isolated chloroplasts. The in vivo relevance of inactivation was shown in leaves subjected to cold and wilting stress and during senescence. Based on these results, it is hypothesized that in addition to its function in peroxide detoxification, 2-Cys Prx may play a role as a structural redox sensor in chloroplasts.
Peroxiredoxins Plant Proteins/chemistry/genetics/metabolism Peroxidases/*chemistry/genetics/metabolism Oxidation-Reduction Molecular Sequence Data Hordeum Chloroplasts/metabolism Amino Acid Sequence Catalytic Domain Protein Conformation Sequence Alignment Substrate Specificity
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König J, Lotte K, Plessow R, Brockhinke A, Baier M, Dietz K-J. Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(27):24409-24420.
König, J., Lotte, K., Plessow, R., Brockhinke, A., Baier, M., & Dietz, K. - J. (2003). Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(27), 24409-24420.
König, J., Lotte, K., Plessow, R., Brockhinke, A., Baier, M., and Dietz, K. - J. (2003). Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure. JOURNAL OF BIOLOGICAL CHEMISTRY 278, 24409-24420.
König, J., et al., 2003. Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(27), p 24409-24420.
J. König, et al., “Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, 2003, pp. 24409-24420.
König, J., Lotte, K., Plessow, R., Brockhinke, A., Baier, M., Dietz, K.-J.: Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure. JOURNAL OF BIOLOGICAL CHEMISTRY. 278, 24409-24420 (2003).
König, Janine, Lotte, Kirsten, Plessow, Regina, Brockhinke, Andreas, Baier, Margarete, and Dietz, Karl-Josef. “Reaction mechanism of plant 2-Cys peroxiredoxin - Role of the C terminus and the quaternary structure”. JOURNAL OF BIOLOGICAL CHEMISTRY 278.27 (2003): 24409-24420.

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Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.
Nelson KJ, Perkins A, Van Swearingen AED, Hartman S, Brereton AE, Parsonage D, Salsbury FR, Karplus PA, Poole LB., Antioxid Redox Signal 28(7), 2018
PMID: 28375740
Peroxiredoxins and Redox Signaling in Plants.
Liebthal M, Maynard D, Dietz KJ., Antioxid Redox Signal 28(7), 2018
PMID: 28594234
Expression of OsTPX Gene Improves Cellular Redox Homeostasis and Photosynthesis Efficiency in Synechococcus elongatus PCC 7942.
Kim YS, Kim JJ, Park SI, Diamond S, Boyd JS, Taton A, Kim IS, Golden JW, Yoon HS., Front Plant Sci 9(), 2018
PMID: 30619416
Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus.
Singh A, Kumar N, Tomar PPS, Bhose S, Ghosh DK, Roy P, Sharma AK., Protoplasma 254(4), 2017
PMID: 27987036
Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.
Carvalho LAC, Truzzi DR, Fallani TS, Alves SV, Toledo JC, Augusto O, Netto LES, Meotti FC., J Biol Chem 292(21), 2017
PMID: 28348082
Molecular cloning, expression and antioxidative activity of 2-cys-peroxiredoxin from freshwater mussel Cristaria plicata.
Wang X, Hu B, Wen C, Zhang M, Jian S, Yang G., Fish Shellfish Immunol 66(), 2017
PMID: 28499967
Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation.
Poynton RA, Peskin AV, Haynes AC, Lowther WT, Hampton MB, Winterbourn CC., Biochem J 473(4), 2016
PMID: 26614766
Plant protein 2-Cys peroxiredoxin TaBAS1 alleviates oxidative and nitrosative stresses incurred during cryopreservation of mammalian cells.
Chow-Shi-Yée M, Grondin M, Averill-Bates DA, Ouellet F., Biotechnol Bioeng 113(7), 2016
PMID: 26724792
Characterization of the Arabidopsis thaliana 2-Cys peroxiredoxin interactome.
Cerveau D, Kraut A, Stotz HU, Mueller MJ, Couté Y, Rey P., Plant Sci 252(), 2016
PMID: 27717466
Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.
Tairum CA, Santos MC, Breyer CA, Geyer RR, Nieves CJ, Portillo-Ledesma S, Ferrer-Sueta G, Toledo JC, Toyama MH, Augusto O, Netto LE, de Oliveira MA., Sci Rep 6(), 2016
PMID: 27629822
Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC.
Parsonage D, Nelson KJ, Ferrer-Sueta G, Alley S, Karplus PA, Furdui CM, Poole LB., Biochemistry 54(7), 2015
PMID: 25633283
Molecular characterization and functional analysis of a peroxiredoxin 1 cDNA from golden pompano (Trachinotus ovatus).
Wang L, Guo H, Zhang N, Ma Z, Jiang S, Zhang D., Dev Comp Immunol 51(2), 2015
PMID: 25889122
Phototropins maintain robust circadian oscillation of PSII operating efficiency under blue light.
Litthauer S, Battle MW, Lawson T, Jones MA., Plant J 83(6), 2015
PMID: 26215041
In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.
Noichri Y, Palais G, Ruby V, D'Autreaux B, Delaunay-Moisan A, Nyström T, Molin M, Toledano MB., Redox Biol 6(), 2015
PMID: 26335398
Peroxiredoxins as biomarkers of oxidative stress.
Poynton RA, Hampton MB., Biochim Biophys Acta 1840(2), 2014
PMID: 23939310
Molecular characterization and expression analysis of a peroxiredoxin 1 cDNA from Korean rose bitterling (Rhodeus uyekii).
Cho HK, Kong HJ, Moon JY, Kim JD, Kim DG, Kim WJ, Nam BH, Kim YO, Kim HS, An CM, Kim BS., Mol Biol Rep 41(4), 2014
PMID: 24420863
Identification and functional analysis of peroxiredoxin isoforms in Euglena gracilis.
Tamaki S, Maruta T, Sawa Y, Shigeoka S, Ishikawa T., Biosci Biotechnol Biochem 78(4), 2014
PMID: 25036955
Thioredoxin reductase type C (NTRC) orchestrates enhanced thermotolerance to Arabidopsis by its redox-dependent holdase chaperone function.
Chae HB, Moon JC, Shin MR, Chi YH, Jung YJ, Lee SY, Nawkar GM, Jung HS, Hyun JK, Kim WY, Kang CH, Yun DJ, Lee KO, Lee SY., Mol Plant 6(2), 2013
PMID: 23024205
The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.
König J, Galliardt H, Jütte P, Schäper S, Dittmann L, Dietz KJ., J Exp Bot 64(11), 2013
PMID: 23828546
Hydroperoxide and peroxynitrite reductase activity of poplar thioredoxin-dependent glutathione peroxidase 5: kinetics, catalytic mechanism and oxidative inactivation.
Selles B, Hugo M, Trujillo M, Srivastava V, Wingsle G, Jacquot JP, Radi R, Rouhier N., Biochem J 442(2), 2012
PMID: 22122405
Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin.
Tairum CA, de Oliveira MA, Horta BB, Zara FJ, Netto LE., J Mol Biol 424(1-2), 2012
PMID: 22985967
Chloroplast NADPH-dependent thioredoxin reductase from Chlorella vulgaris alleviates environmental stresses in yeast together with 2-Cys peroxiredoxin.
Machida T, Ishibashi A, Kirino A, Sato J, Kawasaki S, Niimura Y, Honjoh K, Miyamoto T., PLoS One 7(9), 2012
PMID: 23029353
A comparison of thiol peroxidase mechanisms.
Flohé L, Toppo S, Cozza G, Ursini F., Antioxid Redox Signal 15(3), 2011
PMID: 20649470
Antitumor quinol PMX464 is a cytocidal anti-trypanosomal inhibitor targeting trypanothione metabolism.
König J, Wyllie S, Wells G, Stevens MF, Wyatt PG, Fairlamb AH., J Biol Chem 286(10), 2011
PMID: 21212280
Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study.
Nagy P, Karton A, Betz A, Peskin AV, Pace P, O'Reilly RJ, Hampton MB, Radom L, Winterbourn CC., J Biol Chem 286(20), 2011
PMID: 21385867
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin.
Aran M, Ferrero D, Wolosiuk A, Mora-García S, Wolosiuk RA., J Biol Chem 286(26), 2011
PMID: 21525006
Peroxiredoxins in plants and cyanobacteria.
Dietz KJ., Antioxid Redox Signal 15(4), 2011
PMID: 21194355
Regulatory subunit B'gamma of protein phosphatase 2A prevents unnecessary defense reactions under low light in Arabidopsis.
Trotta A, Wrzaczek M, Scharte J, Tikkanen M, Konert G, Rahikainen M, Holmström M, Hiltunen HM, Rips S, Sipari N, Mulo P, Weis E, von Schaewen A, Aro EM, Kangasjärvi S., Plant Physiol 156(3), 2011
PMID: 21571669
Characterisation of 2-Cys peroxiredoxin isozyme (Prx1) from Taiwanofungus camphorata (Niu-chang-chih): Expression and enzyme properties
Liau Yi-Jen, Chen Yu-Ting, Lin Choa-Yi, Huang Jenq-Kuen, Lin Chi-Tsai., Food Chem 119(1), 2010
PMID: IND44277177
Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: catalytic mechanism and high reactivity.
Horta BB, de Oliveira MA, Discola KF, Cussiol JR, Netto LE., J Biol Chem 285(21), 2010
PMID: 20335172
Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts.
Pulido P, Spínola MC, Kirchsteiger K, Guinea M, Pascual MB, Sahrawy M, Sandalio LM, Dietz KJ, González M, Cejudo FJ., J Exp Bot 61(14), 2010
PMID: 20616155
Dynamic translocation of ligand-complexed DNA through solid-state nanopores with optical tweezers.
Sischka A, Spiering A, Khaksar M, Laxa M, König J, Dietz KJ, Anselmetti D., J Phys Condens Matter 22(45), 2010
PMID: 21339608
Typical 2-Cys peroxiredoxins--modulation by covalent transformations and noncovalent interactions.
Aran M, Ferrero DS, Pagano E, Wolosiuk RA., FEBS J 276(9), 2009
PMID: 19476489
The quaternary structure of NADPH thioredoxin reductase C is redox-sensitive.
Pérez-Ruiz JM, González M, Spínola MC, Sandalio LM, Cejudo FJ., Mol Plant 2(3), 2009
PMID: 19825629
Genetic variation and drought response in two Populus x euramericana genotypes through 2-DE proteomic analysis of leaves from field and glasshouse cultivated plants.
Bonhomme L, Monclus R, Vincent D, Carpin S, Claverol S, Lomenech AM, Labas V, Plomion C, Brignolas F, Morabito D., Phytochemistry 70(8), 2009
PMID: 19560791
The oligomeric conformation of peroxiredoxins links redox state to function.
Barranco-Medina S, Lázaro JJ, Dietz KJ., FEBS Lett 583(12), 2009
PMID: 19464293
Multiple redox and non-redox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast.
Muthuramalingam M, Seidel T, Laxa M, Nunes de Miranda SM, Gärtner F, Ströher E, Kandlbinder A, Dietz KJ., Mol Plant 2(6), 2009
PMID: 19995730
Generation of superoxide anion in chloroplasts of Arabidopsis thaliana during active photosynthesis: a focus on rapidly induced genes.
Scarpeci TE, Zanor MI, Carrillo N, Mueller-Roeber B, Valle EM., Plant Mol Biol 66(4), 2008
PMID: 18158584
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin.
Parsonage D, Karplus PA, Poole LB., Proc Natl Acad Sci U S A 105(24), 2008
PMID: 18165315
ATP-dependent modulation and autophosphorylation of rapeseed 2-Cys peroxiredoxin.
Aran M, Caporaletti D, Senn AM, Tellez de Iñon MT, Girotti MR, Llera AS, Wolosiuk RA., FEBS J 275(7), 2008
PMID: 18279387
The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii.
Dayer R, Fischer BB, Eggen RI, Lemaire SD., Genetics 179(1), 2008
PMID: 18493039
NTRC new ways of using NADPH in the chloroplast.
Spínola MC, Pérez-Ruiz JM, Pulido P, Kirchsteiger K, Guinea M, González M, Cejudo FJ., Physiol Plant 133(3), 2008
PMID: 18346073
The ferredoxin/thioredoxin system of oxygenic photosynthesis.
Schürmann P, Buchanan BB., Antioxid Redox Signal 10(7), 2008
PMID: 18377232
Redox signal integration: from stimulus to networks and genes.
Dietz KJ., Physiol Plant 133(3), 2008
PMID: 18429942
NTRC new ways of using NADPH in the chloroplast
Spínola MC, Pérez-Ruiz JM, Pulido P, Kirchsteiger K, Guinea M, González M, Cejudo FJ., Physiol Plant 133(3), 2008
PMID: IND44069757
The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.
Rey P, Bécuwe N, Barrault MB, Rumeau D, Havaux M, Biteau B, Toledano MB., Plant J 49(3), 2007
PMID: 17217469
The redox imbalanced mutants of Arabidopsis differentiate signaling pathways for redox regulation of chloroplast antioxidant enzymes.
Heiber I, Ströher E, Raatz B, Busse I, Kahmann U, Bevan MW, Dietz KJ, Baier M., Plant Physiol 143(4), 2007
PMID: 17337533
Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers.
Herbette S, Roeckel-Drevet P, Drevet JR., FEBS J 274(9), 2007
PMID: 17419737
Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.
Barranco-Medina S, Krell T, Finkemeier I, Sevilla F, Lázaro JJ, Dietz KJ., Plant Physiol Biochem 45(10-11), 2007
PMID: 17881238
Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii.
Naumann B, Busch A, Allmer J, Ostendorf E, Zeller M, Kirchhoff H, Hippler M., Proteomics 7(21), 2007
PMID: 17922516
S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
Romero-Puertas MC, Laxa M, Mattè A, Zaninotto F, Finkemeier I, Jones AM, Perazzolli M, Vandelle E, Dietz KJ, Delledonne M., Plant Cell 19(12), 2007
PMID: 18165327
The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts.
Peltier JB, Cai Y, Sun Q, Zabrouskov V, Giacomelli L, Rudella A, Ytterberg AJ, Rutschow H, van Wijk KJ., Mol Cell Proteomics 5(1), 2006
PMID: 16207701
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, Schöttler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, Miginiac-Maslow M, Dietz KJ., Plant J 45(6), 2006
PMID: 16507087
Molecular and functional characterization of sulfiredoxin homologs from higher plants.
Liu XP, Liu XY, Zhang J, Xia ZL, Liu X, Qin HJ, Wang DW., Cell Res 16(3), 2006
PMID: 16541127
Structural and functional regulation of eukaryotic 2-Cys peroxiredoxins including the plant ones in cellular defense-signaling mechanisms against oxidative stress.
Jang HoHee, Chi YongHun, Park SooKwon, Lee SeungSik, Lee JungRo, Park JinHo, Moon JeongChan, Lee YoungMee, Kim SunYoung, Lee KyunOh, Lee SangYeol., Physiol Plant 126(4), 2006
PMID: IND43792494
Plant thioredoxins are key actors in the oxidative stress response.
Vieira Dos Santos C, Rey P., Trends Plant Sci 11(7), 2006
PMID: 16782394
Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum.
Barranco-Medina S, López-Jaramillo FJ, Bernier-Villamor L, Sevilla F, Lázaro JJ., Acta Crystallogr Sect F Struct Biol Cryst Commun 62(pt 7), 2006
PMID: 16820697
The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an electron donor to 2-Cys peroxiredoxins in chloroplasts.
Moon JC, Jang HH, Chae HB, Lee JR, Lee SY, Jung YJ, Shin MR, Lim HS, Chung WS, Yun DJ, Lee KO, Lee SY., Biochem Biophys Res Commun 348(2), 2006
PMID: 16884685
Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage.
Pérez-Ruiz JM, Spínola MC, Kirchsteiger K, Moreno J, Sahrawy M, Cejudo FJ., Plant Cell 18(9), 2006
PMID: 16891402
The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature.
Goulas E, Schubert M, Kieselbach T, Kleczkowski LA, Gardeström P, Schröder W, Hurry V., Plant J 47(5), 2006
PMID: 16923014
Protein-protein interactions within peroxiredoxin systems.
Noguera-Mazon V, Krimm I, Walker O, Lancelin JM., Photosynth Res 89(2-3), 2006
PMID: 17089212
Protein sulfenic acids in redox signaling.
Poole LB, Karplus PA, Claiborne A., Annu Rev Pharmacol Toxicol 44(), 2004
PMID: 14744249
Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.
Rouhier N, Gelhaye E, Corbier C, Jacquot JP., Physiol Plant 120(1), 2004
PMID: 15032877
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
Vitamin E is essential for seed longevity and for preventing lipid peroxidation during germination.
Sattler SE, Gilliland LU, Magallanes-Lundback M, Pollard M, DellaPenna D., Plant Cell 16(6), 2004
PMID: 15155886


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