Abstract
We have surveyed the early biochemical, structural and enzymatic studies on the peroxiredoxin family, within the broad context of the other chapters included within this book. Both the antioxidant defence and peroxide-linked cell signalling roles of the peroxiredoxins are introduced. The possible membrane-association of certain peroxiredoxins is assessed and the structural characterization of the peroxiredoxins by electron microscopy is given some emphasis here. The important contribution of X-ray crystallographic studies to the understanding of peroxiredoxin structure is given due attention. Finally, some medical perpectives are introduced, with emphasis upon the understanding of the microbial peroxiredoxins as possible future drug targets
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References
Allen, D.W., Cadman, S., 1979, Calcium-induced erythrocyte membrane changes. The role of adsorption of cytosol proteins and proteases. Biochim. Biophys. Acta 551: 1–9.
Aslan, M., Ozben, T., 2003, Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid. Redox Signal 5: 781–788.
Baker, L.M., Poole, L.B., 2003, Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. J. Biol. Chem. 278: 9203–9211.
Baker, L.M, Raudonikiene, A., Hoffman, P.S., Poole, L.B., 2001, Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183: 1961–1973.
Banning, A., Deubel, S., Kluth, D., Zhou, Z., Brigelius-Flohé, R., 2005, The GI-GPx gene is a target for Nrf2. Mol. Cell. Biol. 25: 4914–4923.
Becker, K., Rahlfs, S., Nickel, C., Schirmer, R.H., 2003, Glutathione–functions and metabolism in the malarial parasite Plasmodium falciparum. Biol. Chem. 384: 551–566.
Bozonet, S.M, Findlay, V.J., Day, A.M., Cameron, J., Veal, E.A., 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.
Brigelius-Flohé, R., Banning, A., Kny, M., Bol, G.F., 2004, Redox events in interleukin-1 signaling. Arch. Biochem. Biophys. 423: 66–73.
Brigelius, R., 1985, Mixed didulfides: biological functions and increase in oxidative Stress. Academic Press, London, Orlando, San Diego, New York, Toronto, Montreal, Sydney, Tokyo.
Bryk, R., Griffin, P., Nathan, C., 2000, Peroxynitrite reductase activity of bacterial perioxiredoxins. Nature 407: 211–215.
Bryk, R., Lime, C.D., Erdjument-Bromage, H., Tempst, P., Nathan, C., 2002. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295: 1073–1077
Budde, H., Flohé, L., Hecht, H.-J., Hofmann, B., Stehr, M., Wissing, J., Lûnsdorf, H., 2003, Kinetics and redox-sensitive oligomerization reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol. Chem. 384: 619–633.
Cao, Z., Roszak, A.W., Gourlay, L.J., Lindsay, J.G., Isaacs N.W., 2005, Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure 13: 1661–1664.
Carnieri, E.G., Moreno, S.N., Docampo, R., 1993, Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages. Mol. Biochem. Parasitol. 61: 79–86.
Castro, H., Sousa, C., Santos, M., Cordeiro-da-Silva, A., Flohé, L., Tomas, A.M., 2002, Complementary antioxidant defence by cytoplasmic and mitochondrial peroxiredoxins in Leishmania infantum. Free Radic. Biol. Med. 33: 1552–1562.
Cha, M.-K., Kim, I.-H., 1995, Thioredoxin-linked peroxidase from human red blood cell: Evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem. Biophys. Res. Commun. 217: 900–907.
Cha, M-K., Yin, C.-H. Kim, I.-H., 2000, Interaction of human thiol-specific antioxidant protein I with erythrocyte plasma membrane. Biochemistry 39: 6944–6950.
Chae, H.Z, Chung, S,J., Rhee, S.G., 1994a, Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269: 27670–27678.
Chae, H.Z., Rhee, S.G., 1994, A thiol-specific antioxidant and sequence homology to various proteins of unknown function. Biofactors 4: 177–180.
Chae, H.Z., Uhm, T.B., Rhee, S.G., 1994c, Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl. Acad.Sci. USA 91: 7022–7026.
Chae, H.Z., Kim, I.H., Kim, K., Rhee, S.G., 1993, Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J. Biol. Chem. 268: 16815–16821.
Chae, H.Z., Robison, K,. Poole, L.B., Church, G., Storz, G., Rhee, S.G., 1994b, 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. USA 91: 7017–7021.
Choi, H.-J., Kang, S.W., Yang, C.-H., Rhee, S.G., Ryu, S.-E., 1998, Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution. Nature Struct. Biol. 5: 400–406.
Choi, M.-H., Sajed, D., Poole, L., Hirata, K., Herdman, S., Torian, B.E., Reed, S.L., 2005, An unusual surface peroxiredoxin protects invasive Entamoeba histolytica from oxidant attack. Mol. Biochem. Parasitol. 143: 80–89.
Christman, M.F., Storz, G., Ames, B.N., 1989, OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc. Natl.Acad. Sci. USA 86: 3484–3488.
Comini, M., Menge, U., Wissing, J., Flohé, L., 2005, Trypanothione synthesis in Crithidia revisited. J. Biol.Chem. 280: 6850–6860.
Comini, M.A., Guerrero, S.A., Haile, S., Menge, U., Lünsdorf, H., Flohé, L., 2004, Validation of Trypanosoma brucei trypanothione synthetase as drug target. Free Radic. Biol. Med. 36: 1289–1302.
Czech. M.P., Lawrence. J.C. Jr., Lynn. W.S., 1974, Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. Proc. Natl. Acad. Sci. USA 71: 4173–4177.
Declercq. J.-P., Evrard, C., Clippe. A., van der Stricht. D., Bernard. A., Knoops, B., 2001, Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution. J. Mol. Biol. 311: 751–759.
Dormeyer, M., Reckenfelderbäumer, N., Lüdemann, H., Krauth-Siegel, R.L., 2001, Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase. J. Biol. Chem. 276: 10602–10606.
Dumas, C., Ouellette, M., Tovar, J., Cunningham, M.L., Fairlamb, A.H., Tamar, S., Olivier, M., Papadopoulou, B., 1997, Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. EMBO J. 16: 2590–2598.
Eling, T.E., Glasgow, W.C., 1994, Cellular proliferation and lipid metabolism: importance of lipoxygenases in modulating epidermal growth factor-dependent mitogenesis. Cancer Metastasis Rev. 13: 397–410.
Ellis, H.R., Poole, L.B., 1997, Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry 36:15013–15018.
Evrard, C., Capron, A., Marchand, C., Clippe, A., Wattiez, R., Soumillon, P., Knoops, B., Declercq, J.-P., 2004, Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. J. Mol. Biol. 337: 1079–1090.
Fairlamb, A., 2003, Chemotherapy of human African trypanosomiasis: current and future prospects. Trends Parasitol. 19: 488–494.
Fairlamb. A.H., Cerami. A., 1992, Metabolism and functions of trypanothione in the Kinetoplastida. Ann. Rev. Microbiol. 46: 695–729.
Finkel, T., 2000, Redox-dependent signal transduction. FEBS Lett. 476: 52–54.
Fischer. E.H., 1997, Cellular regulation by protein phosphorylation: a historical overview. Biofactors 6: 367–374.
Fisher. A.B., Dodia. C., Manevich. Y., Chen. J.W., Feinstein. S.I., 1999, Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. J. Biol. Chem. 274: 21326–21334.
Flohé. L., 1998, The Achilles’ heel of trypanosomatids: trypanothione-mediated hydroperoxide metabolism. Biofactors 8: 87–91.
Flohé. L., 1989, The selenoprotein glutathione peroxidase. John Wiley & Sons, Inc., New York.
Flohé. L., Andreesen. J.R., Brigelius-Flohé. R., Maiorino. M., Ursini. F., 2000, Selenium, the element of the moon, in life on earth. IUBMB Life 49: 411–420.
Flohé L., Brigelius-Flohé R., 2006, Selenoproteins of the glutathione system. Kluwer Academic Publishers, Boston, Dordrecht, London.
Flohé, L., Brigelius-Flohé, R., Saliou, C., Traber, M.G., Packer, L., 1997, Redox regulation of NF-kappa B activation. Free Radic. Biol. Med. 22: 1115–1126.
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., Wylegalla, C., Hecht, H.J., 2002, Tryparedoxin peroxidase of Leishmania donovani: molecular cloning, heterologous expression, specificity, and catalytic mechanism. Arch. Biochem. Biophys. 397: 324–335.
Flohé, L., Hecht, H.J., Steinert, P., 1999, Glutathione and trypanothione in parasitic hydroperoxide metabolism. Free Radic. Biol. Med. 27: 966–984.
Gao, L., Tse, S.-W., Conrad, C., Andreadis, A., 2005, Saitohin, which is nested in the tau locus and confers allele-specific susceptibility to several neurodegenerative diseases, interacts with peroxiredoxin 6. J. Biol.Chem. 280: 39268–39272.
Gommel, D.U., Nogoceke, E., Morr, M., Kiess, M., Kalisz, H.M., Flohé, L., 1997, Catalytic characteristics of tryparedoxin. Eur. J. Biochem. 248: 913–918.
Gourlay, L.J., Bhella, D., Kelly, S.M., Price, N.C. Lindsay, J.G., 2003, Structure-function analysis of recombinant substrate protein 22 kDa (SP-22). J. Biol. Chem. 278: 32631–32637.
Griendling, K.K., Ushio-Fukai, M., 2000, Reactive oxygen species as mediators of angiotensin II signaling. Regul. Pept. 91: 1–27.
Harris, J.R., 1968, Release of a macromolecular protein component from human erythrocyte ghosts. Biochim. Biophys. Acta 150: 534–537.
Harris, J.R., 1969, Some negative staining features of a protein from erythrocyte ghosts. J. Mol. Biol. 46: 329–335.
Harris, J.R., 1971, Further studies on the proteins released from haemoglobin-free erythrocyte ghosts at low ionic strength. Biochim. Biophys. Acta 229: 761–770.
Harris, J.R., 1980, Torin and Cylindrin, two extrinsic proteins of the erythrocyte membrane: a review. Nouv. Rev. Fr. Hematol. 22: 411–448.
Harris, J.R., Bhella, D., Adrian, M., 2006. Recent developments in negative staining for transmission electron microscopy. Microscopy and Analysis, Issue 101, May, pp. 17–21.
Harris, J.R., Naeem, I., 1978, The subunit composition of two high molecular weight extrinsic proteins from human erythrocyte membranes. Biochim. Biophys. Acta 537: 495–500.
Harris, J.R., Schröder, E., Isupov, M.N., Scheffler, D., Kristensen, P., Littlechild, J.A., Vagin A.A., Meissner U., 2001, Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. Biochim. Biophys. Acta 1547: 221–234.
Harris, J.R., Scheffler, D., 2002, Routine preparation of air-dried negatively stained specimens and unstained specimens on holey carbon support films: a review of applications. Micron 33: 461–480.
Heffetz, D., Bushkin, I., Dror, R., Zick, Y., 1990, The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J. Biol. Chem. 265: 2896–2902.
Henderson, G.B., Fairlamb, A.H., Cerami, A., 1987, Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei. Mol. Biochem. Parasitol. 24: 39–45.
Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J., Mori, K., Yodoi, J., 1999, Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB. J. Biol. Chem. 274: 27891–27897.
Hirotsu, S., Abe, Y., Okada, K., Nagahara, N., Hori, H., Nishino, T., Hakoshima, T., 1999, Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23kDa/proliferation-associated gene product. Proc.Natl. Acad. Sci. USA 96: 12333–12338.
Hofmann, B., Hecht, H.J., Flohé, L., 2002, Peroxiredoxins. Biol. Chem. 383: 347–364.
Hungyi, S., Kim, A.T., Hedrick, C.C., Lusis, A.J., Tompkins, C., Finney, R., Leung, D.W., Paglia, D.E., 1997, Endogenous natural killer enhancing factor-B increases cellular resistance to oxidative stresses. Free Rad. Biol. Med. 22: 497–507.
Immenschuh, S., Iwahara, S., Satoh, H., Nell, C., Katz, N., Müller-Eberhard, U., 1995, Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells. Biochemistry 34: 13407–13411.
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J.D., Yamamoto, M., 1999, Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Devel. 13: 76–86.
Iwahara, S., Satoh, H., Song, D.X., Webb, J., Burlingame, A.L., Nagae, Y., Müller-Eberhard, U., 1995, Purification, characterization, and cloning of a heme-binding protein (23kDa) in rat liver cytosol. Biochemistry 34: 13398–13406.
Jacob, H.S., Jandl, J.H., 1966, Effects of sulfhydryl inhibition on red blood cells. 3. Glutathione in the regulation of the hexose monophosphate pathway. J. Biol. Chem. 241: 4243–4250.
Jacobson, F.S., Morgan, R.W., Christman, M.F., Ames, B.N., 1989, An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties. J. Biol. Chem. 264: 1488–1496.
Jaeger, T., Budde, H., Flohé, L., Menge, U., Singh, M., Trujillo, M., Radi, R., 2004, Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423: 182–191.
Jaeger, T., Flohé, L., 2006, The thiol-based redox network of pathogens as target in the search for new drugs. BioFactors 27: 109–120.
Jäschke, A., Mi, H., Tropschug, M., 1998, Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity. J. Mol. Biol. 277: 763–769.
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, C.-W., Yun, D.-J., Rhee, S.G., Cho, M.J., 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.
Jenney, F.E. Jr., Verhagen, M.F., Cui, X., Adams, M.W., 1999. Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286: 306–309.
Jeon, S.-J., Ishikawa, K., 2003, Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum perinix K1*. J. Biol. Chem. 278: 24174–24180.
Kato, H., Asanoi, M., Nakazawa, T., Maruyama, K., 1985, Cylinder protein isolated from rat liver mitochondria. Zool. Sci. 2: 485–490.
Kawai, S., Takeshita, S., Okazaki, M., Kikuno, R., Kudo, A., Amann, E., 1994, Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells. J. Biochem. 115: 641–643.
Kim, K., Kim, I.H., Lee, K.Y., Rhee, S.G., Stadtman, E.R., 1988, The isolation and purification of a specific ‘‘protector’’ protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system. J. Biol. Chem. 263: 4704–4711.
Kim, S.H., Fountoulakis, M., Cairns, N., Lubec, G., 2001, Protein levels in human peroxiredoxin subtypes in brains of patients with Alzheimer’s disease and Down syndrome. J. Neural Transm. Suppl 61: 223–235.
Kitano, K., Niimura, Y., Nishiyama, Y., Miki, K., 1999, Stimulation of peroxidase activity by decamerization relation to ionic strength: AhpC protein from Amphibacillus xylanus. J. Biochem. 126: 313–319.
Krapfenbauer, K., Engidawork, E., Cairns, N., Fountoulakis, M., Lubec, G., 2003, Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. Brain Res. 967: 152–160.
Krauth-Siegel, R.L., Meiering, S.K., Schmidt, H., 2003, The parasite-specific trypanothione metabolism of trypanosoma and leishmania. Biol. Chem. 384: 539–549.
Krieger, S., Schwarz, W., Ariyanayagam, M.R., Fairlamb, A.H., Krauth-Siegel, R.L., Clayton, C., 2000, Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol. Microbiol. 35: 542–552.
Kristensen, P., Rasmussen, D.E., Kristensen, B.I., 1999, Properties of thiol-specific anti-oxidant protein or calpromotin in solution. Biochem. Biophys. Res. Commun. 262: 127–131.
Leavey, P.J., Gonzalez-Aller, C., Thurman, G., Kleinberg, M., Rinckel, L., Ambrusso, D.W., Freeman, S., Kuypers, F.A., Ambrusso, D.R., 2002, A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity. J.Biol. Chem. 277: 45181–45187.
Lee, S.P., Hwang, Y.S., Kim, Y.J., Kwon, K.S., Kim, H.J., Kim, K., Chae, H.Z., 2001, Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J Biol Chem 276: 29826–29832.
Lee, T.H., Kim, S.U., Yu, S.L., Kim, S.H., Park, do S., Moon, H.B., Dho, S.H., Kwon, K.S., Kwon, H.J., Han, Y.H., Jeong, S., Kang, S.W., Shin, H.S., Lee, K.K., Rhee, S.G., Yu, D.Y., 2003, Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood 101: 5033–5038.
Levick, M.P., Tetaud, E., Fairlamb, A.H., Blackwell, J.M., 1998, Identification and characterisation of a functional peroxidoxin from Leishmania major. Mol. Biochem. Parasitol. 96: 125–137.
Li, S., Peterson, N.A., Kim, M.-Y., Kim, C.-Y., Hung, L.-W., Yi, M., Lekin, T., Segelke, B.W., Lott, J.S., Baker, E.N., 2005, Crystal structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin. J. Mol.Biol. 346: 1035–1046.
Lim, Y.S., Cha, M.K., Kim, H.K., Uhm, T.B., Park, J.W., Kim, K., Kim, I.H., 1993, Removal of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem. Biophys. Res. Commun. 192: 273–280.
Lim, M.J., Chae, H.Z., Rhee, S.G., Yu, D.Y., Lee, K.K., Yeom, Y.I., 1998, The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution. Gene 216: 197–205.
Lim, Y.S., Cha, M.K., Kim, H.K., Kim, I.H., 1994a, The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions. Gene 140: 279–284.
Lim, Y.-S., Cha, M.K., Yun, C.-H., Kim, H.-K., Kim, K., Kim, I.-H., 1994b, Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein. Biochem. Biophys. Res. Commun. 199: 199–206.
Lopez, J.A., Carvalho, T.U., de Souza,W., Flohé, L., Guerrero, S.A., Montemartini, M., Kalisz, H.M., Nogoceke, E., Singh, M., Alves, M.J., Colli W., 2000, Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi. Free Radic. Biol. Med. 28: 767–772.
Lüdemann, H., Dormeyer, M., Sticherling, C., Stallmann, D., Follmann, H., Krauth-Siegel, R.L., 1998, Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes. FEBS Lett. 431: 381–385.
Manevich, Y., Feinstein, S.I., Fisher, A.B., 2004. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc. Natl. Acad. Sci. USA 10: 3780–3785.
Maulik, N., Das, D.K., 2002, Redox signaling in vascular angiogenesis. Free Radic. Biol. Med. 33: 1047–1060.
Marianayagam, N.J., Sunde, M., Matthews, J.M., 2004, The power of two: protein dimerization in biology. TIBS 29: 618–625.
May, J.M., de Haen, C., 1979a, The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes. J. Biol. Chem. 254: 9017–9021.
May, J.M., de Haen, C., 1979b, Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells. J. Biol. Chem. 254: 2214–2220.
Meissner, U., Schröder, E., Scheffler, D., Martin, A.G., Harris, J.R., 2007, Formation, TEM study and 3D Reconstruction of the Human Erythrocyte Peroxidredoxin-2 Dodecahedral Higher-order Assembly. Micron 38: 29–39.
Mizohata, E., Sakai, H., Fusatomi, E., Terada, T., Murayama, K., Shorouzu, M., Yokoyama, S., 2005, Crystal structure of an archeal peroxiredoxin from the aerobic hypothermic crenarchaeon Aeropyrum perixK1. J. Mol. Biol. 354: 317–329.
Moore, R.B., Plishker, G.A., Shriver, S.K., 1990, Purification and measurement of calpromotin, the cytoplasmic protein which activates calcium-dependent potassium transport. Biochem. Biophys. Res. Commun. 166: 146–153.
Moore, R.B., Mankad, M.V., Shriver, S.K., Mankad, V.N., 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.
Moore, R.B., Shriver S.K., Jenkins L.D., Mankad V.N., Shah A.K., Plishker G.A., 1997, Calpromotin, a cytoplasmic protein, is associated with the formation of dense cells in sickle cell anemia. Amer. J. Hematol. 56: 100–106.
Moore, R.B., Shrivner, S.K., 1997, Protein 7.2b of human erythrocyte membranes binds to calpromotin. Biochem. Biophys. Res. Commun. 232: 294–297.
Mukherjee, S.P., Lynn, W.S., 1977, Reduced nicotinamide adenine dinucleotide phosphate oxidase in adipocyte plasma membrane and its activation by insulin. Possible role in the hormone’s effects on adenylate cyclase and the hexose monophosphate shunt. Arch. Biochem. Biophys. 184: 69–76.
Nakashima, K., Pontremoli, S., Horecker, B.L., 1969, Activation of rabbit liver fructose diphosphatase by coenzyme A and acyl carrier protein. Proc. Natl. Acad. Sci. USA 64: 947–951.
Netto, L.E.S., Chae, H.Z., Kang, S.-W., Rhee, S.G., Stadtman, E.R., 1996, Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. J. Biol.Chem. 271: 15315–15321.
Nogoceke, E., Gommel, D.U., Kiess, M., Kalisz, H.M., Flohé, L., 1997, A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378: 827–836.
Pedrajas, J.R., Miranda-Vizuete, A., Javanmardy, N., Gustafsson, J.A., Spyrou, G., 2000, Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J. Biol. Chem. 275: 16296–16301.
Phalen, T.J., Weirather, K., Deming, P.B., Anathy, V., Howe, A.K., van der Vlier, A., Jönsson, T.J., Poole, L.B., Heintz, N.H., 2006, Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery. J. Cell Biol. 175: 779–789.
Plishker, G.A., White, P.A., Cadman, E.D., 1986, Involvement of a cytoplasmic protein calcium-dependent potassium efflux in red blood cells. Am. J. Physiol. 251: C535.
Plishker, G.A., Chevalier, D., Seinsoth, L., Moore, R.B., 1992, Calcium-activated potassium transport and high molecular weight forms of calpromotin. J. Biol. Chem. 267: 21839–21843.
Pontremoli, S., Luppis, B., Traniello, S., Rippa, M., Horecker, B.L., 1965, Fructose diphosphatase from rabbit liver.IV. Sulfhydryl groups and their relation to the catalytic activity. Arch. Biochem. Biophys. 112: 1–15.
Pontremoli, S., Traniello, S., Enser, M., Shapiro, S., Horecker, B.L.,1967, Regulation of fructose diphosphatase activity by disulfide exchange. Proc. Natl. Acad. Sci. USA 58: 286–293.
Poole, L.B., Ellis, H.R., 2002, Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. Meth. Enzymol. 348: 122–136.
Posner, B.I., Faure, R., Burgess, J.W., Bevan, A.P., Lachance, D., Zhang-Sun, G., Fantus, I.G., Ng, J.B., Hall, D.A., Lum, B.S., et al., 1994, Peroxovanadium compounds. A new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics. J. Biol. Chem. 269: 4596–4604.
Rabilloud, T., Berthier, R., Vincon, M., Ferbus, D., Doubin, G., Lawrence, J.J., 1995, Early events in erythroid differentiation: accumulation of the acidic peroxiredoxin. Biochem. J. 312: 669–705.
Radeke, H.H., Meier, B., Topley, N., Floge, J., Habermehl, G.G., Resch, K., 1990, Interleukin 1-alpha and tumor necrosis factor-alpha induce oxygen radical production in mesangial cells. Kidney Int. 37: 767–775.
Ralat, L.A., Manevich, Y., Fisher, A.B., Colman R.F., 2006, Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry 45: 360–372.
Reynolds, C.M., Poole, L.B., 2001, Activity of one of two engineered heterodimers of AhpF, the NADH:peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains. Biochemistry 40: 3912–3919.
Rhee. S.G, 1999, Redox signalling: hydrogen peroxides as intracellular messenger. Exptl. Molec. Med. 31: 53–59.
Rhee. S.G., Chang. T.S., Bae. YS., Lee, S.R., Kang, S.W., 2003, Cellular regulation by hydrogen peroxide. J. Am. Soc. Nephrol. 14(8 Suppl 3):S211–215.
Rhee, S.G., Kang, S.W., Jeong, W., Chang, T.-S., Yang, K.-S., Woo, H.A., 2005, Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 183–189.}
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., Ichijo, H., 1998, Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17: 2596–2606.
Sarma, G.N., Nickel, C., Rahlfs, S., Fischer, M., Becker, K., Karplus, P.A., 2005, Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin. J. Mol. Biol. 346: 1021–1034.
Sasagawa, I., Matsuki, S., Suzuki, Y., Iuchi, Y., Tohya, K., Kimura, M., Nakada, T., Fujii, J., 2001, Possible involvement of the membrane-bound form of peroxiredoxin 4 in acrosome formation during spermiogenesis of rats. Eur J. Biochem. 268: 3053–3061.
Schmidt, A.K., Krauth-Siegel, R., 2002, Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development. Curr. Top. Med. Chem. 2:1239–1259.
Schmidt, A and Krauth-Siegel, RL (2002) Enzymes of the trypanothione metabolism as targets for antitrypanosomal drug development. Curr Top Med Chem:1239–1259.
Schröder, E., Isupov, M.N., Naran, A., Littlechild, J.A., 1999, Crystallization and preliminary X-ray analysis of human thioredoxin peroxidase-B from red blood cells. Acta Cryst. D55: 536–538.
Schröder, E., Littlechild, J.A., Lebedev, A.A., Errington, N., Vagin, A.A., Isupov, M.N., 2000, Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7Å resolution. Structure 8: 605–615.
Schröder, E., Ponting, C.P, 1998. Evidence that the peroxiredoxins are novel members of the thioredoxin fold superfamily. Protein Science 7: 2465–2468.
Schröder, E., Willis, A.C., Ponting, C.P., 1998, Porcine natural-killer enhancing factor-B: oligomerization and identification as a calpain substrate in vitro. Biochim Biophys. Acta 1383: 279–291.
Shau, H., Kim, A., 1994, Identification of natural killer enhancing factor as a major antioxidant in human red blood cells. Biochem. Biophys. Res. Commun. 199: 83–88.
Shau, H., Kim, A.T., Hedrick, C.C., Lusis, A.J., Tompkins, C., Finney, R., Leung, D.W., Paglia, D.E., 1997, Endogenous natural killer enhancing factor-B increases cellular resistance to oxidative stress. Free Rad. Biol. Med. 22: 497–507.
Sies, H., Gerstenecke, R.C., Menzel, H., Flohé, L., 1972, Oxidation in the NADP system and release of GSSG from hemoglobin-free perfused rat liver during peroxidatic oxidation of glutathione by hydroperoxides. FEBS Lett. 27: 171–175.
Söhling, B., Parther, T., Rucknagel, K.P., Wagner, M.A., Andreesen, J.R., 2001. A selenocysteine-containing peroxiredoxin from the strictly anaerobic organism Eubacterium acidaminophilum. Biol Chem. 382: 979–986.
Stacy, R.A., Munthe, E., Steinum, T., Sharma, B., Aalen, R.B., 1996, A peroxiredoxin antioxidant is encoded by a dormancy-related gener, Per1, expressed during late development in the aleurone and embryo of barley grains. Plant Mol. Biol. 31: 1205–1216.
Sztajer, H., Gamain, B., Aumann, K.D., Slomianny, C., Becker, K., Brigelius-Flohé, R., Flohé, L., 2001, The putative glutathione peroxidase gene of Plasmodium falciparum codes for a thioredoxin peroxidase. J. Biol. Chem. 276: 7397–7403.
Tang, D.G., La, E., Kern, J., Kehrer, P., 2002, Fatty acid oxidation and signaling in apoptosis. Biol. Chem. 383: 425–442.
Tartaglia, L.A., Storz, G., Brodsky, M.H., Lai, A., Ames, B.N., 1990, Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredocind reductase and other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 265: 10535–10540
Tetaud, E., Giroud, C., Prescott, A.R., Parkin, D.W., Baltz, D., Biteau, N., Baltz, T, Fairlamb, A.H., 2001, Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei. Mol. Biochem. Parasitol. 116: 171–183.
Toledano, M.B., Delaunay, A., Monceau, L., Tacnet, F., 2004. Microbial rm H2O2 sensors as archetypical redox signaling modules. TIBS. 29: 351–357.
Tovar, J., Cunningham, M.L., Smith, A.C., Croft, S.L., Fairlamb, A.H., 1998a, Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: effect on parasite intracellular survival. Proc. Natl. Acad. Sci. USA 95: 5311–5316.
Tovar, J., Wilkinson, S., Mottram, J.C., Fairlamb, A.H., 1998b, Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus. Mol. Microbiol. 29: 653–660.
Trujillo, M., Budde, H., Pineyro, M.D, Stehr, M., Robello, C., Flohé, L., Radi, R., 2004, Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. J. Biol. Chem. 279: 34175–34182.
Ursini, F., Heim, S., Kiess, M., Maiorino, M., Roveri, A., Wissing, J., Flohé, L., 1999 Dual function of the selenoprotein PHGPx during sperm maturation. Science 285: 1393–1396.
Veal, E.A., Findlay, V.J., Day, A.M., Bozonet, S.M., Evans, J.M., Quinn, J., 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
Vivancos, A.P., Castillo, E.A., Biteau, B., Nicot, C., Ayte, J., Toledano, M.B., Hidalgo, E., 2005, A cysteine-sulphinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc. Natl. Acad. Sci. USA 102: 8875–8880.
Watabe, S., Hiroi, T., Yamamoto, Y., Fujioka, Y., Hasegawa, H., Yago, N., Takahashi, S.Y., 1997, SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria. Eur.J. Biochem. 249: 52–60.
Wilkinson, S.R., Prathalingam, S.R., Kelly, J.M., 2003, RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome. J. Biol. Chem. 278: 31640–31646.
Wilkinson, S.R., Temperton, N.J., Mondragon, A., Kelly, .M., 2000, Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. J. Biol. Chem. 275: 8220–8225.
Wood, Z., Schröder, E., Harris, J.R., Poole, L.B., 2003, Structure, mechanism and regulation of peroxiredoxins. TIBS 28: 32–40.
Yamamoto, T., Matsui, Y., Natori, S., Obinata, M., 1989, Cloning of a housekeeping gene (MER5) preferentially expressed in murine erythroleukemia cells. Gene 80: 337–343.
Zhu, H., Bunn, H.F., 1999, Oxygen sensing and signaling: impact on the regulation of physiologically important genes. Respir. Physiol. 115: 239–247.
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Flohé, L., Harris, J.R. (2007). Introduction. 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_1
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