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Science 300 (5619): 653-656

Copyright © 2003 by the American Association for the Advancement of Science

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Hyun Ae Woo,1* Ho Zoon Chae,2*{dagger} Sung Chul Hwang,2{ddagger} Kap-Seok Yang,1 Sang Won Kang,1 Kanghwa Kim ,2§ Sue Goo Rhee2||

Abstract: The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. However, by metabolic labeling of mammalian cells with 35S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H2O2, is rapidly reduced to the catalytically active thiol form. The mammalian cells' ability to reduce protein sulfinic acid might serve as a mechanism to repair oxidatively damaged proteins or represent a new type of cyclic modification by which the function of various proteins is regulated.

1 Center for Cell Signaling Research and Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, Korea.
2 Laboratory of Cell Signaling, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

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{dagger} Present address: Department of Biological Sciences, College of Natural Sciences, Chonnam National University, Kwangju 500-757, Korea.

{ddagger} Present address: Department of Pulmonary and Critical Care Medicine, Ajou University School of Medicine, Suwon 442-749, Korea.

§ Present address: Department of Food and Nutrition, College of Home Economics, Chonnam National University, Kwangju 500-757, Korea.

* These authors contributed equally to this work.

|| To whom correspondence should be addressed. E-mail: sgrhee{at}

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   Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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Y. Ikeda, M. Nakano, H. Ihara, R. Ito, N. Taniguchi, and J. Fujii (2011)
J. Biochem. 149, 443-453
   Abstract »    Full Text »    PDF »
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I. Iglesias-Baena, S. Barranco-Medina, F. Sevilla, and J.-J. Lazaro (2011)
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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J. Biol. Chem. 285, 34485-34492
   Abstract »    Full Text »    PDF »
Redox Regulation of Lipopolysaccharide-mediated Sulfiredoxin Induction, Which Depends on Both AP-1 and Nrf2.
H. Kim, Y. Jung, B. S. Shin, H. Kim, H. Song, S. H. Bae, S. G. Rhee, and W. Jeong (2010)
J. Biol. Chem. 285, 34419-34428
   Abstract »    Full Text »    PDF »
T-LAK Cell-originated Protein Kinase (TOPK) Phosphorylation of Prx1 at Ser-32 Prevents UVB-induced Apoptosis in RPMI7951 Melanoma Cells through the Regulation of Prx1 Peroxidase Activity.
T. A. Zykova, F. Zhu, T. I. Vakorina, J. Zhang, L. A. Higgins, D. V. Urusova, A. M. Bode, and Z. Dong (2010)
J. Biol. Chem. 285, 29138-29146
   Abstract »    Full Text »    PDF »
Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling.
E. W. Miller, B. C. Dickinson, and C. J. Chang (2010)
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   Abstract »    Full Text »    PDF »
K. Wetzelberger, S. P. Baba, M. Thirunavukkarasu, Y.-S. Ho, N. Maulik, O. A. Barski, D. J. Conklin, and A. Bhatnagar (2010)
J. Biol. Chem. 285, 26135-26148
   Abstract »    Full Text »    PDF »
Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation.
T. J. Tavender and N. J. Bulleid (2010)
J. Cell Sci. 123, 2672-2679
   Abstract »    Full Text »    PDF »
The CCAAT-binding complex coordinates the oxidative stress response in eukaryotes.
M. Thon, Q. Al Abdallah, P. Hortschansky, D. H. Scharf, M. Eisendle, H. Haas, and A. A. Brakhage (2010)
Nucleic Acids Res. 38, 1098-1113
   Abstract »    Full Text »    PDF »
Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin.
I. Iglesias-Baena, S. Barranco-Medina, A. Lazaro-Payo, F. J. Lopez-Jaramillo, F. Sevilla, and J.-J. Lazaro (2010)
J. Exp. Bot. 61, 1509-1521
   Abstract »    Full Text »    PDF »
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J. Biol. Chem. 284, 33305-33310
   Abstract »    Full Text »    PDF »
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K.-S. Lee, K. Iijima-Ando, K. Iijima, W.-J. Lee, J. H. Lee, K. Yu, and D.-S. Lee (2009)
J. Biol. Chem. 284, 29454-29461
   Abstract »    Full Text »    PDF »
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J. W. Park, J. J. Mieyal, S. G. Rhee, and P. B. Chock (2009)
J. Biol. Chem. 284, 23364-23374
   Abstract »    Full Text »    PDF »
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J. H. Seo, J. C. Lim, D.-Y. Lee, K. S. Kim, G. Piszczek, H. W. Nam, Y. S. Kim, T. Ahn, C.-H. Yun, K. Kim, et al. (2009)
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   Abstract »    Full Text »    PDF »
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Y. H. Noh, J. Y. Baek, W. Jeong, S. G. Rhee, and T.-S. Chang (2009)
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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S. Y. Kim, H.-Y. Jo, M. H. Kim, Y.-y. Cha, S. W. Choi, J.-H. Shim, T. J. Kim, and K.-Y. Lee (2008)
J. Biol. Chem. 283, 33563-33568
   Abstract »    Full Text »    PDF »
Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate.
T. J. Jonsson, M. S. Murray, L. C. Johnson, and W. T. Lowther (2008)
J. Biol. Chem. 283, 23846-23851
   Abstract »    Full Text »    PDF »
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Y. M. Lee, S. H. Park, D.-I. Shin, J.-Y. Hwang, B. Park, Y.-J. Park, T. H. Lee, H. Z. Chae, B. K. Jin, T. H. Oh, et al. (2008)
J. Biol. Chem. 283, 9986-9998
   Abstract »    Full Text »    PDF »
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N. Fujiwara, M. Nakano, S. Kato, D. Yoshihara, T. Ookawara, H. Eguchi, N. Taniguchi, and K. Suzuki (2007)
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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P. Cordray, K. Doyle, K. Edes, P. J. Moos, and F. A. Fitzpatrick (2007)
J. Biol. Chem. 282, 32623-32629
   Abstract »    Full Text »    PDF »
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R. C. Cumming, R. Dargusch, W. H. Fischer, and D. Schubert (2007)
J. Biol. Chem. 282, 30523-30534
   Abstract »    Full Text »    PDF »
Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation.
J. R. Burgoyne, M. Madhani, F. Cuello, R. L. Charles, J. P. Brennan, E. Schroder, D. D. Browning, and P. Eaton (2007)
Science 317, 1393-1397
   Abstract »    Full Text »    PDF »
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R. L. Charles, E. Schroder, G. May, P. Free, P. R. J. Gaffney, R. Wait, S. Begum, R. J. Heads, and P. Eaton (2007)
Mol. Cell. Proteomics 6, 1473-1484
   Abstract »    Full Text »    PDF »
Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences.
A. Martinez-Ruiz and S. Lamas (2007)
Cardiovasc Res 75, 220-228
   Abstract »    Full Text »    PDF »
Glutathione Is Recruited into the Nucleus in Early Phases of Cell Proliferation.
J. Markovic, C. Borras, A. Ortega, J. Sastre, J. Vina, and F. V. Pallardo (2007)
J. Biol. Chem. 282, 20416-20424
   Abstract »    Full Text »    PDF »
Role of p53 in antioxidant defense of HPV-positive cervical carcinoma cells following H2O2 exposure.
B. Ding, S. G. Chi, S. H. Kim, S. Kang, J. H. Cho, D. S. Kim, and N. H. Cho (2007)
J. Cell Sci. 120, 2284-2294
   Abstract »    Full Text »    PDF »
The Peroxiredoxin Tpx1 Is Essential as a H2O2 Scavenger during Aerobic Growth in Fission Yeast.
M. Jara, A. P. Vivancos, I. A. Calvo, A. Moldon, M. Sanso, and E. Hidalgo (2007)
Mol. Biol. Cell 18, 2288-2295
   Abstract »    Full Text »    PDF »
Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia.
S. S. Mukhopadhyay, K. S. Leung, M. J. Hicks, P. J. Hastings, H. Youssoufian, and S. E. Plon (2006)
J. Cell Biol. 175, 225-235
   Abstract »    Full Text »    PDF »
Molecular Mechanism of the Reduction of Cysteine Sulfinic Acid of Peroxiredoxin to Cysteine by Mammalian Sulfiredoxin.
W. Jeong, S. J. Park, T.-S. Chang, D.-Y. Lee, and S. G. Rhee (2006)
J. Biol. Chem. 281, 14400-14407
   Abstract »    Full Text »    PDF »
Decline of contractility during ischemia-reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin.
F. C. Chen and O. Ogut (2006)
Am J Physiol Cell Physiol 290, C719-C727
   Abstract »    Full Text »    PDF »
Regulation of heavy subunit chain of {gamma}-glutamylcysteine synthetase by tumor necrosis factor-{alpha} in lens epithelial cells: role of LEDGF/p75.
Y. Takamura, N. Fatma, E. Kubo, and D. P. Singh (2006)
Am J Physiol Cell Physiol 290, C554-C566
   Abstract »    Full Text »    PDF »
Single-Site Oxidation, Cysteine 108 to Cysteine Sulfinic Acid, in D-Amino Acid Oxidase from Trigonopsis variabilis and Its Structural and Functional Consequences.
A. Slavica, I. Dib, and B. Nidetzky (2005)
Appl. Envir. Microbiol. 71, 8061-8068
   Abstract »    Full Text »    PDF »
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. C. Moon, 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, et al. (2005)
J. Biol. Chem. 280, 28775-28784
   Abstract »    Full Text »    PDF »
A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway.
A. P. Vivancos, E. A. Castillo, B. Biteau, C. Nicot, J. Ayte, M. B. Toledano, and E. Hidalgo (2005)
PNAS 102, 8875-8880
   Abstract »    Full Text »    PDF »
Oxidation of a Eukaryotic 2-Cys Peroxiredoxin Is a Molecular Switch Controlling the Transcriptional Response to Increasing Levels of Hydrogen Peroxide.
S. M. Bozonet, V. J. Findlay, A. M. Day, J. Cameron, E. A. Veal, and B. A. Morgan (2005)
J. Biol. Chem. 280, 23319-23327
   Abstract »    Full Text »    PDF »
Variable overoxidation of peroxiredoxins in human lung cells in severe oxidative stress.
S. T. Lehtonen, P. M. H. Markkanen, M. Peltoniemi, S. W. Kang, and V. L. Kinnula (2005)
Am J Physiol Lung Cell Mol Physiol 288, L997-L1001
   Abstract »    Full Text »    PDF »
Oxidative Modifications and Aggregation of Cu,Zn-Superoxide Dismutase Associated with Alzheimer and Parkinson Diseases.
J. Choi, H. D. Rees, S. T. Weintraub, A. I. Levey, L.-S. Chin, and L. Li (2005)
J. Biol. Chem. 280, 11648-11655
   Abstract »    Full Text »    PDF »
Reduction of Cysteine Sulfinic Acid by Sulfiredoxin Is Specific to 2-Cys Peroxiredoxins.
H. A. Woo, W. Jeong, T.-S. Chang, K. J. Park, S. J. Park, J. S. Yang, and S. G. Rhee (2005)
J. Biol. Chem. 280, 3125-3128
   Abstract »    Full Text »    PDF »
Hydrogen peroxide as a signal controlling plant programmed cell death.
T. S. Gechev and J. Hille (2005)
J. Cell Biol. 168, 17-20
   Abstract »    Full Text »    PDF »
Contribution of the Helicobacter pylori Thiol Peroxidase Bacterioferritin Comigratory Protein to Oxidative Stress Resistance and Host Colonization.
G. Wang, A. A. Olczak, J. P. Walton, and R. J. Maier (2005)
Infect. Immun. 73, 378-384
   Abstract »    Full Text »    PDF »
Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine.
T.-S. Chang, W. Jeong, H. A. Woo, S. M. Lee, S. Park, and S. G. Rhee (2004)
J. Biol. Chem. 279, 50994-51001
   Abstract »    Full Text »    PDF »
Regulation of Anaerobic Dehalorespiration by the Transcriptional Activator CprK.
S. M. Pop, R. J. Kolarik, and S. W. Ragsdale (2004)
J. Biol. Chem. 279, 49910-49918
   Abstract »    Full Text »    PDF »
Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors.
J. Kwon, S.-R. Lee, K.-S. Yang, Y. Ahn, Y. J. Kim, E. R. Stadtman, and S. G. Rhee (2004)
PNAS 101, 16419-16424
   Abstract »    Full Text »    PDF »
Role of Oxidative Modifications in Atherosclerosis.
R. Stocker and J. F. Keaney Jr. (2004)
Physiol Rev 84, 1381-1478
   Abstract »    Full Text »    PDF »
Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers.
H. J. Forman, J. M. Fukuto, and M. Torres (2004)
Am J Physiol Cell Physiol 287, C246-C256
   Abstract »    Full Text »    PDF »
Biochemical Characterization of 2-Cys Peroxiredoxins from Schistosoma mansoni.
A. A. Sayed and D. L. Williams (2004)
J. Biol. Chem. 279, 26159-26166
   Abstract »    Full Text »    PDF »
The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization.
R. M. Canet-Aviles, M. A. Wilson, D. W. Miller, R. Ahmad, C. McLendon, S. Bandyopadhyay, M. J. Baptista, D. Ringe, G. A. Petsko, and M. R. Cookson (2004)
PNAS 101, 9103-9108
   Abstract »    Full Text »    PDF »
The Structure of the Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans: DO CONFORMATIONAL CHANGES FACILITATE RECYCLING OF THE REDOX DISULFIDE?.
C. Meunier-Jamin, U. Kapp, G. A. Leonard, and S. McSweeney (2004)
J. Biol. Chem. 279, 25830-25837
   Abstract »    Full Text »    PDF »
Peroxiredoxin-null Yeast Cells Are Hypersensitive to Oxidative Stress and Are Genomically Unstable.
C.-M. Wong, K.-L. Siu, and D.-Y. Jin (2004)
J. Biol. Chem. 279, 23207-23213
   Abstract »    Full Text »    PDF »
Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress.
R. C. Cumming, N. L. Andon, P. A. Haynes, M. Park, W. H. Fischer, and D. Schubert (2004)
J. Biol. Chem. 279, 21749-21758
   Abstract »    Full Text »    PDF »
Regeneration of Peroxiredoxins by p53-Regulated Sestrins, Homologs of Bacterial AhpD.
A. V. Budanov, A. A. Sablina, E. Feinstein, E. V. Koonin, and P. M. Chumakov (2004)
Science 304, 596-600
   Abstract »    Full Text »    PDF »
Taurine Supplementation Reduces Oxidative Stress and Improves Cardiovascular Function in an Iron-Overload Murine Model.
G. Y. Oudit, M. G. Trivieri, N. Khaper, T. Husain, G. J. Wilson, P. Liu, M. J. Sole, and P. H. Backx (2004)
Circulation 109, 1877-1885
   Abstract »    Full Text »    PDF »
The NAD(P)H Oxidase Homolog Nox4 Modulates Insulin-Stimulated Generation of H2O2 and Plays an Integral Role in Insulin Signal Transduction.
K. Mahadev, H. Motoshima, X. Wu, J. M. Ruddy, R. S. Arnold, G. Cheng, J. D. Lambeth, and B. J. Goldstein (2004)
Mol. Cell. Biol. 24, 1844-1854
   Abstract »    Full Text »    PDF »
Cytosolic Peroxiredoxin Attenuates The Activation Of Jnk And P38 But Potentiates That Of Erk In Hela Cells Stimulated With Tumor Necrosis Factor-{alpha}.
S. W. Kang, T.-S. Chang, T.-H. Lee, E. S. Kim, D.-Y. Yu, and S. G. Rhee (2004)
J. Biol. Chem. 279, 2535-2543
   Abstract »    Full Text »    PDF »
Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid: IMMUNOBLOT DETECTION WITH ANTIBODIES SPECIFIC FOR THE HYPEROXIDIZED CYSTEINE-CONTAINING SEQUENCE.
H. A. Woo, S. Won Kang, H. K. Kim, K.-S. Yang, H. Z. Chae, and S. G. Rhee (2003)
J. Biol. Chem. 278, 47361-47364
   Abstract »    Full Text »    PDF »
Phorbol Ester-dependent Activation of Peroxiredoxin I Gene Expression via a Protein Kinase C, Ras, p38 Mitogen-activated Protein Kinase Signaling Pathway.
A. Hess, N. Wijayanti, A. P. Neuschafer-Rube, N. Katz, T. Kietzmann, and S. Immenschuh (2003)
J. Biol. Chem. 278, 45419-45434
   Abstract »    Full Text »    PDF »
M. Chevallet, E. Wagner, S. Luche, A. van Dorsselaer, E. Leize-Wagner, and T. Rabilloud (2003)
J. Biol. Chem. 278, 37146-37153
   Abstract »    Full Text »    PDF »
BIOCHEMISTRY: An Overoxidation Journey with a Return Ticket.
G. Georgiou and L. Masip (2003)
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   Abstract »    Full Text »    PDF »

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