Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Logo for

Science 300 (5619): 592-594

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

BIOCHEMISTRY:
An Overoxidation Journey with a Return Ticket

George Georgiou and Lluis Masip

The peroxiredoxins are ubiquitous enzymes that catalyze the reduction of hydrogen peroxide. In their Perspective, Georgiou and Masip discuss some intriguing new details of peroxiredoxin biochemistry that reveal how these enzymes can be simultaneously both antioxidants and modulators of signal transduction (Wood et al.; Woo et al.).


The authors are in the Department of Chemical Engineering, Biomedical Engineering and Institute for Cell and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. E-mail: gg{at}che.utexas.edu


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structural basis of redox-dependent modulation of galectin-1 dynamics and function.
C. M. Guardia, J. J. Caramelo, M. Trujillo, S. P. Mendez-Huergo, R. Radi, D. A. Estrin, and G. A. Rabinovich (2014)
Glycobiology 24, 428-441
   Abstract »    Full Text »    PDF »
Crystal Structures of Complexes of the Branched-Chain Aminotransferase from Deinococcus radiodurans with {alpha}-Ketoisocaproate and L-Glutamate Suggest the Radiation Resistance of This Enzyme for Catalysis.
C.-D. Chen, C.-H. Lin, P. Chuankhayan, Y.-C. Huang, Y.-C. Hsieh, T.-F. Huang, H.-H. Guan, M.-Y. Liu, W.-C. Chang, and C.-J. Chen (2012)
J. Bacteriol. 194, 6206-6216
   Abstract »    Full Text »    PDF »
Shedding Light on Selenium Biomineralization: Proteins Associated with Bionanominerals.
M. Lenz, B. Kolvenbach, B. Gygax, S. Moes, and P. F. X. Corvini (2011)
Appl. Envir. Microbiol. 77, 4676-4680
   Abstract »    Full Text »    PDF »
NADPH Thioredoxin Reductase C Controls the Redox Status of Chloroplast 2-Cys Peroxiredoxins in Arabidopsis thaliana.
K. Kirchsteiger, P. Pulido, M. Gonzalez, and F. J. Cejudo (2009)
Mol Plant 2, 298-307
   Abstract »    Full Text »    PDF »
Irreversible Oxidation of the Active-site Cysteine of Peroxiredoxin to Cysteine Sulfonic Acid for Enhanced Molecular Chaperone Activity.
J. C. Lim, H.-I. Choi, Y. S. Park, H. W. Nam, H. A. Woo, K.-S. Kwon, Y. S. Kim, S. G. Rhee, K. Kim, and H. Z. Chae (2008)
J. Biol. Chem. 283, 28873-28880
   Abstract »    Full Text »    PDF »
Phorbol 12-Myristate 13-Acetate-dependent Protein Kinase C{delta}-Tyr311 Phosphorylation in Cardiomyocyte Caveolae.
V. O. Rybin, J. Guo, Z. Gertsberg, S. J. Feinmark, and S. F. Steinberg (2008)
J. Biol. Chem. 283, 17777-17788
   Abstract »    Full Text »    PDF »
Dimer-Oligomer Interconversion of Wild-type and Mutant Rat 2-Cys Peroxiredoxin: DISULFIDE FORMATION AT DIMER-DIMER INTERFACES IS NOT ESSENTIAL FOR DECAMERIZATION.
T. Matsumura, K. Okamoto, S.-i. Iwahara, H. Hori, Y. Takahashi, T. Nishino, and Y. Abe (2008)
J. Biol. Chem. 283, 284-293
   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 »
Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte.
F. M. Low, M. B. Hampton, A. V. Peskin, and C. C. Winterbourn (2007)
Blood 109, 2611-2617
   Abstract »    Full Text »    PDF »
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life.
B. Halliwell (2006)
Plant Physiology 141, 312-322
   Full Text »    PDF »
Model Systems for Environmental Signaling.
N. W. Blackstone and D. M. Bridge (2005)
Integr. Comp. Biol. 45, 605-614
   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 »
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 »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882