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Science 25 April 2003:
Vol. 300. no. 5619, pp. 650 - 653
DOI: 10.1126/science.1080405
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Reports

Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling

Zachary A. Wood,1* Leslie B. Poole,2 P. Andrew Karplus1{dagger}

Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide–mediated signal transduction. We showthat bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.

1 Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97333, USA.
2 Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA.



* Present address: Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403, USA.

{dagger} To whom correspondence should be addressed. E-mail: karplusp{at}ucs.orst.edu

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Regeneration of Peroxiredoxins during Recovery after Oxidative Stress: ONLY SOME OVEROXIDIZED PEROXIREDOXINS CAN BE REDUCED DURING RECOVERY AFTER OXIDATIVE STRESS.
M. Chevallet, E. Wagner, S. Luche, A. van Dorsselaer, E. Leize-Wagner, and T. Rabilloud (2003)
J. Biol. Chem. 278, 37146-37153
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Science. ISSN 0036-8075 (print), 1095-9203 (online)