TAILIEUCHUNG - Báo cáo khoa học: Typical 2-Cys peroxiredoxins – modulation by covalent transformations and noncovalent interactions

2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces not only the usual thiol–disulfide exchange but also higher oxida-tion states of the sulfur atom. | REVIEW ARTICLE Typical 2-Cys peroxiredoxins - modulation by covalent transformations and noncovalent interactions Martin Aran Diego S. Ferrero Eduardo Pagano and Ricardo A. Wolosiuk Institute Leloir Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires Argentina Keywords 2-Cys peroxiredoxin ATP binding autophosphorylation molecular chaperone oligomerization overoxidation oxidative stress peroxidase mechanism sulfenic acid sulfinic-phosphorylanhydride Correspondence R. A. Wolosiuk Instituto Leloir IIBBA-CONICET Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires Patricias Argentinas 435 C1405BWE Buenos Aires Argentina Fax 54 11 5238 7501 Tel 54 11 5238 7500 E-mail rwolosiuk@ Present address Catedra de Bioquimica Facultad de Agronomia Universidad de Buenos Aires Argentina 2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines whose modification embraces not only the usual thiol-disulfide exchange but also higher oxidation states of the sulfur atom. These changes are part of a complex system wherein the cooperation with other post-translational modifications - phosphorylation acetylation - may function as major regulatory mechanisms of the quaternary structure. More importantly modern proteomic approaches have identified the oxyacids at cysteine residues as novel protein targets for unsuspected post-translational modifications such as phosphorylation that yields the unusual sulfi o nic-phosphoryl anhydride. In this article we review the biochemical attributes of 2-Cys peroxiredoxins that in combination with complementary studies of forward and reverse genetics have generated stimulating molecular models to explain how this enzyme integrates into cell signaling in vivo. Received 10 December 2008 revised 30 .

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