tailieunhanh - Báo cáo khoa học: Typical 2-Cys peroxiredoxins – structures, mechanisms and functions

Peroxiredoxins are abundant cellular antioxidant proteins that help to con-trol intracellular peroxide levels. These proteins may also function, in part, through an evolved sensitivity of some peroxiredoxins towards peroxide-mediated inactivation in hydrogen peroxide signaling in eukaryotes. | ỊFEBS Journal REVIEW ARTICLE Typical 2-Cys peroxiredoxins - structures mechanisms and functions Andrea Hall1 P. A. Karplus1 and Leslie B. Poole2 1 Department of Biochemistry and Biophysics Oregon State University Corvallis OR USA 2 Department of Biochemistry Wake Forest University Schoolof Medicine Winston-Salem NC USA Keywords antioxidants hydrogen peroxide hydroperoxides mechanisms NADPH oxidase oxidative stress peroxiredoxins redox signaling signal transduction sulfenic acid Correspondence L. B. Poole Department of Biochemistry Wake Forest University Schoolof Medicine MedicalCenter Boulevard Winston-Salem NC 27157 USA Fax 1 336 716 6711 Tel 1 336 777 3242 E-mail lbpoole@ Received 6 October 2008 revised 3 February 2009 accepted 25 February 2009 doi Peroxiredoxins are abundant cellular antioxidant proteins that help to control intracellular peroxide levels. These proteins may also function in part through an evolved sensitivity of some peroxiredoxins towards peroxidemediated inactivation in hydrogen peroxide signaling in eukaryotes. This review summarizes recent progress in our understanding of the catalytic and regulatory mechanisms of typical 2-Cys peroxiredoxins and of the biological roles played by these important enzymes in oxidative stress and nonstress-related cellular signaling. New evidence suggests localized peroxide buildup plays a role in nonstress-related signaling. Peroxiredoxins Prxs EC are ubiquitous antioxidant enzymes found in all organisms with the single exception to our knowledge of Borrelia burgdorferi and other Borrelia species . The broad distribution of Prxs and the high levels of expression 1 suggest that they are both an ancient and important enzyme family. Prxs are assumed to have evolved from a thioredoxin-like precursor protein and a model for the evolutionary path has been presented 2 . The initial publication defining this family of enzymes introduced the term peroxidoxin 3 but .