Catalytic Thr or ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

Typical 2-Cys Peroxiredoxins (2-Cys Prxs) reduce hydroperoxides with extraordinary rates due to an active site composed of a catalytic triad, containing a peroxidatic cysteine (C P ), an Arg, and a Thr (or Ser). 2-Cys Prx are involved in processes such as cancer; neurodegeneration and host-pathogen...

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Bibliographic Details

Main Author:	Tairum, C. A. (author)
Other Authors:	Santos, M. C. (author), Breyer, C. A. (author), Geyer, R. R. (author), Nieves Álvarez, Cecilia J. (author), Portillo-Ledesma, Stephanie (author), Ferrer-Sueta, Gerardo (author), Toledo, J. C. Jr (author), Toyama, M. H. (author), Augusto, Ohara (author), Netto, Luis E. S. (author), De Oliveira, M. A. (author)
Format:	article
Language:	English
Published:	2016
Subjects:	2-Cys Prx Peroxiredoxin
Online Access:	https://hdl.handle.net/20.500.12008/22009
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