Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87604
Title: Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins
Authors: Kamariah, Neelagandan
Sek, Mun Foong
Eisenhaber, Birgit
Eisenhaber, Frank
Grüber, Gerhard
Keywords: Hydrogen Peroxide
DRNTU::Science::Biological sciences
Prokaryotic Cells
Issue Date: 2016
Source: Kamariah, N., Sek, M. F., Eisenhaber, B., Eisenhaber, F., & Grüber, G. (2016). Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins. Scientific Reports, 6, 37610-. doi:10.1038/srep37610
Series/Report no.: Scientific Reports
Abstract: In addition to their antioxidant function, the eukaryotic peroxiredoxins (Prxs) facilitate peroxide-mediated signaling by undergoing controlled inactivation by peroxide-driven over-oxidation. In general, the bacterial enzyme lacks this controlled inactivation mechanism, making it more resistant to high H2O2 concentrations. During peroxide reduction, the active site alternates between reduced, fully folded (FF), and oxidized, locally unfolded (LU) conformations. Here we present novel insights into the divergence of bacterial and human Prxs in robustness and sensitivity to inactivation, respectively. Structural details provide new insights into sub-steps during the catalysis of peroxide reduction, enabling the transition from an FF to a LU conformation. Complementary to mutational and enzymatic results, these data unravel the essential role of the C-terminal tail of bacterial Prxs to act as a molecular switch, mediating the transition from an FF to a LU state. In addition, we propose that the C-terminal tail has influence on the propensity of the disulphide bond formation, indicating that as a consequence on the robustness and sensitivity to over-oxidation. Finally, a physical linkage between the catalytic site, the C-terminal tail and the oligomer interface is described.
URI: https://hdl.handle.net/10356/87604
http://hdl.handle.net/10220/46764
DOI: http://dx.doi.org/10.1038/srep37610
Rights: © 2016 The Authors (Nature Publishing Group). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
metadata.item.grantfulltext: open
metadata.item.fulltext: With Fulltext
Appears in Collections:SBS Journal Articles

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.