Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87604
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dc.contributor.authorKamariah, Neelagandanen
dc.contributor.authorSek, Mun Foongen
dc.contributor.authorEisenhaber, Birgiten
dc.contributor.authorEisenhaber, Franken
dc.contributor.authorGrüber, Gerharden
dc.date.accessioned2018-12-03T05:18:48Zen
dc.date.accessioned2019-12-06T16:45:28Z-
dc.date.available2018-12-03T05:18:48Zen
dc.date.available2019-12-06T16:45:28Z-
dc.date.issued2016en
dc.identifier.citationKamariah, 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/srep37610en
dc.identifier.urihttps://hdl.handle.net/10356/87604-
dc.description.abstractIn 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.en
dc.format.extent15 p.en
dc.language.isoenen
dc.relation.ispartofseriesScientific Reportsen
dc.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/en
dc.subjectHydrogen Peroxideen
dc.subjectDRNTU::Science::Biological sciencesen
dc.subjectProkaryotic Cellsen
dc.titleTransition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxinsen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Computer Science and Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1038/srep37610en
dc.description.versionPublished versionen
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