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Spectroelectrochemical insights into structural and redox properties of immobilized endonuclease III and its catalytically inactive mutant
Citation key ISI:000412608600021
Author Moe, Elfin and Rollo, Filipe and Silveira, Celia M. and Sezer, Murat and Hildebrandt, Peter and Todorovic, Smilja
Pages 149-154
Year 2018
ISSN 1386-1425
DOI 10.1016/j.saa.2017.06.050
Volume 188
Month JAN 5
Abstract Endonuclease III is a Fe-S containing bifunctional DNA glycosylase which is involved in the repair of oxidation damaged DNA. Here we employ surface enhanced IR spectroelectrochemistry and electrochemistry to study the enzyme from the highly radiation- and desiccation-resistant bacterium Deinococcus radiodurans (DrEndoill(2)). The experiments are designed to shed more light onto specific parameters that are currently proposed to govern damage search and recognition by endonucleases III. We demonstrate that electrostatic interactions required for the redox activation of DrEndoill(2) may result in high electric fields that alter its structural and thermodynamic properties. Analysis of inactive DrEndollI(2) (K132A/D150A double mutant) interacting with undamaged DNA, and the active enzyme interacting with damaged DNA also indicate that the electron transfer is modulated by subtle differences in the protein-DNA complex. (C) 2017 Elsevier B.V. All rights reserved.
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