Spectroelectrochemical insights into structural and redox properties of immobilized endonuclease III and its catalytically inactive mutant

Moe E., Rollo F., Silveira C. M., SEZER M., Hildebrandt P., Todorovic S.

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, cilt.188, ss.149-154, 2018 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 188
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1016/j.saa.2017.06.050
  • Dergi Adı: SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.149-154
  • Anahtar Kelimeler: Endonuclease III, 4Fe-4S cluster, Surface enhanced IR absorption, DNA repair, Cyclic voltammetry, Resonance Raman spectroscopy, IRON-SULFUR CLUSTERS, DNA-REPAIR, DEINOCOCCUS-RADIODURANS, CYTOCHROME-C, SUBSTRATE-SPECIFICITY, ELECTRON-TRANSFER, CRYSTAL-STRUCTURE, FREE-RADICALS, GLYCOSYLASE, PROTEIN
  • İstanbul Üniversitesi Adresli: Hayır

Özet

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.