Thermodynamics of the DNA repair process by endonuclease VIII

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4 Citations (Scopus)

Abstract

In the present work, a thermodynamic analysis of the interaction between endonuclease VIII (Endo VIII) and model DNA substrates containing damaged nucleotides, such as 5,6-dihydrouridine and 2-hydroxymethyl- 3-hydroxytetrahydrofuran (F-site), was performed. The changes in the fluorescence intensity of the 1,3-diaza-2-oxophenoxazine (tCO) residue located in the complementary chain opposite to the specific site were recorded in the course of the enzyme-substrate interaction. The kinetics was analyzed by the stopped-flow method at different temperatures. The changes of standard Gibbs free energy, enthalpy, and entropy of sequential steps of DNA substrate binding, as well as activation enthalpy and entropy for the transition complex formation of the catalytic stage, were calculated. The comparison of the kinetic and thermodynamic data characterizing the conformational transitions of enzyme and DNA in the course of their interaction made it possible to specify the nature of the molecular processes occurring at the stages of substrate binding, recognition of the damaged base, and its removal from DNA.

Translated title of the contributionТермодинамические параметры взаимодействия эндонуклеазы VIII с поврежденной ДНК
Original languageEnglish
Pages (from-to)29-37
Number of pages9
JournalActa Naturae
Volume11
Issue number1
DOIs
Publication statusPublished - 1 Jan 2019

Keywords

  • DNA glycosylase
  • Kinetic mechanism
  • Pre-steady-state kinetics
  • Thermodynamics
  • pre-steady-state kinetics
  • thermodynamics
  • LESION RECOGNITION
  • BINDING
  • kinetic mechanism

State classification of scientific and technological information

  • 34 BIOLOGY

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