Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation

L. Y. Kanazhevskaya, D. A. Smyshlyaev, I. V. Alekseeva, O. S. Fedorova

Research output: Contribution to journalArticlepeer-review

Abstract

Fe2+/2-ketoglutarate-dependent DNA-dioxygenase AlkB from Escherichia coli is able to restore the native structure of alkylated DNA bases. The enzymatic process utilizes the molecular oxygen, and proceeds through a mechanism of oxidative dealkylation. Here, the kinetics of conformational changes of AlkB and DNA substrates in the course of binding steps were studied. Nickel and cobalt divalent ions were used instead of Fe2+ as metal cofactors in order to inhibit the catalytic activity of AlkB and to study certain stages leading to the formation of a catalytically active enzyme–substrate complex.

Original languageEnglish
Pages (from-to)630-640
Number of pages11
JournalRussian Journal of Bioorganic Chemistry
Volume45
Issue number6
DOIs
Publication statusPublished - 1 Nov 2019

Keywords

  • conformational dynamics
  • demethylation of DNA
  • DNA dioxygenase AlkB
  • pre-steady-state kinetics

Fingerprint

Dive into the research topics of 'Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation'. Together they form a unique fingerprint.

Cite this