Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation
- 作者: Kanazhevskaya L.1, Smyshlyaev D.2, Alekseeva I.1, Fedorova O.1,2
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隶属关系:
- Institute of Chemical Biology and Fundamental Medicine
- Department of Natural Sciences, Novosibirsk State University
- 期: 卷 45, 编号 6 (2019)
- 页面: 630-640
- 栏目: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/229276
- DOI: https://doi.org/10.1134/S1068162019060190
- ID: 229276
如何引用文章
详细
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.
作者简介
L. Kanazhevskaya
Institute of Chemical Biology and Fundamental Medicine
编辑信件的主要联系方式.
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
俄罗斯联邦, Novosibirsk, 630090
D. Smyshlyaev
Department of Natural Sciences, Novosibirsk State University
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
俄罗斯联邦, Novosibirsk, 630090
I. Alekseeva
Institute of Chemical Biology and Fundamental Medicine
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
俄罗斯联邦, Novosibirsk, 630090
O. Fedorova
Institute of Chemical Biology and Fundamental Medicine; Department of Natural Sciences, Novosibirsk State University
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
俄罗斯联邦, Novosibirsk, 630090; Novosibirsk, 630090