Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation
- Авторы: Kanazhevskaya L.1, Smyshlyaev D.2, Alekseeva I.1, Fedorova O.1,2
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Учреждения:
- Institute of Chemical Biology and Fundamental Medicine
- Department of Natural Sciences, Novosibirsk State University
- Выпуск: Том 45, № 6 (2019)
- Страницы: 630-640
- Раздел: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/229276
- DOI: https://doi.org/10.1134/S1068162019060190
- ID: 229276
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Аннотация
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.
Об авторах
L. Kanazhevskaya
Institute of Chemical Biology and Fundamental Medicine
Автор, ответственный за переписку.
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
Россия, Novosibirsk, 630090
D. Smyshlyaev
Department of Natural Sciences, Novosibirsk State University
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
Россия, Novosibirsk, 630090
I. Alekseeva
Institute of Chemical Biology and Fundamental Medicine
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
Россия, Novosibirsk, 630090
O. Fedorova
Institute of Chemical Biology and Fundamental Medicine; Department of Natural Sciences, Novosibirsk State University
Email: Lyubov.Kanazhevskaya@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630090