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

被引：3
|
作者：
Kanazhevskaya, L. Y. [1 ]
Smyshlyaev, D. A. [2 ]
Alekseeva, I., V [1 ]
Fedorova, O. S. [1 ,2 ]
机构：
[1] Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia
[2] Novosibirsk State Univ, Dept Nat Sci, Novosibirsk 630090, Russia
来源：
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY | 2019年 / 45卷 / 06期
基金：
俄罗斯科学基金会;
关键词：
DNA dioxygenase AlkB; demethylation of DNA; conformational dynamics; pre-steady-state kinetics; OXIDATIVE DEMETHYLATION; CRYSTAL-STRUCTURES; PROTEIN DYNAMICS; REPAIR; DAMAGE; METHYLATION; RNA;
D O I：
10.1134/S1068162019060190
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：630 / 640
页数：11
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