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Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation. / Kanazhevskaya, L. Y.; Smyshlyaev, D. A.; Alekseeva, I. V. и др.

в: Russian Journal of Bioorganic Chemistry, Том 45, № 6, 01.11.2019, стр. 630-640.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Kanazhevskaya, LY, Smyshlyaev, DA, Alekseeva, IV & Fedorova, OS 2019, 'Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation', Russian Journal of Bioorganic Chemistry, Том. 45, № 6, стр. 630-640. https://doi.org/10.1134/S1068162019060190

APA

Kanazhevskaya, L. Y., Smyshlyaev, D. A., Alekseeva, I. V., & Fedorova, O. S. (2019). Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation. Russian Journal of Bioorganic Chemistry, 45(6), 630-640. https://doi.org/10.1134/S1068162019060190

Vancouver

Kanazhevskaya LY, Smyshlyaev DA, Alekseeva IV, Fedorova OS. Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation. Russian Journal of Bioorganic Chemistry. 2019 нояб. 1;45(6):630-640. doi: 10.1134/S1068162019060190

Author

Kanazhevskaya, L. Y. ; Smyshlyaev, D. A. ; Alekseeva, I. V. и др. / Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation. в: Russian Journal of Bioorganic Chemistry. 2019 ; Том 45, № 6. стр. 630-640.

BibTeX

@article{23aa4e8613374bcfa9cd5249973d0275,
title = "Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation",
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.",
keywords = "conformational dynamics, demethylation of DNA, DNA dioxygenase AlkB, pre-steady-state kinetics",
author = "Kanazhevskaya, {L. Y.} and Smyshlyaev, {D. A.} and Alekseeva, {I. V.} and Fedorova, {O. S.}",
year = "2019",
month = nov,
day = "1",
doi = "10.1134/S1068162019060190",
language = "English",
volume = "45",
pages = "630--640",
journal = "Russian Journal of Bioorganic Chemistry",
issn = "1068-1620",
publisher = "MAIK NAUKA/INTERPERIODICA/SPRINGER",
number = "6",

}

RIS

TY - JOUR

T1 - Conformational Dynamics of Dioxygenase AlkB and DNA in the Course of Catalytically Active Enzyme–Substrate Complex Formation

AU - Kanazhevskaya, L. Y.

AU - Smyshlyaev, D. A.

AU - Alekseeva, I. V.

AU - Fedorova, O. S.

PY - 2019/11/1

Y1 - 2019/11/1

N2 - 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.

AB - 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.

KW - conformational dynamics

KW - demethylation of DNA

KW - DNA dioxygenase AlkB

KW - pre-steady-state kinetics

UR - http://www.scopus.com/inward/record.url?scp=85078600637&partnerID=8YFLogxK

U2 - 10.1134/S1068162019060190

DO - 10.1134/S1068162019060190

M3 - Article

AN - SCOPUS:85078600637

VL - 45

SP - 630

EP - 640

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

SN - 1068-1620

IS - 6

ER -

ID: 23318484