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1.


   
    A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN [Text] / L. Y. Antipina [et al.] // J. Struct. Chem. - 2011. - Vol. 52, Is. 5. - P870-875. - Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213). . - ISSN 0022-4766
РУБ Chemistry, Inorganic & Nuclear + Chemistry, Physical
Рубрики:
CALCIUM-DISCHARGED OBELIN
   SEMIEMPIRICAL METHODS

   1.7 ANGSTROM

   OPTIMIZATION

   PARAMETERS

   MECHANISM

   FLUORESCENCE

   ELEMENTS

   PROTEIN

   EMITTER

Кл.слова (ненормированные):
coelenterazine -- 2-hydroperoxy-coelenterazine -- Obelia longissima -- Renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.

Держатели документа:
[Antipina, L. Yu
Tomilin, F. N.
Ovchinnikov, S. G.] Russian Acad Sci, LV Kirensky Phys Inst, Siberian Div, Krasnoyarsk, Russia
[Vysotskii, E. S.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Antipina, L. Yu
Ovchinnikov, S. G.] MF Reshetnev Siberian State Aerosp Univ, Krasnoyarsk, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Antipina, L.Y.; Tomilin, F.N.; Vysotskii, E.S.; Ovchinnikov, S.G.

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2.


   
    A New Bias Site for Epigenetic Modifications: How Non-Canonical GC Base Pairs Favor Mechanochemical Cleavage of DNA / D. A. Semyonov, I. V. Eltsov, Y. D. Nechipurenko // Bioessays. - 2020. - Vol.: 42, Issue : 11. - Ст. 2000051, DOI 10.1002/bies.202000051. - Cited References:55. - The authors thank Dr. Dmitry M. Graifer, Prof. Vladimir A. Reznikov, and Dr. Anastasia Anashkina, for useful discussion. The authors thank the Prof. D. R. Forsdyke whose advice on improving the style of the manuscript was very useful. This work was supported by the program of the Presidium of the Russian Academy of Sciences for Molecular and Cellular Biology and the Program of Fundamental Research for State Academies for years 2013-2020, project no. 01201363818. The work was supported by the Russian Ministry of Science and High Education (grant #05.604.21.0234, unique number RFMEFI60419X0234) . - ISSN 0265-9247. - ISSN 1521-1878
РУБ Biochemistry & Molecular Biology + Biology
Рубрики:
NUCLEIC-ACIDS
   CYTOSINE

   MUTAGENESIS

   N-4-METHOXYCYTOSINE

Кл.слова (ненормированные):
5-methylcytosines -- mechanochemical cleavage of DNAs -- molecular basis of -- epigenetics -- tautomers -- transient base pairs in DNAs -- wobble base pairs
Аннотация: Properties of non-canonical GC base pairs and their relations with mechanochemical cleavage of DNA are analyzed. A hypothesis of the involvement of the transient GC wobble base pairs both in the mechanisms of the mechanochemical cleavage of DNA and epigenetic mechanisms involving of 5-methylcytosine, is proposed. The hypothesis explains the increase in the frequency of the breaks of the sugar-phosphate backbone of DNA after cytosines, the asymmetric character of these breaks, and an increase in break frequency in CpG after cytosine methylation. As an alternative hypothesis, probable implication of GC(+)Hoogsteen base pairs is considered, which now exemplify the best-studied non-canonical GC base pairs in the DNA double helix. Also see the video abstract here https://youtu.be/EUunVWL0ptw.

WOS,
Файл:  доступ к статье - 0
https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202000051
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Akademgorodok 50, Krasnoyarsk 660036, Russia.
Novosibirsk State Univ, Novosibirsk, Russia.
Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow, Russia.

Доп.точки доступа:
Semyonov, Denis A.; Eltsov, Ilia, V; Nechipurenko, Yury D.; program of the Presidium of the Russian Academy of Sciences for Molecular and Cellular Biology; Program of Fundamental Research for State Academies for years 2013-2020 [01201363818]; Russian Ministry of Science and High Education [05.604.21.0234, RFMEFI60419X0234]

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