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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (1)

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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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    Structural properties of tryptophan microenvironment in bacterial luciferase [Text] / A. A. Deeva, E. V. Nemtseva, V. A. Kratasyuk // Luminescence. - 2014. - Vol. 29. - P72-73. - Cited References: 4 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
FLUORESCENCE
   RESIDUES

WOS
Держатели документа:
[Deeva, Anna A.
Nemtseva, Elena V.
Kratasyuk, Valentina A.] Siberian Fed Univ, Krasnoyarsk, Russia
[Nemtseva, Elena V.
Kratasyuk, Valentina A.] Inst Biophys SB RAS, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deeva, A.A.; Nemtseva, E.V.; Kratasyuk, V.A.

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A circadian rhythm of grazing of microalgae by a laboratory culture of Ceriodaphnia quadrangula [Текст] / V. I. Kolmakov [и др.] // Biofizika. - 2002. - Vol. 47, Is. 4. - P. 673-676. - Cited References: 12 . - ISSN 0006-3029

РУБ Biophysics
Рубрики:
CLOSED CULTIVATORS
FLUORESCENCE
ZOOPLANKTON
Кл.слова (ненормированные):
daily rhythm of grazing -- fluorescence -- microalgae -- flowing-through cultivator -- photoperiod -- statistical spectral analysis
Аннотация: The circadian rhythm of grazing of microalgae by a laboratory culture of Ceriodaphnia quadrangula under continuous illumination was studied by continuous registration of chlorophyll fluorescence at the outlet of a flow-through cultivator. A culture of green alga Chlorella vulgaris was used as a feed. The data obtained were treated by the statistical spectral analysis. It was found that animals preliminarily grown under a 12 h light : 12 h dark regime and transferred to constant light showed two maxima in the circadian rhythm of grazing with periods of 0.7 and 1.1 h. Animals preliminarily grown under constant light showed no circadian rhythm of grazing. It was concluded that the circadian rhythm of grazing of C quadrangula has endogenous nature and can change according to light conditions.

WOS
Держатели документа:
Krasnoyarsk State Univ, Krasnoyarsk 660042, Russia
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kolmakov, V.I.; Levin, L.A.; Dubovskaya, O.P.; Gladyshev, M.I.

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Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin [Text] / N. V. Sablin, M. A. Gerasimova, E. V. Nemtseva // Russ. Phys. J. - 2016. - Vol. 58, Is. 12. - P1797-1803, DOI 10.1007/s11182-016-0719-6. - Cited References:16. - This work was supported in part by the Russian Academy of Sciences (The program "Molecular and Cell Biology", project No. 6.8), the Ministry of Education and Science of the Russian Federation (project No. 1762), and the Federal Agency of scientific organizations of the Russian Federation (project No. VI 57.1.1). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
ROOM-TEMPERATURE
   AQUEOUS-SOLUTION
   PHOSPHORESCENCE
   FLUORESCENCE
   EOSIN
Кл.слова (ненормированные):
erythrosin B -- phosphorescence -- delayed fluorescence -- quantum yield -- phosphorescence lifetime -- bovine serum albumin
Аннотация: Changes in absorption, fluorescence, phosphorescence, and delayed fluorescence spectra of erythrosin B are studied in the presence of bovine serum albumin at room temperature. Spectral and chronoscopic characteristics of the observed photophysical processes are defined. The binding of erythrosin B with the protein followed by spectral changes is demonstrated. Absorption and fluorescence spectra of the dye in the bound state are described, the binding mechanism is analyzed. The binding parameters of the dye-protein complex are estimated.

WOS,
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Держатели документа:
Siberian Fed Univ, Krasnoyarsk, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia.

Доп.точки доступа:
Sablin, N. V.; Gerasimova, M. A.; Nemtseva, E. V.; Russian Academy of Sciences [6.8]; Ministry of Education and Science of the Russian Federation [1762]; Federal Agency of scientific organizations of the Russian Federation [VI 57.1.1]

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