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 Найдено в других БД:Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (1)
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1.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : 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).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): 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.
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2.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deeva A.A., Nemtseva E.V., Kratasyuk V.A.
Заглавие : Structural properties of tryptophan microenvironment in bacterial luciferase
Колич.характеристики :2 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29. - С. 72-73. - ISSN 1522-7235. - ISSN 1522-7243
Примечания : Cited References: 4
Предметные рубрики: FLUORESCENCE
RESIDUES
WOS
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3.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kolmakov V.I., Levin L.A., Dubovskaya O.P., Gladyshev M.I.
Заглавие : A circadian rhythm of grazing of microalgae by a laboratory culture of Ceriodaphnia quadrangula
Колич.характеристики :4 с
Место публикации : Biofizika: MEZHDUNARODNAYA KNIGA, 2002. - Vol. 47, Is. 4. - P673-676. - ISSN 0006-3029
Примечания : Cited References: 12
Предметные рубрики: CLOSED CULTIVATORS
FLUORESCENCE
ZOOPLANKTON
Ключевые слова (''Своб.индексиров.''): 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
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4.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sablin N. V., Gerasimova M. A., Nemtseva E. V.
Заглавие : Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin
Колич.характеристики :7 с
Коллективы : 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]
Место публикации : Russ. Phys. J.: SPRINGER, 2016. - Vol. 58, Is. 12. - С. 1797-1803. - ISSN 1064-8887, DOI 10.1007/s11182-016-0719-6. - ISSN 1573-9228(eISSN)
Примечания : 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).
Предметные рубрики: ROOM-TEMPERATURE
AQUEOUS-SOLUTION
PHOSPHORESCENCE
FLUORESCENCE
EOSIN
Ключевые слова (''Своб.индексиров.''): 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.
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