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^a343.17.09.05^2VINITI
Б 81

Бондарь, В. С.
Люминесценция in vitro экстрактов из полихет Arotonoe vittata [Текст] : научное издание / В. С. Бондарь, С. В. Вологина, Е. С. Высоцкий ; Академия наук СССР. Сибирское отделение. Институт биофизики, АН СССР. СО. Ин-т биофиз. // Препр. - 1991. - N 164. - С. 1-17

ГРНТИ

34.17.09

РУБ 343.17.09.05
Рубрики:
ЛЮМИНЕСЦЕНЦИЯ
   ПОЛИХЕТЫ
   ЭКСТРАКТЫ
   LUMINESCENCE
Аннотация: Исследована люминесценция экстрактов из полихет Arotonoe vittata. Но гомогенатах, полученных из элитр животных, показано, что биолюминесцентная система полихет данного вида относится к фотопротеиновому типу и стимулируется in vitro как О[2]{-} при использовании реагентов Фентона, так и при {-}ОС1 анионом при использовании гипохлорита натрия. Определены величины K[m] для реагентов Фентона в люминесцентной реакции, которые составили 0,37 мМ для FeSO[4] и 8,20 мМ для Н[2]О[2]. Аскорбат (1 и 10 мМ) ингибировал люминесценцию, инициированную реагентами Фентона, тогда как диэтилдитиокарбамат (0,1; 1,0 и 10 мМ) - увеличивал. Показано, что люминесценция экстрактов протекает с существенно большим квантовым выходом при стимуляции ее {-}OCl анионом по сравнению с О[2]{-}. Константы псевдопервого порядка спада люминесцентной реакции составили 0,34 с{-1} для NaOCl и 5,63 с{-1} для реагентов Фентона. Ни аскорбат, ни диэтилдитиокарбамат практически не влияли на люминесценцию, инициированную гипохлоритом натрия
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Вологина, С.В.; Высоцкий, Е.С.; Академия наук СССР. Сибирское отделение. Институт биофизики

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^a343.17.09.05^2VINITI
Л 94

Люминесценция Ca{2}{+}-активируемого фотопротеина обелина под действием активных форм кислорода [Текст] : научное издание / Е. С. Высоцкий [и др.] // Докл. АН СССР. - 1991. - Т. 321, N 4. - С. 850-854 . - ISSN 0002-3264

ГРНТИ

34.17.09

РУБ 343.17.09.05
Рубрики:
БЕЛОК
   ОБЕЛИН
   КАЛЬЦИЙ-АКТИВИРУЕМЫЙ
   ЛЮМИНЕСЦЕНЦИЯ
   КИСЛОРОД АКТИВНЫЙ
   КИШЕЧНОПОЛОСТНЫЕ
   PROTEIN
   LUMINESCENCE
   ACTION OXYGEN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Высоцкий, Евгений Степанович; Бондарь, Владимир Станиславович; Трофимов, К. П.; Гительзон, Иосиф Исаевич

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Ligand binding and conformational states of the photoprotein obelin / E. V. Eremeeva [et al.] // FEBS Lett. - 2012. - Vol. 586, Is. 23. - P4173-4179, DOI 10.1016/j.febslet.2012.10.015. - Cited References: 24. - The work was supported by RFBR grant 12-04-00131, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.058), by the Program "Molecular and Cellular Biology" of RAS. The Wageningen University Sandwich PhD-Fellowship Program supported E.V.E. . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   LIGHT-EMISSION
   APO-AEQUORIN
   BIOLUMINESCENCE
   COELENTERAZINE
   LUMINESCENCE
   STABILITY
   ANGSTROM
   PROTEINS
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Thermostability
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Westphal, Adrie H.
van Mierlo, Carlo P. M.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Vysotski, Eugene S.] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Vysotski, E.S.; Westphal, A.H.; van Mierlo, CPM; van Berkel, WJH

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Cloning and expression of cDNA for a luciferase from the marine copepod Metridia longa - A novel secreted bioluminescent reporter enzyme [Text] / S. V. Markova [et al.] // J. Biol. Chem. - 2004. - Vol. 279, Is. 5. - P3212-3217, DOI 10.1074/jbc.M309639200. - Cited References: 37 . - ISSN 0021-9258

РУБ Biochemistry & Molecular Biology
Рубрики:
VARGULA-HILGENDORFII LUCIFERASE
   GREEN FLUORESCENT PROTEIN
   GENE-EXPRESSION
   FIREFLY LUCIFERASE
   PROMOTER ACTIVITY
   MAMMALIAN-CELLS
   RECEPTOR
   CANCER
   PHOTOPROTEINS
   LUMINESCENCE
Аннотация: Metridia longa is a marine copepod from which a blue bioluminescence originates as a secretion from epidermal glands in response to various stimuli. We demonstrate that Metridia luciferase is specific for coelenterazine to produce blue light (lambda(max)=480 nm). Using an expression cDNA library and functional screening, we cloned and sequenced the cDNA encoding the Metridia luciferase. The cDNA is an 897-bp fragment with a 656-bp open reading frame, which encodes a 219-amino acid polypeptide with a molecular weight of 23,885. The polypeptide contains an N-terminal signal peptide of 17 amino acid residues for secretion. On expression of the Metridia luciferase gene in mammalian Chinese hamster ovary cells the luciferase is detected in the culture medium confirming the existence of a naturally occurring signal peptide for secretion in the cloned luciferase. The novel secreted luciferase was tested in a practical assay application in which the activity of A2a and NPY2 G-protein-coupled receptors was detected. These results clearly suggest that the secreted Metridia luciferase is well suited as a reporter for monitoring gene expression and, in particular, for the development of novel ultra-high throughput screening technologies.

Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Bayer AG, Pharma Res Mol Screening Technol, D-42096 Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Golz, S...; Frank, L.A.; Kalthof, B...; Vysotski, E.S.

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Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species [Text] / E. S. Vysotski [et al.] // Biochemistry. - 2003. - Vol. 42, Is. 20. - P6013-6024, DOI 10.1021/bi027258h. - Cited References: 45 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CALCIUM
   LUMINESCENCE
   LONGISSIMA
   EVOLUTION
   PROTEINS
   COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA USA
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia
Univ Washington, Friday Harbor Labs, Seattle, WA 98195 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Liu, Z.J.; Markova, S.V.; Blinks, J.R.; Deng, L...; Frank, L.A.; Herko, M...; Malikova, N.P.; Rose, J.P.; Wang, B.C.; Lee, J...

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Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator [Text] / B. A. Illarionov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P223-249. - Cited References: 58 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
PHOTOPROTEIN OBELIN
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   DIRECTED MUTAGENESIS
   SEQUENCE-ANALYSIS
   HYDROID OBELIA
   AEQUORIN
   PROTEIN
   BIOLUMINESCENCE
   LUMINESCENCE

Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Univ Washington, Friday Harbor Labs, Friday Harbor, WA 98250 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarionov, B.A.; Frank, L.A.; Illarionova, V.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.

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Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2015. - Vol. 51, Is. 4. - P419-424, DOI 10.1134/S0003683815040110. - Cited References:35. - The authors are grateful to N. V. Psurtseva (curator of the collection of basidiomycetes of the Botanical Institute, Russian Academy of Science) for help with the species affiliation of the IBSO 2328 culture. This work was supported by the Program of Interdisciplinary Projects of the Siberian Branch of the Russian Academy of Sciences, project no. 71. . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
OXIDATIVE STRESS
   SYSTEM
   FUNGI
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
basidiomycetes -- luminescence -- peroxidase -- catalase
Аннотация: The peroxidase and catalase activities in the mycelium of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in normal conditions and under stress were compared. An increase in the luminescence level was observed under stress, as well as an increase in peroxidase and catalase activities. Moreover, the peroxidase activity in extracts of A. borealis mycelium was found to be almost one and a half orders of magnitude lower, and the catalase activity more than two orders of magnitude higher in comparison with the N. nambi mycelium. It can be suggested that the difference between the brightly luminescent and dimly luminescent mycelium of N. nambi is due to the content of (HO2)-O-2 or other peroxide compounds.

WOS,
Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogil'naya, O. A.; Ronzhin, N. O.; Medvedeva, S. E.; Bondar', V. S.; Siberian Branch of the Russian Academy of Sciences [71]

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Growth and light emission of luminous basidiomycetes cultivated on solid media and in submerged culture [Text] / S. E. Medvedeva [et al.] // Mycosphere. - 2014. - Vol. 5, Is. 4. - P565-577, DOI 10.5943/mycosphere/5/4/9. - Cited References:23. - This study was supported by grant No. 11.G34.31.058 (RF Government) and Projects No. 71 and No. 38 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
MYCELIAL GROWTH
   PANELLUS-STYPTICUS
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
luminescence -- luminous higher fungi -- mycelium
Аннотация: There are higher fungi that emit visible light; however, little is known about their requirements for good growth and bright luminescence. Knowledge of these requirements is extremely important for maintaining fungal cultures in laboratory conditions and preparation of luminous mycelia for research purposes. Luminous higher fungi Panellus stipticus, Armillaria sp. and Neonothopanus nambi isolated from different climatic areas and maintained in CCIBSO 836 (Collection of IBP SB RAS, Russia) were used for experiments. Techniques for static and submerged cultivation of mycelia of higher fungi have been developed and optimized for the production of samples of aerial and globular mycelia with prolonged and stable luminescence. We investigated the growth characteristics and luminescence of mycelia cultivated in/on different nutrient media, and the effects of deionized water and mechanical damage on the light emission of mycelia. An increase in luminescence intensity of fungal mycelia can be obtained during cultivation of fungi on a nutrient medium with a certain composition. A significant increase in light emission from N. nambi mycelium can also be obtained after its incubation in water and mechanical damage. The light emission from N. nambi mycelium was greatly enhanced after these treatments, in contrast to the mycelia of Armillaria sp. or P. stipticus. Cultivation conditions that enable growing mycelia with high levels of luminescence will expedite further studies to gain a better understanding of fungal bioluminescence.

WOS
Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Medvedeva, S. E.; Artemenko, K. S.; Krivosheenko, A. A.; Rusinova, A. G.; Rodicheva, E. K.; Puzyr, A. P.; Bondar, V. S.; RF Government [11.G34.31.058]; SB RAS [71, 38]

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