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^a621.41.09^2VINITI
И 88

Использование Ca-зависимого фотопротеина обелина в качестве метки в иммунолюминесцентном анализе [Текст] : научное издание / В. Н. Вербов [и др.] // Актуал. вопр. мед. биотехнол.: Матер. науч. конф., посвящ. 85-летию Том. НИИ вакцине и сывороток НПО "Вирион". - Томск, 1991. - Ч. 2. - С. 39-40

ГРНТИ

62.41.09

РУБ 621.41.09
Рубрики:
БЕЛОК
   ФОТОБЕЛОК
   ОБЕЛИН
   CA-ЗАВИСИМЫЙ
   СОЕДИНЕНИЯ-МЕТКА
   ИММУНОХИМИЧЕСКАЯ РЕАКЦИЯ
   ИСПОЛЬЗОВАНИЕ
   OBELIA LONGISSIMA
   PHOTOPROTEIN
Аннотация: В процессе поиска соединений-меток, к-рые при иммунохимической реакции обеспечивают более высокую чувствительность иммунологического анализа, был изучен фотобелок обелин, выделенный из экстрактов люминесцирующего гидроида Obelia longissima. Обелин, взаимодействуя с ионами кальция, способен испускать 4,5* *10{1}{5} кванта света на 1 мг белка, что позволяет обнаружить до 10{-}{2}{0}-10{-}{2}{1} Моль в-ва метки. Россия, НИИ Вакцин и сывороток НПО "Вирион", г. Томск.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Вербов, В.Н.; Высоцкий, Е.С.; Бондарь, В.С.; Артюхов, А.И.; Летунов, В.Н.; Мартюшин, С.В.

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^a314.23.27.07.11^2VINITI
В 93

Высоцкий, Евгений Степанович.
Выделение и свойства различных молекулярных форм Ca{2}{+}-активируемого фотопротеина обелина [Текст] : научное издание / Е. С. Высоцкий, В. С. Бондарь, И. И. Гительзон // Докл. АН СССР. - 1991. - Т. 321, N 1. - С. 214-217 . - ISSN 0002-3264

ГРНТИ

31.23.27

РУБ 314.23.27.07.11
Рубрики:
ФОТОПРОТЕИН
   CA-АКТИВИРУЕМЫЙ
   ОБЕЛИН
   ВЫДЕЛЕНИЕ
   СВОЙСТВА
   CA-ACTIVATED PHOTOPROTEIN
   OBELIN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, Владимир Станиславович; Гительзон, Иосиф Исаевич

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^a314.23.27.07.11^2VINITI
В 93

Высоцкий, Е. С.
Выделение и очистка Ca-зависимого фотопротеина - обелина из гидроидных полипов Obelia longissima [Текст] : научное издание / Е. С. Высоцкий, В. С. Бондарь, В. Н. Летунов // Биохимия. - 1989. - Т. 54, N 6. - С. 965-973 . - ISSN 0320-9725

ГРНТИ

31.23.27

РУБ 314.23.27.07.11
Рубрики:
ФОТОПРОТЕИН
   КАЛЬЦИЙ-ЗАВИСИМЫЙ
   ОБЕЛИН
   ВЫДЕЛЕНИЕ
   ОЧИСТКА
   OBELIA LONGISSIMA
   ПОЛИПЫ ГИДРОИДНЫЕ
   OBELIN
   CA-ACTIVATED PHOTOPROTEIN
   EXTRACTION/PURIFICATION
   HYDROID POLYPS
   BIOLUMINESCENCE
Аннотация: Описан способ выделения и очистки Ca-зависимого фотопротеина - обелина из гидроидных полипов Obelia longissima, включающий: разрушение материала в гипотонич. буфере, фракционирование ПЭГ 6000, фракционирование (NH[4])[2]SO[4] в диапазоне 40-75% насыщения, хроматографию на ДЭАЭ-целлюлозе DE-52, хроматографию на фенил-сефарозе 4В, гель-фильтрацию на сефадексе G-75, гель-фильтрацию на колонке Superose 12 HR 10/30 при помощи системы FPLC. С помощью предложенного метода получен практически чистый обелин с выходом 30-40%. Мол. м. полученного белка, определенная гель-фильтрацией в неденатурирующих условиях, составляет 39,6 кДа, тогда как электрофорез в полиакриламидном геле с додецилсульфатом натрия показывал наличие двух белков с мол. м. 27 и 15,6 кДа соответственно. Библ. 28. Ин-т биофизики СО АН СССР, Красноярск, СССР
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Летунов, В.Н.

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^a314.23.27.07.11^2VINITI
Б 81

Бондарь, В. С.
Физико-химические свойства фотопротеина из гидроидного полипа Obelia longissima [Текст] : научное издание / В. С. Бондарь, К. П. Трофимов, Е. С. Высоцкий // Биохимия. - 1992. - Т. 57, N 10. - С. 78 . - ISSN 0320-9725

ГРНТИ

31.23.27

РУБ 314.23.27.07.11
Рубрики:
ФОТОПРОТЕИНЫ
   ФИЗИКО-ХИМИЧЕСКИЕ СВОЙСТВА
   ГИДРОИДНЫЕ ПОЛИПЫ
   PHOTOPROTEIN PROPERTIES
Аннотация: Из гидроидов вида Obelia longissima по схеме, включающей гель-фильтрацию на Сефадексе G-75 (fine), ИОХ на Полисил СА-300 (10 мкм), гидрофобную хр-фию на фенил-Сефарозе CL-4В, гель-фильтрацию на Сефакриле S-200 (Superfine), ИОХ на колонке Mono Q при pH 7,0, хроматофокусирввание на колонке MonoP (градиент pH 6,0-4,0) ИОХ на колонке Mono Q при pH 5,5; 8,8; 7,0 выделен гомогенный (по данным ЭФ с DDC-Na) фотопротеин обелин. Мол. м. белка в нативных условиях составляет 30 кД, в присутствии DDC-Na-19,8 кД. Уд. акт. обелина равна 4,9*10{1}{5} квант на 1 мг белка; константа псевдопер.З064 вого порядка спада биолюминесценции - 4 с{-}{1}; квантовый выход - 0,16. Интервал измерения ионов кальция составляет 10{-}{7}-10{-}{5} М. Для обелина характерен спектр люминесценции с максимумом при 469 нм, спектральный максимум флуоресценции разряженного фотопротеина находится при 455 нм. Оптимум pH люминесценции обелина приходится на интервал 9,0-10,5. Молек. константы ионизации имеют значения pK[1] 6,8 и pK[2] 12,2; константы ионизации для активного центра - pK[1] 9,1 и pK[2] 10,2 соотв. Библ. 36. Россия, ин-т биофизики СО РАН, Красноярск.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Трофимов, К.П.; Высоцкий, Е.С.

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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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Violet and greenish photoprotein obelin mutants for reporter applications in dual-color assay [Text] / L. A. Frank [et al.] // Anal. Bioanal. Chem. - 2008. - Vol. 391, Is. 8. - P2891-2896, DOI 10.1007/s00216-008-2223-5. - Cited References: 22 . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   BIOLUMINESCENCE
   AEQUORIN
   IMMUNOASSAY
   EXPRESSION
   CDNA
   PURIFICATION
   CLONING
Кл.слова (ненормированные):
Ca(2+)-regulated photoprotein -- bioluminescence -- dual-color assay
Аннотация: Two kinds of Ca(2+)-regulated photoprotein obelin with altered color of bioluminescence were obtained by active-center amino acid substitution. The mutant W92F-H22E emits violet light (lambda(max)=390 nm) and the mutant Y139F emits greenish light (lambda (max)=498 nm), with small spectral overlap, both display high activity and stability and thus may be used as reporters. For demonstration, the mutants were applied in dual-color simultaneous immunoassay of two gonadotropic hormones-follicle-stimulating hormone and luteinizing hormone. Bioluminescence of the reporters was simultaneously triggered by single injection of Ca(2+) solution, divided using band-pass optical filters and measured with a two-channel photometer. The sensitivity of simultaneous bioluminescence assay was close to that of a separate radioimmunoassay.

Держатели документа:
[Frank, Ludmila A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Frank, Ludmila A.
Borisova, Vasilisa V.
Markova, Svetlana V.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Markova, S.V.; Malikova, N.P.; Stepanyuk, G.A.; Vysotski, E.S.

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Use of proZZ-obelin fusion protein in bioluminescent immunoassay [Text] / L. A. Frank, V. A. Illarionova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 1996. - Vol. 219, Is. 2. - P475-479, DOI 10.1006/bbrc.1996.0258. - Cited References: 21 . - 5. - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
   EXPRESSION
   AEQUORIN
   PURIFICATION
   SYSTEM
Аннотация: Obelin is a photoprotein that emits light by Ca2+-binding. To develop a bioluminescent immunoassay based on the light emission property of obelin, we have expressed the apoobelin fusion protein with ZZ-domain of S. aureus protein A in E. coil by recombinant DNA techniques. The pro2Z-obelin expressed was purified by one-step affinity chromatography on IgG-Agarose. The purified proZZ-obelin has both the luminescent activity of obelin and the IgG-binding ability of ZZ-domain. The specific activity of fusion protein was 8.5 x 10(15) photons per mg of protein. (C) 1996 Academic Press, Inc.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Illarionova, V.A.; Vysotski, E.S.

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Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory / F. N. Tomilin, A. V. Rogova, L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2021. - Vol. 20, Is. 4. - P559-570, DOI 10.1007/s43630-021-00039-5 . - ISSN 1474-905X
Кл.слова (ненормированные):
Absorption spectra -- Absorption spectroscopy -- Blue shift -- Dihedral angle -- Substrates -- Absorption maxima -- Covalently bound -- Electronic excitation -- Linear scaling -- Mechanical methods -- Substrate complexes -- Time dependent density functional theory -- Visible absorption spectra -- Density functional theory
Аннотация: Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460–470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein–substrate complex was optimized using a linear scaling quantum–mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60° of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified. © 2021, The Author(s), under exclusive licence to European Photochemistry Association,European Society for Photobiology.

Scopus
Держатели документа:
Kirensky Institute of Physics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/38, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodny 79 pr., Krasnoyarsk, 660041, Russian Federation
National Research Tomsk State University, Lenin Avenue 36, Tomsk, 634050, Russian Federation
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation
Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, South Korea
Research Center for Computational Design of Advanced Functional Materials (CD-FMat), National Institute of Advanced Industrial Science and Technology (AIST), Central 2, Umezono 1-1-1, Tsukuba, 305-8568, Japan

Доп.точки доступа:
Tomilin, F. N.; Rogova, A. V.; Burakova, L. P.; Tchaikovskaya, O. N.; Avramov, P. V.; Fedorov, D. G.; Vysotski, E. S.

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РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

Аннотация: Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460-470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein-substrate complex was optimized using a linear scaling quantum-mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60 degrees of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Kirensky Inst Phys SB RAS, Akademgorodok 50-38, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny 79 Pr, Krasnoyarsk 660041, Russia.
Natl Res Tomsk State Univ, Lenin Ave 36, Tomsk 634050, Russia.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Inst Biophys SB RAS, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Kyungpook Natl Univ, 80 Daehakro, Daegu 41566, South Korea.
Natl Inst Adv Ind Sci & Technol, Res Ctr Computat Design Adv Funct Mat CD FMat, Cent 2,Umezono 1-1-1, Tsukuba, Ibaraki 3058568, Japan.

Доп.точки доступа:
Tomilin, Felix N.; Rogova, Anastasia V.; Burakova, Ludmila P.; Tchaikovskaya, Olga N.; Avramov, Pavel V.; Fedorov, Dmitri G.; Vysotski, Eugene S.; Burakova, Lyudmila; Vysotski, Eugene; Anastasia, Rogova; Tomilin, Felix; RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]; NSFCNational Natural Science Foundation of China (NSFC) [19-54-53004]; Russian Ministry of Science and EducationMinistry of Education and Science, Russian Federation [0721-2020-0033]

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10.

Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation / L. P. Burakova, M. S. Lyakhovich, K. S. Mineev [et al.] // Org. Lett. - 2021. - Vol. 23, Is. 17. - P6846-6849, DOI 10.1021/acs.orglett.1c02410. - Cited References:20. - This work was supported by grant 20-04-00085 of the Russian Foundation for Basic Research, grant 20-44-242003 of the Russian Foundation for Basic Research, Krasnoyarsk Territory, and Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds, grant 17-1401169p of the Russian Science Foundation, and the President of Russian Federation grant for Leading Scientific Schools LS-2605.2020.4 in part of structural elucidation of native products and organic synthesis. We thank Konstantin Antonov (IBCh RAS) and Igor Ivanov (IBCh RAS) for the registration of HRMS spectra. . - ISSN 1523-7060. - ISSN 1523-7052

РУБ Chemistry, Organic
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENCE
   OBELIN
   RESIDUES
   BINDING
Аннотация: Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photo-inactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Lyakhovich, Maria S.; Mineev, Konstantin S.; Petushkov, Valentin N.; Zagitova, Renata, I; Tsarkova, Aleksandra S.; Kovalchuk, Sergey, I; Yampolsky, Ilia, V; Vysotski, Eugene S.; Kaskova, Zinaida M.; Mineev, Konstantin; Tsarkova, Aleksandra; Vysotski, Eugene; Kaskova, Zinaida; Burakova, Lyudmila; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085]; Russian Foundation for Basic Research, Krasnoyarsk Territory [20-44-242003]; Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds; Russian Science FoundationRussian Science Foundation (RSF) [17-1401169p]; Russian FederationRussian Federation [LS-2605.2020.4]

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11.

Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+-regulated Photoproteins of Different Organisms / E. V. Eremeeva [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P495-502, DOI 10.1111/php.12664. - Cited References:55. - This work was supported by RFBR grant 14-04-31092 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 01201351504 and 01201351502). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
AEQUORIN BIOLUMINESCENCE
SEQUENCE-ANALYSIS
Аннотация: Upon binding their metal ion cofactors, Ca2+-regulated photoproteins display a rapid increase of light signal, which reaches its peak within milliseconds. In the present study, we investigate bioluminescence kinetics of the entire photoprotein family. All five recombinant hydromedusan Ca2+-regulated photoproteinsaequorin from Aequorea victoria, clytin from Clytia gregaria, mitrocomin from Mitrocoma cellularia and obelins from Obelia longissima and Obelia geniculatademonstrate the same bioluminescent kinetics pattern. Based on these findings, for the first time we propose a unanimous kinetic model describing the bioluminescence mechanism of Ca2+-regulated photoproteins.

WOS,
Смотреть статью
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Theoret Biophys Lab, Krasnoyarsk, Russia.
Wageningen Univ & Res, Biochem Lab, Wageningen, Netherlands.

Доп.точки доступа:
Eremeeva, Elena V.; Bartsev, Sergey I.; van Berkel, Willem J. H.; Vysotski, Eugene S.; RFBR [14-04-31092]; Russian Academy of Sciences [01201351504, 01201351502]

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12.

Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa / M. D. Larionova, S. V. Markova, E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P503-510, DOI 10.1111/php.12694. - Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.

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Смотреть статью
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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13.

Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria [Text] / E. V. Eremeeva, E. S. van Berkel, E. S. Vysotski // FEBS Lett. - 2016. - Vol. 590, Is. 3. - P307-316, DOI 10.1002/1873-3468.12052. - Cited References:34. - This study was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0014-5793. - ISSN 1873-3468

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
ENERGY-TRANSFER
CA2+-REGULATED
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine -- FRET -- obelin -- protein-protein -- interaction
Аннотация: Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.

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Scopus
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Wageningen Univ, Biochem Lab, NL-6700 AP Wageningen, Netherlands.

Доп.точки доступа:
Eremeeva, Elena V.; van Berkel, Willem J. H.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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14.

Three-dimensional structures of mutants of Ca2+-regulated photoprotein obelin provide insight into molecular mechanisms underlying changes in bioluminescent properties [Text] / P. . Natashin, E. . Vysotski, Z. J. Liu // Luminescence. - 2014. - Vol. 29. - P36-36. - Cited References: 2 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Natashin, Pavel
Vysotski, Eugene] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China
[Natashin, Pavel
Vysotski, Eugene] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk, Russia
[Liu, Zhi-Jie] Shanghai Tech Univ, iHuman Inst, Shanghai, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P...; Vysotski, E...; Liu, Z.J.

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15.

The recombinant Ca(2+)-regulated photoprotein berovin from Beroe abyssicola displays in vitro both luciferase and photoprotein activities [Text] / L. P. Burakova [et al.] // Luminescence. - 2006. - Vol. 21, Is. 5. - P272-272. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
RAS, SB, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Bayer HealthCare, Global Drug Discovery Target Res, D-42096 Wuppertal, Germany
Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Burakova, L.P.; Markova, S.V.; Golz, S...; Frank, L.A.; Vysotski, E.S.

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16.

The photoprotein obelin as a bioluminescent reporter to monitor protein-protein interactions in vivo and in vitro by protein-fragment complementation assays [Text] / S. V. Markova, P. V. Natashin, E. S. Vysotski // J. Biotechnol. - 2010. - Vol. 150: 14th International Biotechnology Symposium and Exhibition (IBS-2008) (SEP 14-18, 2010, Rimini, ITALY). - S93-S93, DOI 10.1016/j.jbiotec.2010.08.241. - Cited References: 0 . - ISSN 0168-1656

РУБ Biotechnology & Applied Microbiology

Кл.слова (ненормированные):
Bioluminescence -- Reporter -- Obelin -- Protein-protein interactions

Держатели документа:
[Markova, S. V.
Vysotski, E. S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Moscow 117901, Russia
[Markova, S. V.
Natashin, P. V.] Siberian Fed Univ, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Natashin, P.V.; Vysotski, E.S.

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17.

THE MAIN FUNCTION OF HIS175, TRP179, AND TYR190 RESIDUES OF THE OBELIN BINDING SITE IS TO STABILIZE THE HYDROPEROXYCOELENTERAZINE INTERMEDIATE [Text] / E. V. Eremeeva [et al.] ; ed. AA Szalay [et al.] // BIOLUMINESCENCE AND CHEMILUMINESCENCE: CHEMISTRY, BIOLOGY AND APPLICATIONS : WORLD SCIENTIFIC PUBL CO PTE LTD, 2007. - 14th International Symposium on Bioluminescence and Chemiluminescence (OCT 15-19, 2006, San Diego, CA). - P7-10, DOI 10.1142/9789812770196_0002. - Cited References: 7 . - ISBN 978-981-270-816-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Applied
Рубрики:
PHOTOPROTEIN OBELIN
BIOLUMINESCENCE

Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Frank, L. A.
Vysotski, E. S.] Inst Biophys SB RAS, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Vysotski, E.S.; Szalay, AA \ed.\; Hill, PJ \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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18.

The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein / S. V. Markova [et al.] // FEBS J. - 2012. - Vol. 279, Is. 5. - P856-870, DOI 10.1111/j.1742-4658.2012.08476.x. - Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany). . - ISSN 1742-464X

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   C-TERMINAL PROLINE
   SEQUENCE-ANALYSIS
   MNEMIOPSIS-SP
   COELENTERAZINE-BINDING
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURES
   EXCITED-STATE
   CDNA CLONING
Кл.слова (ненормированные):
bioluminescence -- calcium -- coelenterazine -- luciferase -- mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Malikova, Natalia P.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Dept Biophys, Krasnoyarsk, Russia
[Golz, Stefan] Bayer Pharma AG, Global Drug Discovery, Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Golz, S...; Malikova, N.P.; Frank, L.A.; Vysotski, E.S.

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19.

The isospecies of Ca(2+)-regulated photoprotein bolinopsin from Bolinopsis infundibulum [Text] / L. P. Burakova [et al.] // Luminescence. - 2006. - Vol. 21, Is. 5. - P273-273. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
RAS, SB, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Bayer HealthCare, Global Drug Discovery Target Res, D-42096 Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Burakova, L.P.; Markova, S.V.; Golz, S...; Frank, L.A.; Vysotski, E.S.

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20.

The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding [Text] / E. V. Eremeeva [et al.] // FEBS Lett. - 2009. - Vol. 583, Is. 12. - P1939-1944, DOI 10.1016/j.febslet.2009.04.043. - Cited References: 28. - We thank Prof. John Lee for valuable suggestions and providing constructive criticisms. The work was supported by Wageningen University Sandwich PhD-Fellowship Program, Grants 02.512.12. 2006 and 1211.2008.4 of Ministry of Education and Science of Russian Federation, MCB Program of RAS, and by Grant No. 2 of SB RAS. . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
CRYSTAL-STRUCTURE
   CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   CALCIUM
   REGENERATION
   APOAEQUORIN
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Photoprotein -- Trp fluorescence
Аннотация: The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Westphal, Adrie H.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Westphal, A.H.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.; Wageningen University Sandwich PhD-Fellowship Program [02.512.12. 2006]; Ministry of Education and Science of Russian Federation, MCB Program of RAS [1211.2008.4]; SB RAS

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