Главная
Авторизация
Фамилия
Пароль
 

Базы данных


Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска
Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН
Иностранные журналы библиотеки Института биофизики СО РАН
Отечественные журналы библиотеки Института биофизики СО РАН
Каталог диссертаций ИБФ СО РАН
Труды сотрудников ИБФ СО РАН
Область поиска
Формат представления найденных документов:
полныйинформационныйкраткий
Отсортировать найденные документы по:
авторузаглавиюгоду изданиятипу документа
Поисковый запрос: (<.>S=CA2+-REGULATED PHOTOPROTEIN OBELIN<.>)
Общее количество найденных документов : 4
Показаны документы с 1 по 4
1.


   
    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.

WOS,
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]

Найти похожие
2.


   
    Crystal structure of semisynthetic obelin-v / M. D. Larionova, L. J. Wu, E. V. Eremeeva [et al.] // Protein Sci. - 2021, DOI 10.1002/pro.4244. - Cited References:69. - National Natural Science Foundation of China, Grant/Award Number: 32011530076; Russian Foundation for Basic Research, Grant/Award Numbers: 20-04-00085, 20-44-240006, 20-54-53011 . - Article in press. - ISSN 0961-8368. - ISSN 1469-896X
РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
   PHOTOLUMINESCENCE QUANTUM YIELD
Кл.слова (ненормированные):
analog -- bioluminescence -- coelenterazine -- coelenterazine-v -- obelin -- photoprotein -- protein structure
Аннотация: Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca2+-regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca2+-regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 angstrom resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (phi(FL)) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (phi(R)) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (phi(S)). In turn, the low phi(S) value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.

WOS
Держатели документа:
SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia.
ShanghaiTech Univ, iHuman Inst, Ren Bldg,393 Middle Huaxia Rd, Shanghai 201210, Peoples R China.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk, Russia.
ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China.

Доп.точки доступа:
Larionova, Marina D.; Wu, Lijie; Eremeeva, Elena, V; Natashin, Pavel, V; Gulnov, Dmitry, V; Nemtseva, Elena, V; Liu, Dongsheng; Liu, Zhi-Jie; Vysotski, Eugene S.; Eremeeva, Elena; Nemtseva, Elena; Vysotski, Eugene; Gulnov, Dmitry; Natashin, Pavel; Larionova, Marina; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [32011530076]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 20-44-240006, 20-54-53011]

Найти похожие
3.


   
    Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067
РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
   CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

Найти похожие
4.


   
    Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067
РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
   CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

Найти похожие
 
Стандартный
Расширенный
Профессиональный
Распределенный
По словарю
ГРНТИ-навигатор
УДК-навигатор
Тематический навигатор

Другие библиотеки

Библиотека института физики
Центральная научная библиотека КНЦ СО РАН
Библиотека института химии и химический технологии
Библиотека института вычислительного моделирования
Библиотека института леса
Библиотека СФУ
Краевая научная библиотека
© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)