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   Е071
   Б 63

    Франк, Л. А.
    Целентеразин-зависимые биолюминесцентные системы [Текст] = Coelenterazine-dependent bioluminescent systems / Л. А. Франк // Биофизика для экологии и медицины: к 90-летию академика РАН И. И. Гительзона / И. И. Гительзон, Т. Г. Волова, А. Г. Дегерменджи [и др.] ; ред., авт. предисл. Т. Г. Волова. - Новосибирск : Издательство Сибирского отделения Российской академии наук, 2019. - С. 72-87. - Библиогр.: с. 85-87 . - ISBN 978-5-7692-1650-3

УДК

577

574

ББК Е071я43 + Р252.0я43

Кл.слова (ненормированные):
люцифераза

Доп.точки доступа:
Гительзон, Иосиф Исаевич; Волова, Татьяна Григорьевна; Дегерменджи, Андрей Георгиевич; Дегерменджи, Н. Н.; Шевырногов, Анатолий Петрович; Кратасюк, В. А.; Барцев, Сергей иванович; Болсуновский, Александр Яковлевич; Бондарь, Владимир Антонович; Буров, А. Е.; Величко, В. В.; Гладышев, Михаил Иванович; Есимбекова, Е. Н.; Дементьев, Д. В.; Задереев, Егор Сергеевич; Зотина, Т. А.; Косиненко, Сергей Васильевич; Медведева, С. Е.; Петушков, В. Н.; Печуркин, Николай Савельевич; Прокопкин, И. Г.; Пузырь, А. П.; Пуртов, К. В.; Рогозин, Денис Юрьевич; Родионова, Н. С.; Ронжин, Н. О.; Сомова, Лидия Александровна; Тихомиров, Александр Аполлинариевич; Тихомирова, Наталья Александровна; Трифонов, С. В.; Ушакова, Софья Аврумовна; Хромечек, Е. Б.; Шишацкая, Е. И.; Шуваев, А. Н.; Российская академия наук. Сибирское отделение; Институт биофизики(Красноярск)

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^a311.15.03.21^2VINITI
К 32

Квантово-химическое исследование образования 2-гидроперокси-целентеразина в Ca{2+}-регулируемом фотопротеине обелине [Текст] : научное издание / Л. Ю. Антипина [и др.] // Ж. структур. химии. - 2011. - Т. 52, N 5. - С. 900-905. - 19 . - ISSN 0136-7463

ГРНТИ

31.15.03

РУБ 311.15.03.21
Рубрики:
2-ГИДРОПЕРОКСИ-
   ЦЕЛЕНТЕРАЗИН
   ОБРАЗОВАНИЕ
   БЕЛКИ
   ОБЕЛИН
   CA{2+}-РЕГУЛИРУЕМЫЙ
   КВАНТОВОХИМИЧЕСКИЙ РАСЧЕТ
   НЕЭМПИРИЧЕСКИЙ
Аннотация: Ca{2+}-Регулируемый фотопротеин обелин определяет свечение морского гидроида Obelia longissima. Биолюминесценция инициируется кальцием и возникает вследствие окислительного декарбоксилирования связанного с белком субстрата целентеразина. Люцифераза светящегося морского коралла Renilla muelleri (RM) также использует целентеразин в качестве субстрата. Однако в биолюминесценцию этих животных in vivo вовлечено три белка: люцифераза, зеленый флуоресцентный белок и Ca{2+}-регулируемый целентеразин-связывающий белок (coelenterazine-binding protein (CBP)). Фактически, "субстратом" люциферазы RM в биолюминесцентной реакции in vivo является CBP, содержащий одну молекулу прочно связанного целентеразина. Целентеразин становится доступным для реакции с люциферазой и кислорода только после связывания с CBP ионов кальция. В отличие от Ca{2+}-регулируемых фотопротеинов в молекуле CBP не происходит активации кислородом молекулы целентеразина. В работе с помощью квантово-химических методов исследовано поведение субстратов в данных белках. Показано, что целентеразин может образовывать различные таутомерные формы - CLZ(2H) и CLZ(7H). Исследован механизм образования 2-гидропероксицелентеразина. Согласно полученным данным, эти белки используют для реакции различные формы субстратов: в обелине субстрат находится в форме CLZ(2H), из которой и происходит образование гидроперекиси. В RM целентеразин находится в форме CLZ(7H), и поэтому активации кислородом в CBP не происходит
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Антипина, Л.Ю.; Томилин, Ф.Н.; Высоцкий, Е.С.; Овчинников, С.Г.

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   Е071
   Б 63
Е07 / Б 63-ИБФ-КФ


    Биофизика для экологии и медицины: к 90-летию академика РАН И. И. Гительзона [Текст] / И. И. Гительзон, Т. Г. Волова, А. Г. Дегерменджи [и др.] ; ред., авт. предисл. Т. Г. Волова ; Российская академия наук, Сибирское отделение, Институт биофизики (Красноярск). - Новосибирск : Издательство Сибирского отделения Российской академии наук, 2019. - 292, [2] с. : ил., цв. ил. ; 25 см. - Рез. ст. англ. - Библиогр. в конце ст. - 300 экз. - ISBN 978-5-7692-1650-3 : 1635.00 р.
    Содержание:
Гительзон, Иосиф Исаевич. Краткий очерк истории, состояния и перспектив = A short essay on the history, state and prospects of the institute of biophysics FRC KSC SB RAS / И. И. Гительзон. - С .14-23
Медведева, С. Е. Коллекция культур ибсо как база для исследований биолюминесценции й и грибов в ИБФ СО РАН = Culture collection ibso as a basis for research of bioluminescence of bacteria and fungi in IBP SB RAS / С. Е. Медведева. - С .24-39. - Библиогр.: с. 37-39
Гительзон, Иосиф Исаевич. Биолюминесценция Мирового океана = Bioluminescence of the World Ocean / И. И. Гительзон, Л. А. Левин, А. С. Артемкин, Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П. Утюшев Р. Н. - С .40-60. - Библиогр.: с. 60
Другие авторы: Левин Л. А., Артемкин А. С., Утюшев Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П.
Кратасюк, В. А. Бактериальная люцифераза в биолюминесцентном анализе = Bacterial luciferase in bioluminescent analysis / В. А. Кратасюк, Е. Н. Есимбекова. - С .61-71. - Библиогр.: с. 70-71
Франк, Л. А. Целентеразин-зависимые биолюминесцентные системы = Coelenterazine-dependent bioluminescent systems / Л. А. Франк. - С .72-87. - Библиогр.: с. 85-87
Кл.слова: люцифераза
Пуртов, К. В. Изучение химического механизма биолюминесценции грибов = The study of the chemical mechanism of bioluminescence of fungi / К. В. Пуртов, В. Н. Петушков, Н. С. Родионова. - С .88-98. - Библиогр.: с. 98
Родионова, Н. С. Исследование биолюминесценции сибирских почвенных олигохет = Study of siberian bioluminescent earthworms / Н. С. Родионова, А. А. Петушков. - С .99-118. - Библиогр.: с. 116-118
Тихомиров, А. А. Экспериментальные модели замкнутых экосистем с расчетной долей человека как перспективное направление исследований по созданию биолого-технической системы жизнеобеспечения = Experimental models of closed ecosystems with the human calculated limits as a perspective direction of research on the creation of BTLSS / А. А. Тихомиров, С. А. Ушакова, Н. А. Тихомирова, С. В., Величко В. В. Трифонов С. В. - С .119-128. - Библиогр.: с. 128
Другие авторы: Ушакова С. А., Тихомирова Н. А., Трифонов С. В., Величко В. В.
Волова, Татьяна Григорьевна. Управляемый биосинтез: от параметрически управляемых продуцирующих биосистем до новейших биофизических технологий = Controlled biosynthesis: from parametrically controlled producing biosystems to newest biophysical technologies / Т. Г. Волова, Е. И. Шишацкая. - С .129-148. - Библиогр.: с. 147-148
Бондарь, Владимир Станиславович. Биомедицинские приложения наноалмазов взрывного синтеза = Biomedical applications of nanodiamonds of explosive synthesis / В. С. Бондарь, А. П. Пузырь, Н. О. Ронжин, А. В., Буров А. Е. Барон А. В. - С .149-165. - Библиогр.: с. 161-165
Другие авторы: Пузырь А. П., Ронжин Н. О., Барон А. В., Буров А. Е.
Болсуновский, Александр Яковлевич. Применение радиоизотопных методов в институте биофизики СО РАН: от клеток крови до экосистем = Use od radioisotope techniques in the Institute of Biophysics SB RAS: from blood cells to ecosystems / А. Я. Болсуновский, С. В. Косиненко, Т. А. Зотина, Д. В. Дементьев. - С .166-179. - Библиогр.: с. 177-179
Другие авторы: Косиненко С. В., Зотина Т. А., Дементьев Д. В.
Шевырногов, Анатолий Петрович. Биосфера - взгляд сверху (экспрессные методы мониторинга биосферы в ИБФ СО РАН – ХХ–ХХI вв.) = biosphere - a view from space (express methods of the biosphere monitoring in the Institute of Biophysics SB RAS – XX–XXI century) / А. П. Шевырногов. - С .180-193. - Библиогр.: с. 193
Гладышев, Михаил Иванович. Жирные кислоты в экологической биофизике водных систем = Fatty acids in ecological biophysics of aquatic ecosystems / М. И. Гладышев. - С .194-209. - Библиогр.: с. 206-209
Рогозин, Денис Юрьевич. Сравнительное исследование устойчивости стратификации и структуры трофической сети в меромиктических озерах Шира и Шунет (Южная Сибирь, Россия) = Comparative study of the stability of stratification and the food web structure in the meromictic lakes Shira and Shunet (South Siberia, Russia) / Д. Ю. Рогозин, Е. С. Задереев, И. Г. Прокопкин [и др.]. - С .210-247. - Библиогр.: с. 243-247
Другие авторы: Задереев Е. С., Прокопкин И. Г., Толомеев А. П., Бархатов Ю. В., Хромечек Е. Б., Дегерменджи Н. Н., Дроботов А. В., Дегерменджи А. Г.
Печуркин, Николай Савельевич. Непрерывный рост интенсивности энерго-вещественных взаимодействий в эволюции геобиосферы Земли = Transparent growth of the energy/matter interactions on Earth in the evolution of geobiosphere / Н. С. Печуркин, А. Н. Шуваев, Л. А. Сомова. - С .248-254
Барцев, Сергей Иванович. Малоразмерные модели биосферы и феноменология изменения глобального климата = Small-scale biosphere models and phenomenology of global climate change / С. И. Барцев, А. Г. Дегерменджи. - С .255-283. - Библиогр.: с. 281-283
Дегерменджи, Андрей Георгиевич. Направления развития биофизики в Красноярске / А. Г. Дегерменджи. - С .284-288

ГРНТИ	31.27	76.03
УДК	577	574	61

ББК Е071я43 + Р252.0я43
Рубрики:
Экологическая биофизика
Медицинская биофизика
Кл.слова (ненормированные):
биолюминесценция -- люцифераза -- целентаразин -- олигохеты -- замкнутые экосистемы -- управляемый биосинтез -- наноалмазы -- радиоизотопные методы -- биосфера -- жирные кислоты -- системы жизнеобеспечения -- меромиктические озера -- геобиосфера -- эволюция -- глобальный климат -- Медицинская биофизика
Аннотация: Сборник посвящен широкому кругу исследований в области экологической биофизики – научного направления на стыке наук – от исследований на молекулярном уровне до вопросов управления большими природными экосистемами. Рассмотрены исторические вехи развития экологического направления биофизики. Основной акцент сборника основан на современных, актуальных достижениях красноярских биофизиков, которым удалось сохранить и развить многоплановые направления, которые были заложены в 50-х гг. ХХ века И. И. Гительзоном. Наряду с обзорными материалами и результатами фундаментальных исследований представлен ряд готовых к внедрению биотехнологий. Книга адресована биофизикам, экологам и химикам, а также преподавателям и студентам биофизических, биологических и экологических кафедр университетов.

Держатели документа:
Библиотека Института биофизики СО РАН : 660036, Академгородок, 50/12

Доп.точки доступа:
Гительзон, Иосиф Исаевич; Волова, Татьяна Григорьевна; Дегерменджи, Андрей Георгиевич; Дегерменджи, Н. Н.; Шевырногов, Анатолий Петрович; Кратасюк, В. А.; Барцев, Сергей иванович; Болсуновский, Александр Яковлевич; Бондарь, Владимир Антонович; Буров, А. Е.; Величко, В. В.; Гладышев, Михаил Иванович; Есимбекова, Е. Н.; Дементьев, Д. В.; Задереев, Егор Сергеевич; Зотина, Т. А.; Косиненко, Сергей Васильевич; Медведева, С. Е.; Петушков, В. Н.; Печуркин, Николай Савельевич; Прокопкин, И. Г.; Пузырь, А. П.; Пуртов, К. В.; Рогозин, Денис Юрьевич; Родионова, Н. С.; Ронжин, Н. О.; Сомова, Лидия Александровна; Тихомиров, Александр Аполлинариевич; Тихомирова, Наталья Александровна; Трифонов, С. В.; Ушакова, Софья Аврумовна; Франк, Л. А.; Хромечек, Е. Б.; Шишацкая, Е. И.; Шуваев, А. Н.; Волова, Татьяна Григорьевна \ред., авт. предисл.\; Утюшев Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П.; Трифонов С. В., Величко В. В.; Барон А. В., Буров А. Е.; Толомеев А. П., Бархатов Ю. В., Хромечек Е. Б., Дегерменджи Н. Н.; Дроботов А. В.; Дегерменджи А. Г., Андрей Георгиевич; Гительзон, Иосиф Исаевич \о нем\; Российская академия наук. Сибирское отделение; Институт биофизики (Красноярск)
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ИБФ-КФ (1)
Свободны: ИБФ-КФ (1)
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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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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.

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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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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.

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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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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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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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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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10.

The smallest natural high-active luciferase: Cloning and characterization of novel 16.5-kDa luciferase from copepod Metridia longa [Text] / S. V. Markova [et al.] // Biochem. Biophys. Res. Commun. - 2015. - Vol. 457, Is. 1. - P77-82, DOI 10.1016/j.bbrc.2014.12.082. - Cited References:20. - The cloning of cDNA encoding MLuc7 luciferase of M. longa was supported by Bayer AG (Germany); all other studies - by the grant 14-14-01119 of the Russian Science Foundation. We declare that authors have no conflict of interest. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
   SECRETED LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Mammalian -- expression -- Real-time imaging
Аннотация: Coelenterazine-dependent copepod luciferases containing natural signal peptide for secretion are a very convenient analytical tool as they enable monitoring of intracellular events with high sensitivity, without destroying cells or tissues. This property is well suited for application in biomedical research and development of cell-based assays for high throughput screening. We report the cloning of cDNA gene encoding a novel secreted non-allelic 16.5-kDa isoform (MLuc7) of Metridia longa luciferase, which, in fact, is the smallest natural luciferase of known for today. Despite the small size, isoform contains 10 conservative Cys residues suggesting the presence of up to 5 S-S bonds. This hampers the efficient production of functionally active recombinant luciferase in bacterial expression systems. With the use of the baculovirus expression system, we produced substantial amounts of the proper folded MLuc7 luciferase with a yield of similar to 3 mg/L of a high purity protein. We demonstrate that MLuc7 produced in insect cells is highly active and extremely thermostable, and is well suited as a secreted reporter when expressed in mammalian cells ensuring higher sensitivity of detection as compared to another Metridia luciferase isoform (MLuc164) which is widely employed in real-time imaging. (C) 2014 Elsevier Inc. All rights reserved.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.
ИБФ СО РАН

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Burakova, Ludmila P.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Science Foundation [14-14-01119]

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11.

The Smallest Isoform ofMetridia longaLuciferase as a Fusion Partner for Hybrid Proteins / M. D. Larionova, S. V. Markova, N. V. Tikunova, E. S. Vysotski // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 14. - Ст. 4971, DOI 10.3390/ijms21144971. - Cited References:49. - The reported study was funded by the Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (S.V.M, M.D.L., and E.S.V.) and by the Russian State funded budget project of ICBFM SB RAS No. AAAA-A17-117020210027-9 (N.V.T.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
COELENTERAZINE-BINDING PROTEIN
BIOLUMINESCENT REPORTER
GAUSSIA
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- copepod luciferase -- single-chain -- antibody -- immunoassay -- tick-borne encephalitis virus
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepodMetridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N- or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (K-D= 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (K-D= 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform ofM. longaluciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.
Inst Chem Biol & Fundamental Med, Russian Acad Sci, Siberian Branch, Novosibirsk 630090, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana, V; Tikunova, Nina, V; Vysotski, Eugene S.; Vysotski, Eugene; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; ICBFM SB RAS [AAAA-A17-117020210027-9]; Government of Krasnoyarsk Territory

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12.

The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins / M. D. Larionova, S. V. Markova, N. V. Tikunova, E. S. Vysotski // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 14. - Ст. 4971. - P1-16, DOI 10.3390/ijms21144971 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Immunoassay -- Single-chain antibody -- Tick-borne encephalitis virus -- fusion protein -- glycoprotein -- histidine -- messenger RNA -- Metridia longa luciferase -- recombinant protein -- single chain fragment variable antibody -- unclassified drug -- amino terminal sequence -- antibody affinity -- antigen binding -- Article -- binding assay -- binding site -- bioluminescence -- bioluminescence resonance energy transfer -- cross reaction -- dissociation constant -- enzyme activity -- Escherichia coli -- gene -- genetic engineering -- genetic transfection -- immunoassay -- limit of detection -- mluc7 gene -- molecular cloning -- nonhuman -- nucleotide sequence -- protein expression -- protein purification -- protein unfolding -- spectral sensitivity -- tick borne encephalitis -- Tick borne encephalitis virus
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepod Metridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N-or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (KD = 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (KD = 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform of M. longa luciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Tikunova, N. V.; Vysotski, E. S.

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13.

The novel extremely psychrophilic luciferase from Metridia longa: Properties of a high-purity protein produced in insect cells / M. D. Larionova, S. V. Markova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 2017. - Vol. 483, Is. 1. - P772-778, DOI 10.1016/j.bbrc.2016.12.067. - Cited References:24. - The cloning of cDNAs encoding MLuc2 isoforms of M. longa was supported by Bayer AG (Germany) and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 01201351504); all other studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
EXPRESSION
ENZYME
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Bioluminescent reporter -- Psychrophilic -- enzyme -- Molecular adaptation
Аннотация: The bright bioluminescence of copepod Metridia longa is conditioned by a small secreted coelenterazinedependent luciferase (MLuc). To date, three isoforms of MLuc differing in length, sequences, and some properties were cloned and successfully applied as high sensitive bioluminescent reporters. In this work, we report cloning of a novel group of genes from M. longa encoding extremely psychrophilic isoforms of MLuc (MLuc2-type). The novel isoforms share only similar to 54-64% of protein sequence identity with the previously cloned isoforms and, consequently, are the product of a separate group of paralogous genes. The MLuc2 isoform with consensus sequence was produced as a natively folded protein using baculovirus/ insect cell expression system, purified, and characterized. The MLuc2 displays a very high bioluminescent activity and high thermostability similar to those of the previously characterized M. longa luciferase isoform MLuc7. However, in contrast to MLuc7 revealing the highest activity at 12-17 degrees C and 0.5 M NaCl, the bioluminescence optima of MLuc2 isoforms are at similar to 5 degrees C and 1 M NaCl. The MLuc(2) adaptation to cold is also accompanied by decrease of melting temperature and affinity to substrate suggesting a more conformational flexibility of a protein structure. The luciferase isoforms with different temperature optima may provide adaptability of the M. longa bioluminescence to the changes of water temperature during diurnal vertical migrations. (C) 2016 Elsevier Inc. All rights reserved.

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

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Academy of Sciences [01201351504]; RFBR; Government of Krasnoyarsk Territory [16-44-242099]

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14.

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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15.

The kinetics of coelenterazine binding with apo-obelin and apo-aequorin [Text] / E. V. Eremeeva [et al.] // Luminescence. - 2008. - Vol. 23, Is. 2. - P66-67. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Frank, L. A.
Vysotski, E. S.] SB RAS, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Lee, J.
Vysotski, E. S.] Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
[Eremeeva, E. V.
van Berkel, W. J. H.
Visser, A. J. W. G.] Univ Wageningen & Res Ctr, 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.; Frank, L.A.; Lee, J...; van Berkel, WJH; Visser, AJWG; Vysotski, E.S.

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16.

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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17.

The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin / L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - P313-323, DOI 10.1039/c9pp00436j . - ISSN 1474-905X
Кл.слова (ненормированные):
Amino acids -- Bioluminescence -- Conformations -- Phosphorescence -- Amino acid residues -- Amino acid sequence -- Hydrogen bond networks -- Hydromedusan -- Internal cavities -- Phenyl rings -- Photoproteins -- Pi interactions -- Hydrogen bonds
Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal ?-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first ?-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the ?-? interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins. This journal is © The Royal Society of Chemistry and Owner Societies.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Eremeeva, E. V.; Vysotski, E. S.

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18.

The interaction of C-terminal Tyr208 and Tyr13 of the first alpha-helix ensures a closed conformation of ctenophore photoprotein berovin / L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - P313-323, DOI 10.1039/c9pp00436j. - Cited References:49. - This work was supported by grant 17-04-00764 of the Russian Foundation for Basic Research. . - ISSN 1474-905X. - ISSN 1474-9092

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
GREEN FLUORESCENT PROTEIN
Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal alpha-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first alpha-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the pi-pi interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins.

WOS
Держатели документа:
RAS, SB, Photobiol Lab, Inst Biophys,Fed Res Ctr,Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Eremeeva, Elena V.; Vysotski, Eugene S.; Vysotski, Eugene; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [17-04-00764]

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19.

The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research / V. V. Krasitskaya, E. E. Bashmakova, A. N. Kudryavtsev [et al.] // Russ. J. Bioorg. Chem. - 2020. - Vol. 46, Is. 6. - P1004-1010, DOI 10.1134/S106816202006014X. - Cited References:14. - The study was partially supported by a grant of the President of the Russian Federation for Young Scientists, the Candidates of Sciences (project MK-772.2020.4 in the part involving the synthesis and analysis of variants of proteins with melanoma-inhibiting activity) and a grant of the Russian Science Foundation (project no. 16-14-10296 in the part involving the bioluminescence analysis of binding of DNA aptamers to targets). . - ISSN 1068-1620. - ISSN 1608-330X

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

Кл.слова (ненормированные):
С -- а -- (2+)-regulated photoprotein obelin -- proZZ -- hybrid -- protein -- IgG -- bioluminescence assay
Аннотация: The gene of the hybrid protein that encodes the double synthetic fragment proZZ of the immunoglobulin-binding domain of protein A of Staphylococcus aureus and apo-obelin joined by a short linker has been cloned. The corresponding hybrid protein has been obtained by expression in Escherichia coli cells. The protein activated with a substrate (coelenterazine) possesses the bioluminescent Ca2+-dependent activity of the photoprotein close to that of recombinant wild-type obelin, and the immunoglobulin-binding ability of protein A. It has been shown that the hybrid can be used as a highly sensitive label to detect antibodies and estimate their affinity and interaction with recombinant proteins, as well as in investigations of other kinds.

WOS
Держатели документа:
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Res Ctr, Siberian Branch,Inst Biophys, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia.

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Kudryavtsev, A. N.; Vorobjeva, M. A.; Shatunova, E. A.; Frank, L. A.; Russian FederationRussian Federation [MK-772.2020.4]; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]

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20.

The function of conserved cystein residues in the bioluminescence of coelenterazine-dependent luciferase from Metridia longa; testing with site-directed mutagenesis [Text] / S. V. Markova, G. A. Stepanyuk, E. S. Vysotski // Luminescence. - 2008. - Vol. 23, Is. 2. - P84-84. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
[Markova, S. V.
Stepanyuk, G. A.
Vysotski, E. S.] RAS, SB, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Markova, S.V.; Stepanyuk, G.A.; Vysotski, E.S.

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