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Влияние температуры на активность и стабильность обелина [Текст] : научное издание / В. С. Бондарь [и др.] // Биохимия. - 1992. - Т. 57, N 7. - С. 1039-1048 . - ISSN 0320-9725

ГРНТИ

31.23.27

РУБ 314.23.27.07.11
Рубрики:
ОБЕЛИН
   АКТИВНОСТЬ
   СТАБИЛЬНОСТЬ
   ТЕМПЕРАТУРА
   ВЛИЯНИЕ
   PHOTOPROTEINS
   OBELIN
Аннотация: Исследована зависимость биолюминесцентной активности Ca{2}{+}-активируемого фотопротеина обелина из гидроидного полипа Obelia longissima от т-ры, а также его термостабильность и термоинактивация в присутствии различных концентраций (NH[4])[2]SO[4]. Максимум интенсивности люминесценции обелина наблюдается при 4-15'ГРАДУС'. Фотопротеин при комн. т-ре полностью сохраняет свою активность в течение трех суток. Повышение т-ры до 40'ГРАДУС' приводит к 25-30%-ному снижению активности белка в течение 1 ч. Сульфат аммония стабилизирует активность фотопротеина при термообработке. Обнаружены две точки излома на графике константы скорости псевдопервого порядка спада люминесценции обелина в координатах Аррениуса при т-рах 11'+-'3 и 47'+-'3'ГРАДУС'. В области т-р 10-40'ГРАДУС' обнаружена бифазность биолюминесцентных кривых обелина. Высказано предположение о возможности существования обелина в виде двух кинетически различимых конформеров, относительное содержание к-рых зависит от т-ры. Библ. 15. Россия, ин-т биофизики СО РАН, Красноярск.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Трофимов, К.П.; Сандалова, Т.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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Variation of Spectral Characteristics of Coelenteramide-Containing Fluorescent Protein from Obelia Longissima Exposed to Dimethyl Sulfoxide / A. S. Petrova [et al.] // Russ. Phys. J. - 2016. - Vol. 59, Is. 4. - P562-567, DOI 10.1007/s11182-016-0806-8. - Cited References:33. - This work was supported in part by the Russian Science Foundation (Contract No. 14-14-00076). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
fluorescent coelenteramide-containing fluorescent proteins -- discharged -- obelin -- proton transfer -- dimethyl sulfoxide
Аннотация: Effect of dimethyl sulfoxide (DMSO), a widespread biomedical agent, on spectral-luminescent characteristics of coelenteramide-containing fluorescent protein - discharged obelin - is investigated. Contributions of violet and blue-green spectral components to fluorescence of discharged obelin are elucidated and characterized at different photoexcitation energies. Dependences of these contributions on the DMSO concentration are presented. Spectral changes are related to the destructive effect of DMSO on fluorescent protein and decreasing efficiency of proton transfer to electronically excited states of fluorophore.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Krasnoyarsk State Agrarian Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Petrova, A. S.; Alieva, R. R.; Belogurova, N. V.; Tirranen, L. S.; Kudryasheva, N. S.; Russian Science Foundation [14-14-00076]

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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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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.

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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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Ultraviolet fluorescence of coelenteramide and coelenteramide-containing fluorescent proteins. Experimental and theoretical study / R. R. Alieva [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 162. - P318-323, DOI 10.1016/j.jphotobiol.2016.07.004 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- B3LYP -- Coelenteramide -- Discharged photoproteins -- Excitation energy -- Fluorescence -- Fluorescent protein -- Obelin
Аннотация: Coelenteramide-containing fluorescent proteins are products of bioluminescent reactions of marine coelenterates. They are called ‘discharged photoproteins’. Their light-induced fluorescence spectra are variable, depending considerably on external conditions. Current work studies a dependence of light-induced fluorescence spectra of discharged photoproteins obelin, aequorin, and clytin on excitation energy. It was demonstrated that photoexcitation to the upper electron-excited states (260–300 nm) of the discharged photoproteins initiates a fluorescence peak in the near UV region, in addition to the blue-green emission. To characterize the UV fluorescence, the light-induced fluorescence spectra of coelenteramide (CLM), fluorophore of the discharged photoproteins, were studied in methanol solution. Similar to photoproteins, the CLM spectra depended on photoexcitation energy; the additional peak (330 nm) in the near UV region was observed in CLM fluorescence at higher excitation energy (260–300 nm). Quantum chemical calculations by time depending method with B3LYP/cc-pVDZ showed that the conjugated pyrazine-phenolic fragment and benzene moiety of CLM molecule are responsible for the additional UV fluorescence peak. Quantum yields of CLM fluorescence in methanol were 0.028 ± 0.005 at 270–340 nm photoexcitation. A conclusion was made that the UV emission of CLM might contribute to the UV fluorescence of the discharged photoproteins. The study develops knowledge on internal energy transfer in biological structures – complexes of proteins with low-weight aromatic molecules. © 2016 Elsevier B.V.

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Держатели документа:
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Akademgorodok 50/38, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Alieva, R. R.; Tomilin, F. N.; Kuzubov, A. A.; Ovchinnikov, S. G.; Kudryasheva, N. S.

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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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10.

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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11.

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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12.

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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13.

Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction [Text] / P. V. Natashin [et al.] // Acta Crystallogr. Sect. D-Biol. Crystallogr. - 2014. - Vol. 70. - P720-732, DOI 10.1107/S1399004713032434. - Cited References: 71. - We acknowledge the use of beamline BL17U1 at the Shanghai Synchrotron Radiation Facility, China. This work was supported by RFBR grants 12-04-91153, 12-04-00131 and the China-Russia International Collaboration grant from the Chinese Academy of Sciences and NSFC, by the Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' (grant 11.G34.31.0058) and 'Molecular and Cellular Biology' of the RAS, the President of the Russian Federation 'Leading Science School' (grant 3951.2012.4). PVN and EVE were supported by RFBR grant 14-04-31092. . - ISSN 0907-4449. - ISSN 1399-0047

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Biophysics + Crystallography
Рубрики:
AEQUORIN BIOLUMINESCENCE
   SEQUENCE-ANALYSIS
   CRYSTAL-STRUCTURE
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   CALCIUM CONCENTRATION
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MNEMIOPSIS-LEIDYI
   EXCITED-STATES
Аннотация: Ca2+-regulated photoproteins, which are responsible for light emission in a variety of marine coelenterates, are a highly valuable tool for measuring Ca2+ inside living cells. All of the photoproteins are a single-chain polypeptide to which a 2-hydroperoxycoelenterazine molecule is tightly but noncovalently bound. Bioluminescence results from the oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. Here, the crystal structures of the Y138F obelin mutant before and after bioluminescence are reported at 1.72 and 1.30 angstrom resolution, respectively. The comparison of the spatial structures of the conformational states of Y138F obelin with those of wild-type obelin gives clear evidence that the substitution of Tyr by Phe does not affect the overall structure of both Y138F obelin and its product following Ca2+ discharge compared with the corresponding conformational states of wild-type obelin. Despite the similarity of the overall structures and internal cavities of Y138F and wild-type obelins, there is a substantial difference: in the cavity of Y138F obelin a water molecule corresponding to W2 in wild-type obelin is not found. However, in Ca2+-discharged Y138F obelin this water molecule now appears in the same location. This finding, together with the observed much slower kinetics of Y138F obelin, clearly supports the hypothesis that the function of a water molecule in this location is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion before its decomposition into the excited-state product. Although obelin differs from other hydromedusan Ca2+-regulated photoproteins in some of its properties, they are believed to share a common mechanism.

wos
Держатели документа:
[Natashin, Pavel V.
Ding, Wei
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Chair Biophys, Krasnoyarsk, Russia
[Ding, Wei] Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, Beijing 100080, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem Mol Biol, Athens, GA 30602 USA
[Liu, Zhi-Jie] Shanghai Tech Univ, Human Inst, Shanghai, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Ding, W...; Eremeeva, E.V.; Markova, S.V.; Lee, J...; Vysotski, E.S.; Liu, Z.J.; RFBR [12-04-91153, 12-04-00131, 14-04-31092]; Chinese Academy of Sciences; NSFC; Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' [11.G34.31.0058]; RAS; Russian Federation 'Leading Science School' [3951.2012.4]

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14.

Specific Activities of Hydromedusan Ca2+-Regulated Photoproteins / N. P. Malikova, E. V. Eremeeva, D. V. Gulnov [et al.] // Photochem. Photobiol. - 2021, DOI 10.1111/php.13556 . - Article in press. - ISSN 0031-8655
Аннотация: Nowadays the recombinant Ca2+-regulated photoproteins originating from marine luminous organisms are widely applied to monitor calcium transients in living cells due to their ability to emit light on Ca2+ binding. Here we report the specific activities of the recombinant Ca2+-regulated photoproteins—aequorin from Aequorea victoria, obelins from Obelia longissima and Obelia geniculata, clytin from Clytia gregaria and mitrocomin from Mitrocoma cellularia. We demonstrate that along with bioluminescence spectra, kinetics of light signals and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of bioluminescent reactions. The highest specific activities were found for obelins and mitrocomin, whereas those of aequorin and clytin were shown to be lower. To determine the factors influencing the variations in specific activities the fluorescence quantum yields for Ca2+-discharged photoproteins were measured and found to be quite different varying in the range of 0.16–0.36. We propose that distinctions in specific activities may result from different efficiencies of singlet excited state generation and different fluorescence quantum yields of coelenteramide bound within substrate-binding cavity. This in turn may be conditioned by variations in the amino acid environment of the substrate-binding cavities and hydrogen bond distances between key residues and atoms of 2-hydroperoxycoelenterazine. © 2021 American Society for Photobiology

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Malikova, N. P.; Eremeeva, E. V.; Gulnov, D. V.; Natashin, P. V.; Nemtseva, E. V.; Vysotski, E. S.

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15.

Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state [Text] / G. A. Stepanyuk [et al.] // BBA-Proteins Proteomics. - 2013. - Vol. 1834, Is. 10. - P2139-2146, DOI 10.1016/j.bbapap.2013.07.006. - Cited References: 64. - This work was supported by RFBR grants 09-04-00172, 12-04-00131, 12-04-91153, and NSFC 31270795 and 31021062, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) "Molecular and Cellular Biology" of the RAS. It was also supported in part with funds from the National Institutes of Health (GM62407), The Georgia Research Alliance and the University of Georgia Research Foundation. Data were collected at Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory. Supporting institutions may be found at www.ser-cat.org/members.html. The use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. W-31-109-Eng-38. . - ISSN 1570-9639

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   COELENTERAZINE-BINDING PROTEIN
   CRYSTAL-STRUCTURE
   MNEMIOPSIS-SP
   CA2+-REGULATED PHOTOPROTEINS
   OBELIN BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   RENILLA-RENIFORMIS
   APO-OBELIN
Кл.слова (ненормированные):
Coelenterazine -- Calcium -- Bioluminescence -- Luciferase
Аннотация: The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca2+-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0 angstrom. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. (C) 2013 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
[Stepanyuk, Galina A.
Liu, Zhi-Jie
Lee, John
Rose, John
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Burakova, Ludmila P.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Liu, Zhi-Jie] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
[Burakova, Ludmila P.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Burakova, L.P.; Lee, J...; Rose, J...; Vysotski, E.S.; Wang, B.C.; RFBR [09-04-00172, 12-04-00131, 12-04-91153]; NSFC [31270795, 31021062]; Government of Russian Federation of the RAS [11.G34.31.0058]; National Institutes of Health [GM62407]; Georgia Research Alliance; University of Georgia Research Foundation; U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]

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16.

Semisynthetic photoprotein reporters for tracking fast Ca2+ transients / N. P. Malikova, A. J. Borgdorff, E. S. Vysotski // Photochem. Photobiol. Sci. - 2015. - Vol. 14, Is. 12. - P2213-2224, DOI 10.1039/c5pp00328h . - ISSN 1474-905X
Аннотация: Changes in the intracellular concentration of free ionized calcium ([Ca2+]i) control a host of cellular processes as varied as vision, muscle contraction, neuronal signal transmission, proliferation, apoptosis etc. The disturbance in Ca2+-signaling causes many severe diseases. To understand the mechanisms underlying the control by calcium and how disorder of this regulation relates to pathological conditions, it is necessary to measure [Ca2+]i. The Ca2+-regulated photoproteins which are responsible for bioluminescence of marine coelenterates have been successfully used for this purpose over the years. Here we report the results on comparative characterization of bioluminescence properties of aequorin from Aequorea Victoria, obelin from Obelia longissima, and clytin from Clytia gregaria charged by native coelenterazine and coelenterazine analogues f, i, and hcp. The comparison of specific bioluminescence activity, stability, emission spectra, stopped-flow kinetics, sensitivity to calcium, and effect of physiological concentrations of Mg2+ establishes obelin-hcp as an excellent semisynthetic photoprotein to keep track of fast intracellular Ca2+ transients. The rate of rise of its light signal on a sudden change of [Ca2+] is almost 3- and 11-fold higher than those of obelin and aequorin with native coelenterazine, respectively, and 20 times higher than that of the corresponding aequorin-hcp. In addition, obelin-hcp preserves a high specific bioluminescence activity and displays higher Ca2+-sensitivity as compared to obelin charged by native coelenterazine and sensitivity to Ca2+ comparable with those of aequorin-f and aequorin-hcp. © The Royal Society of Chemistry and Owner Societies 2015.

Scopus,
WOS
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Institut des Neurosciences Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique, Avenue de la Terrasse, Gif-sur-Yvette, France

Доп.точки доступа:
Malikova, N. P.; Borgdorff, A. J.; Vysotski, E. S.
Свободных экз. нет
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17.

Role of key residues of obelin in coelenterazine binding and conversion into 2-hydroperoxy adduct [Text] / E. V. Eremeeva [et al.] // J. Photochem. Photobiol. B-Biol. - 2013. - Vol. 127. - P133-139, DOI 10.1016/j.jphotobiol.2013.08.012. - Cited References: 65. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 3951.2012.4). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program. . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   SEQUENCE-ANALYSIS
   CRYSTAL-STRUCTURE
   APO-OBELIN
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   AEQUORIN REGENERATION
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MNEMIOPSIS-LEIDYI
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Obelin -- Aequorin -- Photoprotein
Аннотация: Bioluminescence of a variety of marine organisms is caused by monomeric Ca2+-regulated photoproteins, to which a peroxy-substituted coelenterazine, 2-hydroperoxycoelenterazine, is firmly bound. From the spatial structure the side chains of Tyr138, His175, Trp179, and Tyr190 of obelin are situated within the substrate-binding pocket at hydrogen bond distances with different atoms of the 2-hydroperoxycoelenterazine. Here we characterized several obelin mutants with substitutions of these residues regarding their bioluminescence, coelenterazine binding, and kinetics of active obelin formation. We demonstrate that Tyr138, His175, Trp179, and Tyr190 are all important for coelenterazine activation; substitution of any of these residues leads to significant decrease of the apparent reaction rate. The hydrogen bond network formed by Tyr138, Trp179 and Tyr190 participates in the proper positioning of coelenterazine in the active site and subsequent stabilization of the 2-hydroperoxy adduct of coelenterazine. His175 might serve as a proton shuttle during 2-hydroperoxycoelenterazine formation. (C) 2013 Elsevier B.V. All rights reserved.

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

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; van Berkel, WJH; Vysotski, E.S.; RFBR [12-04-00131]; Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" [11.G34.31.0058]; "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" [3951.2012.4]; Wageningen University Sandwich PhD-Fellowship Program

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18.

Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin [Text] / V. S. Bondar [et al.] // Biochem.-Moscow. - 2001. - Vol. 66, Is. 9. - P1014-1018, DOI 10.1023/A:1012377827626. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CDNA
   EXPRESSION
   AEQUORIN
   SEQUENCE
   CLONING
Кл.слова (ненормированные):
photoproteins -- obelin -- apoobelin mutants -- bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein > S-mutant > A-mutant. This is consistent with rank of nucleophilicity SH > OH > CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.

Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondar, V.S.; Purtov, K.V.; Malikova, N.P.; Frank, L.A.; Illarionov, B.A.

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19.

Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin / L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2016. - Vol. 15, Is. 5. - P691-704, DOI 10.1039/c6pp00050a . - ISSN 1474-905X
Аннотация: Bright bioluminescence of ctenophores is caused by Ca2+-regulated photoproteins. Although these photoproteins are functionally identical to and share many properties of cnidarian photoproteins, like aequorin and obelin, and retain the same spatial architecture, they are extremely sensitive to light, i.e. lose the ability to bioluminesce on exposure to light over the entire absorption spectrum. In addition, the degree of identity of their amino acid sequences with those of cnidarian photoproteins is only 29.4%. This suggests that the residues involved in bioluminescence of ctenophore and cnidarian photoproteins significantly differ. Here we describe the bioluminescent properties of berovin mutants with substitution of the residues located in the photoprotein internal cavity. Since the spatial structure of berovin bound with a substrate is not determined yet, to identify these residues we have modeled it with an accommodated substrate using the structures of some cnidarian Ca2+-regulated photoproteins with bound coelenterazine or coelenteramide as templates in order to obtain an adequate sampling and to take into account all possible conformers and variants for ligand-protein docking. Based on the impact of substitutions on the bioluminescent properties and model structures we speculate that within the internal cavity of ctenophore photoproteins, coelenterazine is bound as a 2-peroxy anion adduct which is stabilized owing to Coulomb interaction with a positively charged guanidinium group of Arg41 paired with Tyr204. In this case, the bioluminescence reaction is triggered by only calcium-induced conformational changes leading to the disturbance of charge-charge interaction. © 2016 The Royal Society of Chemistry and Owner Societies.

Scopus,
Смотреть статью,
WOS
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

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

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20.

RedquorinXS Mutants with Enhanced Calcium Sensitivity and Bioluminescence Output Efficiently Report Cellular and Neuronal Network Activities / A. Bakayan, S. Picaud, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 21. - Ст. 7846, DOI 10.3390/ijms21217846. - Cited References:53. - This work was supported by grants from Centre National de la Recherche Scientifique (AAP Prematuration CNRS 2016, to A.B. and N.P.; equipment transfer to S.P. and B.L.), from Agence Nationale de la Recherche (AAP Prematuration FCS/IDEX Paris Saclay, to A.B. and N.P., France BioImaging infrastructure ANR-10-INBS-04, ANR-11-EQPX-029 to N.P.), from Fondation pour la Recherche sur le Cerveau/Rotary Club de France (B.L.), and from RFBR (project number 20-04-00085 to N.P.M. and E.S.V.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
IN-VIVO
   PHOTOPROTEIN AEQUORIN
   CA2+-REGULATED PHOTOPROTEINS
   SPREADING
Кл.слова (ненормированные):
bioluminescence -- aequorin -- calcium sensor -- BRET -- mutagenesis -- GPCR -- assay -- neuronal network imaging
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+-dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP-aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty-four amino acid positions in and around EF-hand Ca2+-binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C-terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild-type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild-type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt-Redquorin, and one, RedquorinXS-Q159T, outperformed GA. Finally, wide-field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS-Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS-Q159T is a red light-emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice.

WOS
Держатели документа:
Ctr Natl Rech Sci CNRS, Inst Neurobiol Alfred Fessard, UPR 3294, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Univ Paris Saclay, BioEmergences Unit, CNRS, USR 3695, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Sorbonne Univ, Inst Biol Paris Seine NPS IBPS, INSERM, Neurosci Paris Seine,CNRS,UMR8246,U1130,UM119, F-75005 Paris, France.
Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Bakayan, Adil; Picaud, Sandrine; Malikova, Natalia P.; Tricoire, Ludovic; Lambolez, Bertrand; Vysotski, Eugene S.; Peyrieras, Nadine; Vysotski, Eugene; Centre National de la Recherche ScientifiqueCentre National de la Recherche Scientifique (CNRS); Agence Nationale de la RechercheFrench National Research Agency (ANR) [ANR-10-INBS-04, ANR-11-EQPX-029]; Fondation pour la Recherche sur le Cerveau/Rotary Club de France; RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]

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