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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : 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.
Заглавие : Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation
Колич.характеристики :4 с
Коллективы : 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]
Место публикации : Org. Lett.: AMER CHEMICAL SOC, 2021. - Vol. 23, Is. 17. - С. 6846-6849. - ISSN 1523-7060, DOI 10.1021/acs.orglett.1c02410. - ISSN 1523-7052(eISSN)
Примечания : 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.
Предметные 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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chen S. -F., Vysotski E. S., Liu Y. -J.
Заглавие : H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence
Место публикации : J Phys Chem B: American Chemical Society, 2021. - Article in press. - ISSN 15206106 (ISSN), DOI 10.1021/acs.jpcb.1c03985
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S1) is the emitter of CaRP. The S1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs. © 2021 American Chemical Society.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tomilin, Felix N., Rogova, Anastasia V., Burakova, Ludmila P., Tchaikovskaya, Olga N., Avramov, Pavel V., Fedorov, Dmitri G., Vysotski, Eugene S.
Заглавие : Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory
Колич.характеристики :12 с
Коллективы : 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]
Место публикации : Photochem. Photobiol. Sci.: SPRINGERNATURE, 2021. - Vol. 20, Is. 4. - С. 559-570. - ISSN 1474-905X, DOI 10.1007/s43630-021-00039-5. - ISSN 1474-9092(eISSN)
Примечания : Cited References:61. - The ab initio quantum chemical calculations were funded by RFBR and NSFC as the research project No. 19-54-53004 and RFBR research project No. 20-04-00085. The development of structural atomistic model of berovin without calcium ions generated by the I-TASSER server was funded by project 0721-2020-0033 of the Russian Ministry of Science and Education.
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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tomilin F. N., Rogova A. V., Burakova L. P., Tchaikovskaya O. N., Avramov P. V., Fedorov D. G., Vysotski E. S.
Заглавие : Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory
Место публикации : Photochem. Photobiol. Sci.: Springer Nature, 2021. - Vol. 20, Is. 4. - С. 559-570. - ISSN 1474905X (ISSN), DOI 10.1007/s43630-021-00039-5
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Wu, Lijie, Eremeeva, Elena, V, Natashin, Pavel, V, Gulnov, Dmitry, V, Nemtseva, Elena, V, Liu, Dongsheng, Liu, Zhi-Jie, Vysotski, Eugene S.
Заглавие : Crystal structure of semisynthetic obelin-v
Колич.характеристики :16 с
Коллективы : National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [32011530076]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 20-44-240006, 20-54-53011]
Место публикации : Protein Sci.: WILEY, 2021. - Article in press. - ISSN 0961-8368, DOI 10.1002/pro.4244. - ISSN 1469-896X(eISSN)
Примечания : Cited References:69. - National Natural Science Foundation of China, Grant/Award Number: 32011530076; Russian Foundation for Basic Research, Grant/Award Numbers: 20-04-00085, 20-44-240006, 20-54-53011
Предметные рубрики: CA2+-REGULATED PHOTOPROTEIN OBELIN
PHOTOLUMINESCENCE QUANTUM YIELD
Аннотация: Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca2+-regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca2+-regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 angstrom resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (phi(FL)) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (phi(R)) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (phi(S)). In turn, the low phi(S) value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chen, Shu-Feng, Vysotski, Eugene S., Liu, Ya-Jun
Заглавие : H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence
Колич.характеристики :7 с
Коллективы : Program of Shanghai Institute of Technology [YJ2016-42]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21973005, 21911530094]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 19-14-53004]
Место публикации : J. Phys. Chem. B: AMER CHEMICAL SOC, 2021. - Vol. 125, Is. 37. - С. 10452-10458. - ISSN 1520-6106, DOI 10.1021/acs.jpcb.1c03985. - ISSN 1520-5207(eISSN)
Примечания : Cited References:50. - This work was supported by the Program of Shanghai Institute of Technology (no. YJ2016-42), the National Natural Science Foundation of China (21973005 and 21911530094), and the Russian Foundation for Basic Research (20-04-00085 and 19-14-53004).
Предметные рубрики: CHEMILUMINESCENT DECOMPOSITION
FLUORESCENCE-SPECTRA
MECHANISM
QM/MM
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S-1) is the emitter of CaRP. The S-1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S-1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S-1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S-1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S-1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena, V, Jiang, Tianyu, Malikova, Natalia P., Li, Minyong, Vysotski, Eugene S.
Заглавие : Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents
Колич.характеристики :21 с
Коллективы : RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 15. - Ст.5446. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21155446
Примечания : Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.).
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E. V., Jiang T., Malikova N. P., Li M., Vysotski E. S.
Заглавие : Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 15. - Ст.5446. - С. 1-21. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21155446
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova M. D., Markova S. V., Tikunova N. V., Vysotski E. S.
Заглавие : The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 14. - Ст.4971. - С. 1-16. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21144971
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.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ding B. -W., Eremeeva E. V., Vysotski E. S., Liu Y. -J.
Заглавие : Luminescence Activity Decreases When v-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein—A Theoretical and Experimental Study
Место публикации : Photochem. Photobiol.: Blackwell Publishing Inc., 2020. - Article in press. - ISSN 00318655 (ISSN), DOI 10.1111/php.13280
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analog v-CTZ. The latter is formed by adding a phenyl ring to the ?-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the ?-? stacking interactions between the conjugated moiety of v-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced by v-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments. © 2020 American Society for Photobiology
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova, Ludmila P., Eremeeva, Elena V., Vysotski, Eugene S.
Заглавие : The interaction of C-terminal Tyr208 and Tyr13 of the first alpha-helix ensures a closed conformation of ctenophore photoprotein berovin
Колич.характеристики :11 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [17-04-00764]
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2020. - Vol. 19, Is. 3. - С. 313-323. - ISSN 1474-905X, DOI 10.1039/c9pp00436j. - ISSN 1474-9092(eISSN)
Примечания : Cited References:49. - This work was supported by grant 17-04-00764 of the Russian Foundation for Basic Research.
Предметные 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.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Eremeeva E. V., Vysotski E. S.
Заглавие : The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin
Место публикации : Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - С. 313-323. - ISSN 1474905X (ISSN), DOI 10.1039/c9pp00436j
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.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ding, Bo-Wen, Eremeeva, Elena V., Vysotski, Eugene S., Liu, Ya-Jun
Заглавие : Luminescence Activity Decreases Whenv-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein-A Theoretical and Experimental Study
Колич.характеристики :14 с
Коллективы : National Natural Science Foundation of ChinaNational Natural Science Foundation of China [21911530094, 21673020, 21973005]; RFBRRussian Foundation for Basic Research (RFBR) [19-54-53004, 20-54-53011]; China Postdoctoral Science FoundationChina Postdoctoral Science Foundation [2018M630100]
Место публикации : Photochem. Photobiol.: WILEY, 2020. - Article in press. - ISSN 0031-8655, DOI 10.1111/php.13280. - ISSN 1751-1097(eISSN)
Примечания : Cited References:68. - This study was sponsored by the National Natural Science Foundation of China (Grant No. 21911530094, 21673020 and 21973005) and RFBR (Grant No. 19-54-53004 and 20-54-53011). Ding also thank the support from the China Postdoctoral Science Foundation (Grant No. 2018M630100).
Предметные рубрики: RECOMBINANT SEMISYNTHETIC AEQUORINS
OBELIN BIOLUMINESCENCE
MECHANISTIC
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analogv-CTZ. The latter is formed by adding a phenyl ring to the pi-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the pi-pi stacking interactions between the conjugated moiety ofv-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced byv-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana, V, Tikunova, Nina, V, Vysotski, Eugene S.
Заглавие : The Smallest Isoform ofMetridia longaLuciferase as a Fusion Partner for Hybrid Proteins
Колич.характеристики :16 с
Коллективы : 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
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 14. - Ст.4971. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21144971
Примечания : 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.).
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
BIOLUMINESCENT REPORTER
GAUSSIA
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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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V. V., Bashmakova E. E., Kudryavtsev A. N., Vorobjeva M. A., Shatunova E. A., Frank L. A.
Заглавие : The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research
Колич.характеристики :7 с
Коллективы : Russian FederationRussian Federation [MK-772.2020.4]; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2020. - Vol. 46, Is. 6. - С. 1004-1010. - ISSN 1068-1620, DOI 10.1134/S106816202006014X. - ISSN 1608-330X(eISSN)
Примечания : 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).
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.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev A. N., Burakova L. P., Barinova K. A., Frank L. A.
Заглавие : A test system for tick-borne encephalitis virus detection based on bioluminescent immunoassay
Место публикации : J. Sib. Fed. Univ. - Biol.: Siberian Federal University, 2020. - Vol. 13, Is. 3. - С. 310-321. - ISSN 19971389 (ISSN), DOI 10.17516/1997-1389-0296
Аннотация: The tick-borne encephalitis virus (TBEV) is the causative agent of one of the most severe human neuroinfections. The infection transmitted by ixodid ticks is spread throughout the forest and forest-steppe zones of the temperate climatic belt of the Eurasian continent, including the Siberian region of the Russian Federation. Despite the availability of commercial analytical systems for the detection of TBEV, the task of developing approaches to a quick and reliable analysis that can be performed routinely, particularly in environmental studies, remains topical. A solid-phase bioluminescent immunoassay for determining the tick-borne encephalitis virus (TBEV) in ticks was developed. The assay is based on the hybrid protein consisting of a modified thermostable version of Renilla muelleri luciferase and a single-chain mini-antibody to protein E. This unique protein had been obtained and investigated by the authors earlier. The current study describes the expression of the hybrid protein in two different strains of recombinant E. coli cells. The optimal conditions for obtaining a highly purified protein were found. The bioluminescent reaction of the luciferase domain was triggered with the help of the stable natural form of the substrate, a Ca-dependent coelenterazine-binding protein, the recombinant variant of which was obtained by the authors. The conditions for production and storage of the immunoassay components (the hybrid protein, the stable form of the luciferase substrate, and activated microplates) were determined. Using the developed test system, more than 900 tick samples were analyzed for TBEV. In terms of sensitivity (89.5%) and specificity (98.9%), the proposed method is not inferior to colorimetric detection and is much simpler and faster than the latter. © Siberian Federal University. All rights reserved.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya, Vasilisa V., Bashmakova, Eugenia E., Frank, Ludmila A.
Заглавие : Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications
Колич.характеристики :29 с
Коллективы : Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 20. - Ст.7465. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21207465
Примечания : Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0.
Предметные рубрики: PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V. V., Bashmakova E. E., Frank L. A.
Заглавие : Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 20. - Ст.7465. - С. 1-31. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21207465
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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19.

20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Vysotski E. S.
Заглавие : Recombinant Ca2+-regulated photoproteins of ctenophores: current knowledge and application prospects
Место публикации : Appl. Microbiol. Biotechnol.: Springer Verlag, 2019. - Vol. 103, Is. 15. - С. 5929-5946. - ISSN 01757598 (ISSN) , DOI 10.1007/s00253-019-09939-0
Аннотация: Bright bioluminescence of ctenophores is conditioned by Ca2+-regulated photoproteins. Although they share many properties characteristic of hydromedusan Ca2+-regulated photoproteins responsible for light emission of marine animals belonging to phylum Cnidaria, a substantial distinction still exists. The ctenophore photoproteins appeared to be extremely sensitive to light—they lose the ability for bioluminescence on exposure to light over the entire absorption spectrum. Inactivation is irreversible because keeping the inactivated photoprotein in the dark does not recover its activity. The capability to emit light can be restored only by incubation of inactivated photoprotein with coelenterazine in the dark at alkaline pH in the presence of oxygen. Although these photoproteins were discovered many years ago, only the cloning of cDNAs encoding these unique bioluminescent proteins in the early 2000s has provided a new impetus for their studies. To date, cDNAs encoding Ca2+-regulated photoproteins from four different species of luminous ctenophores have been cloned. The amino acid sequences of ctenophore photoproteins turned out to completely differ from those of hydromedusan photoproteins (identity less than 29%) though also similar to them having three EF-hand Ca2+-binding sites. At the same time, these photoproteins reveal the same two-domain scaffold characteristic of hydromedusan photoproteins. This review is an attempt to systemize and critically evaluate the data scattered through various articles regarding the structural features of recombinant light-sensitive Ca2+-regulated photoproteins of ctenophores and their bioluminescent and physicochemical properties as well as to compare them with those of hydromedusan photoproteins. In addition, we also discuss the prospects of their biotechnology applications. © 2019, Springer-Verlag GmbH Germany, part of Springer Nature.
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