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Influence of NaCl on Productivity and Fluorescence Parameters of Nasturtium officinale R. Br. and Its Relevance to Artificial Closed Ecosystems / A. M. Pavlova, N. A. Gaevskii, O. V. Anishchenko [et al.] // Russ. J. Plant Physiol. - 2021. - Vol. 68, Is. 6. - P1173-1185, DOI 10.1134/S1021443721050137. - Cited References:27. - This work was supported by the fundamental research program of the Russian Academy of Sciences for 2013-2020, project no. 56.1.4 Sustainability of Higher Plant Cenoses Grown on Nutrient Media with Mineralized Organic Waste in Closed Human-Inhabited Ecological Systems. . - ISSN 1021-4437. - ISSN 1608-3407

РУБ Plant Sciences
Рубрики:
CHLOROPHYLL FLUORESCENCE
   SALT STRESS
   TOLERANCE
   PHOTOSYNTHESIS
Кл.слова (ненормированные):
Nasturtium officinale -- glycophyte -- salt tolerance -- photosynthetic -- apparatus -- closed ecosystems
Аннотация: Productivity values, sodium accumulation in aboveground biomass, and photosynthetic indices of watercress (Nasturtium officinale) leaves were investigated under conditions resembling artificial closed ecological systems (CES). The seedlings were grown on nutrient media with various NaCl concentrations (0.7, 1.4, and 1.8 g/L) for 7, 14, and 19 days after transferring them to saline solutions. The productivity of plants on the seventh day of their growth on saline media did not differ from that of control plants. The decrease in plant productivity was noted in all the treatments starting from the 14th day after transferring the plants to saline solutions. When NaCl concentration in the nutrient solution was raised from 0.7 to 1.8 g/L, a significant increase in relative Na+ content in plant tissues was observed, regardless of the duration of NaCl treatment. A substantial decrease in chlorophyll (a + b) to carotenoid content ratio was noted on the seventh and 14th days in plants grown at 1.8 g/L NaCl. In plants treated for 7 days with 0.7 and 1.4 g/L NaCl, the content of chlorophylls a and b and carotenoids was found to increase, which indicates the tolerance of N. officinale to CES conditions. The relative content of chlorophylls a and b in the light-harvesting chlorophyll (a + b) complex was independent of the extent of salinity. The maximum quantum yield of photosystem II reaction in N. officinale plants had typically high values (Y(II)(max) of 0.755 +/- 0.007). Using the Imaging Maxi version of the pulse amplitude-modulated (PAM) fluorometer, it was found that light curves for the effective quantum yield of photochemical and nonphotochemical fluorescence quenching (Y(II) and Y(NPQ), respectively) differed appreciably between the salt-treated and untreated plants in the case of long-term cultivation (19 days) at 0.7 and 1.4 g/L NaCl. The treatment with 1.8 g/L NaCl for the period from 14 to 19 days had no effect on light curves of Y(II) and Y(NPQ). It is argued that N. officinale can be used as a source of NaCl for humans under CES conditions.

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

Доп.точки доступа:
Pavlova, A. M.; Gaevskii, N. A.; Anishchenko, O. V.; Tikhomirova, N. A.; Tikhomirov, A. A.; fundamental research program of the Russian Academy of SciencesRussian Academy of Sciences [56.1.4]

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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.

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

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

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Crystal structure of semisynthetic obelin-v / M. D. Larionova, L. J. Wu, E. V. Eremeeva [et al.] // Protein Sci. - 2021, DOI 10.1002/pro.4244. - Cited References:69. - National Natural Science Foundation of China, Grant/Award Number: 32011530076; Russian Foundation for Basic Research, Grant/Award Numbers: 20-04-00085, 20-44-240006, 20-54-53011 . - Article in press. - ISSN 0961-8368. - ISSN 1469-896X

РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
PHOTOLUMINESCENCE QUANTUM YIELD
Кл.слова (ненормированные):
analog -- bioluminescence -- coelenterazine -- coelenterazine-v -- obelin -- photoprotein -- protein structure
Аннотация: Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca2+-regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca2+-regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 angstrom resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (phi(FL)) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (phi(R)) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (phi(S)). In turn, the low phi(S) value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.

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

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

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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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INTRACANOPY LIGHTING IN PHYTOCENOSES AND PHOTOBIOLOGICAL EFFICIENCY OF RADIATION IN PHOTOCULTURE CONDITIONS / A. A. Tikhomirov // Light Eng. - 2021. - Vol. 29, Is. 2. - P4-15, DOI 10.33383/2020-076. - Cited References:42. - The work is performed as part of state assignments VI.56.1.4 and 0287-2019-0009 "Research of the Effect of Plant Texture on Photosynthesis Efficiency" with the Biophysics Institute of the Federal Research Centre "Krasnoyarsk Research Facility of the Siberian Branch of the Russian Academy of Sciences". . - ISSN 0236-2945

РУБ Engineering, Electrical & Electronic + Optics
Рубрики:
DIFFERENT SPECTRAL COMPOSITION
   EMITTING-DIODES
   GREEN LIGHT
   LETTUCE
Кл.слова (ненормированные):
plant light culture -- intracanopy lighting -- light sources -- canopy -- architectonics -- optical canopy properties -- canopy productivity
Аннотация: The review is devoted to the study of the internal radiation regime in the canopies cultivated under controlled environmental conditions. The expediency of using canopies as an object of research for evaluating the photobiological efficiency of radiation in light culture conditions is justified. The appropriateness of light measurements in multi-tiered canopies is shown, taking into account the role of leaves of different tiers in the formation of an economically useful crop. The main requirements for light devices for their use in measuring artificial radiation in light culture conditions are considered, and a brief analysis of the existing instrument base for performing these studies is given. A number of examples show the complexity and ambiguity of the internal structure of the light field that is forming within canopies in light culture conditions. Conceptual approaches to the choice of spectral and energy characteristics of artificial irradiation for plant light culture are proposed and justified. The necessity of taking into account the light conditions of leaves of different tiers when choosing the spectral and energy characteristics of light sources for the cultivation of multi-tiered canopies is justified. Techniques, methods, and light sources used for additional intracanopy lighting are analysed. The efficiency of using side illumination of plant canopies and conditions for its implementation are considered. The advantages of the volume distribution of canopies on the most common multi-tiered lighting installations are discussed. Based on the presented mate- rial, we consider ways to improve methodological approaches for evaluating the photobiological effectiveness of artificial radiation in light culture conditions for canopies of cultivated plants, taking into account the features of their architectonics and internal radiation regime.

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Держатели документа:
Reshetnev Siberian State Univ Sci & Technol, Krasnoyarsk, Russia.
Krasnoyarsk Sci Ctr, Inst Biophys, SB RAS,Fed Res Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Tikhomirov, Alexander A.; Biophysics Institute of the Federal Research Centre "Krasnoyarsk Research Facility of the Siberian Branch of the Russian Academy of Sciences" [VI.56.1.4, 0287-2019-0009]

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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. C. Xu, T. J. Wang, G. F. Liu [et al.] // Sens. Actuator B-Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991. - Cited References:66. - We are grateful for financial support from the Taishan Scholars Program of Shandong Province (tsqn201812104), the Qingchuang Science and Technology Plan of Shandong Province (2019KJJ017 and 2020KJC004), the National Natural Science Foundation of China (61671107, 62071085, 11704059, and 31802309), and the Youth Innovation Team Lead-Education Project of Shandong Educational Committee. . - ISSN 0925-4005

РУБ Chemistry, Analytical + Electrochemistry + Instruments & Instrumentation
Рубрики:
LABEL-FREE DETECTION
CHEMICAL-VAPOR-DEPOSITION
DNA HYBRIDIZATION
Кл.слова (ненормированные):
Single-crystal graphene -- FET -- Binding kinetics -- LMW drugs -- Imatinib
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 mu M range. This graphene-based FET biosensor (G-FET) was also applied toquantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs.

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Держатели документа:
Dezhou Univ, Inst Biophys, Shandong Key Lab Biophys, Dezhou 253023, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Shandong Normal Univ, Collaborat Innovat Ctr Light Manipulat & Applicat, Jinan 250358, Peoples R China.

Доп.точки доступа:
Xu, Shicai; Wang, Tiejun; Liu, Guofeng; Cao, Zanxia; Frank, Ludmila A.; Jiang, Shouzhen; Zhang, Chao; Li, Zhenhua; Krasitskaya, Vasilisa V.; Li, Qiang; Sha, Yujie; Zhang, Xiumei; Liu, Huilan; Wang, Jihua; Taishan Scholars Program of Shandong Province [tsqn201812104]; Qingchuang Science and Technology Plan of Shandong Province [2019KJJ017, 2020KJC004]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [61671107, 62071085, 11704059, 31802309]; Youth Innovation Team Lead-Education Project of Shandong Educational Committee

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Detecting bioluminescence conditions in fruit bodies of two species of Armillaria basidiomycetes / A. P. Puzyr, A. E. Burov, V. S. Bondar // IOP Conference Series: Earth and Environmental Science : IOP Publishing Ltd, 2021. - Vol. 677: 4th International Scientific Conference on Agribusiness, Environmental Engineering and Biotechnologies, AGRITECH-IV 2020 (18 November 2020 through 20 November 2020, ) Conference code: 167873, Is. 5. - Ст. 052081, DOI 10.1088/1755-1315/677/5/052081
Кл.слова (ненормированные):
Bioluminescence -- Biotechnology -- Fungi -- Phosphorescence -- Armillaria -- Armillaria species -- Fruit body -- Possible mechanisms -- Fruits
Аннотация: Mycelia of various Armillaria fungi are bioluminescent while the fruit bodies do not emit light. The presence in fruit bodies of Armillaria species of enzymes involved in the fungal bioluminescence was investigated by treating them with an exogenous analogue of the substrate for the light-emitting reaction. For this, hot extracts from nonluminous fungus Pholiota squarrosa were used. Upon spraying the pristine and transversely cut fruit bodies with the extracts, light emitting regions of different intensity were revealed. This suggests that the fruit bodies of the studied species are nonluminous due to lack of the substrate for light luminescent reaction. The prolonged incubation of the fruit bodies in water elevated the bioluminescence level. A possible mechanism which can explain this phenomenon is discussed. © 2021 Institute of Physics Publishing. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Federal Research Center for Information and Computational Technologies, Krasnoyarsk, 660049, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Burov, A. E.; Bondar, V. S.

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Transfer efficiency of carbon, nutrients, and polyunsaturated fatty acids in planktonic food webs under different environmental conditions / M. Karpowicz, I. Feniova, M. I. Gladyshev [et al.] // Ecol. Evol. - 2021, DOI 10.1002/ece3.7651. - Cited References:62. - This research was supported by the Polish National Science Centre (2016/21/B/NZ8/00434). The research was also supported by Federal Tasks for Institute of Biophysics SB RAS No. 51.1.1 and Federal Tasks for Siberian Federal University No. FSRG-2020-0019. The authors are thankful to Joanna Kozowska for her help in the collection of samples. . - Article in press. - ISSN 2045-7758

РУБ Ecology + Evolutionary Biology
Рубрики:
PHOSPHORUS STOICHIOMETRY
   LIGHT-INTENSITY
   ZOOPLANKTON
   TEMPERATURE
Кл.слова (ненормированные):
biogeochemical cycle -- dystrophication -- essential substances -- eutrophication -- food quality -- phytoplankton -- zooplankton
Аннотация: The trophic transfer efficiency (TTE) is an important indicator of ecosystem functioning. However, TTE data from freshwater food webs are ambiguous due to differences in time scales and methods. We investigated the transfer of essential substances (carbon, nutrients, and polyunsaturated fatty acids) through plankton communities in 30 Polish lakes with different trophic status in the middle of summer. The results of our study revealed that different essential substances were transferred from phytoplankton to zooplankton with varying efficiencies. The average TTE of C, N, P, and the sum of omega-3 PUFA were 6.55%, 9.82%, 15.82%, and 20.90%, respectively. Our results also show a large mismatch between the elemental and biochemical compositions of zooplankton and their food during the peak of the summer stagnation, which may further promote the accumulation of essential substances. There were also large differences in TTEs between trophic conditions, with the highest efficiencies in oligotrophic lakes and the lowest in dystrophic and eutrophic lakes. Therefore, our study indicates that disturbances like eutrophication and dystrophication similarly decrease the TTE of essential substances between phytoplankton and zooplankton in freshwater food webs.

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Держатели документа:
Univ Bialystok, Dept Hydrobiol, Fac Biol, Ciolkowskiego 1J, PL-15245 Bialystok, Poland.
Russian Acad Sci, Inst Ecol & Evolut, Moscow, Russia.
Russian Acad Sci, Krasnoyarsk Sci Ctr, Siberian Branch, Inst Biophys,Fed Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Polish Acad Sci, Nencki Inst Expt Biol, Res Stn Mikolajki, Warsaw, Poland.
Oklahoma State Univ, Dept Integrat Biol, Stillwater, OK 74078 USA.

Доп.точки доступа:
Karpowicz, Maciej; Feniova, Irina; Gladyshev, Michail I.; Ejsmont-Karabin, Jolanta; Gorniak, Andrzej; Sushchik, Nadezhda N.; Anishchenko, Olesya V.; Dzialowski, Andrew R.; Polish National Science Centre [2016/21/B/NZ8/00434]; Federal Tasks for Institute of Biophysics SB RAS [51.1.1]; Federal Tasks for Siberian Federal University [FSRG-2020-0019]

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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. Xu, T. Wang, G. Liu [et al.] // Sens Actuators, B Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991 . - ISSN 0925-4005
Кл.слова (ненормированные):
Binding kinetics -- FET -- Imatinib -- LMW drugs -- Single-crystal graphene -- Biosensors -- Biosynthesis -- Drug interactions -- Graphene -- Graphene transistors -- Proteins -- Single crystals -- Graphene field-effect transistors -- Graphene sheets -- Interaction kinetics -- Linear response -- Low molecular weight drugs -- Real time -- Small-molecule drugs -- Target proteins -- Field effect transistors
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 ?M range. This graphene-based FET biosensor (G-FET) was also applied to quantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs. © 2020 Elsevier B.V.

Scopus
Держатели документа:
Shandong Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, Dezhou, 253023, China
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Collaborative Innovation Center of Light Manipulations and Applications, Shandong Normal University, Jinan, 250358, China

Доп.точки доступа:
Xu, S.; Wang, T.; Liu, G.; Cao, Z.; Frank, L. A.; Jiang, S.; Zhang, C.; Li, Z.; Krasitskaya, V. V.; Li, Q.; Sha, Y.; Zhang, X.; Liu, H.; Wang, J.

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10.

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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11.

Luminescence Activity Decreases Whenv-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein-A Theoretical and Experimental Study / B. W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. J. Liu // Photochem. Photobiol. - 2020, DOI 10.1111/php.13280. - 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). . - Article in press. - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
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.

WOS
Держатели документа:
Beijing Normal Univ, Coll Chem, Key Lab Theoret & Computat Photochem, Minist Educ, Beijing, Peoples R China.
RAS, Photobiol Lab, Inst Biophys, SB,Fed Res Ctr,Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Ding, Bo-Wen; Eremeeva, Elena V.; Vysotski, Eugene S.; Liu, Ya-Jun; Vysotski, Eugene; 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]

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12.

    Effect of the level of irradiance on growth and content of photosynthetic pigments of Canadian Elodea (Elodea Canadensis) in model system “Water-Bottom Sediments” / Y. V. Aleksandrova, T. A. Zotina, N. A. Gaevsky // J. Sib. Fed. Univ. - Biol. - 2020. - Vol. 13, Is. 2. - С. 188-196, DOI 10.17516/1997-1389-0317 . - ISSN 1997-1389
   Перевод заглавия: Влияние светового фактора на рост и содержание фотосинтетических пигментов элодеи канадской (Elodea canadensis) в модельной системе «вода-донные отложения»
Кл.слова (ненормированные):
Aquatic plant -- Bioassay -- Bottom sediment -- Light saturation -- Photosynthetic pigments -- Root length -- Shoot length
Аннотация: Bioassays based on aquatic plants are a convenient tool for studying the quality of bottom sediments. One of the stages in the development of a bioassay is the selection of optimal growth conditions for indicator plants in a model test system. Response of indicator physiological endpoints of Canadian waterweed (Elodea canadensis) to light flux density was investigated to determine optimal irradiance level in a “water - sediment” model system, proposed previously for contact bioassay of natural bulk bottom sediments. Based on the response of shoot and root growth (length and weight), and concentration and ratio of photosynthetic pigments (chl. a, chl. b, and carotenoids) of Elodea to the change of light flux density, no limitation or inhibition of growth and photosynthesis of Elodea was revealed at light flux density from 56 to 143 µmol quanta • m-2 • s-1. Hence, the level of irradiance within this range can be recommended for use in the experimental system proposed for bioassay of bulk bottom sediments using E. canadensis as an indicator. © Siberian Federal University. All rights reserved

Scopus
Держатели документа:
Institute of Biophysics FRC, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University Krasnoyarsk, Russian Federation

Доп.точки доступа:
Aleksandrova, Y. V.; Zotina, T. A.; Gaevsky, N. A.

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13.

Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties / N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko [et al.] // Dokl. Biochem. Biophys. - 2020. - Vol. 490, Is. 1. - P38-42, DOI 10.1134/S1607672920010135. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASE-ACTIVITY
LIGHT-EMISSION
Кл.слова (ненормированные):
extracellular oxidases -- basidiomycete Neonothopanus nambi -- beta-glucosidase -- gel-filtration chromatography -- veratryl alcohol -- phenol -- FAD
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci, Inst Biophys,Fed Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Ronzhin, N. O.; Mogilnaya, O. A.; Artemenko, K. S.; Posokhina, E. D.; Bondar, V. S.

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14.

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - 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.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
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.

WOS
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; 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

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15.

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. - P1-22, DOI 10.3390/ijms21217846 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- BRET -- Calcium sensor -- GPCR assay -- Mutagenesis -- 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. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institut de Neurobiologie Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique (CNRS), Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
BioEmergences Unit, CNRS USR 3695, Universite Paris?Saclay, Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
Neuroscience Paris Seine ? Institut de Biologie Paris Seine (NPS ? IBPS), CNRS, UMR8246, INSERM U1130, Sorbonne Universite UM119, Paris, 75005, France
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Bakayan, A.; Picaud, S.; Malikova, N. P.; Tricoire, L.; Lambolez, B.; Vysotski, E. S.; Peyrieras, N.

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16.

Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
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.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

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17.

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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18.

Plants with genetically encoded autoluminescence / T. Mitiouchkina, A. S. Mishin, L. G. Somermeyer [et al.] // Nat. Biotechnol. - 2020, DOI 10.1038/s41587-020-0500-9. - Cited References:17. - This study was designed, performed and funded by Planta LLC. We thank K. Wood for assisting in manuscript development. Planta acknowledges support from the Skolkovo Innovation Centre. We thank D. Bolotin and the Milaboratory (milaboratory. com) for access to computing and storage infrastructure. We thank S. Shakhov for providing photography equipment. The Synthetic Biology Group is funded by the MRC London Institute of Medical Sciences (UKRI MC-A658-5QEA0, K.S.S.). K.S.S. is supported by an Imperial College Research Fellowship. Experiments were partially carried out using equipment provided by the Institute of Bioorganic Chemistry of the Russian Academy of Sciences.ore Facility (CKP IBCH; supported by the Russian Ministry of Education and Science Grant RFMEFI62117X0018). The F.A.K. lab is supported by ERC grant agreement 771209-CharFL. This project received funding from the European Union's Horizon 2020 Research and Innovation Programme under Marie Sklodowska-Curie Grant Agreement 665385. K.S.S. acknowledges support by President's Grant 075-15-2019-411. Design and assembly of some of the plasmids was supported by Russian Science Foundation grant 19-74-10102. Imaging experiments were partially supported by Russian Science Foundation grant 17-14-01169p. LC-MS/MS analyses of extracts were supported by Russian Science Foundation grant 16-14-00052p. Design and assembly of plasmids was partially supported by grant 075-15-2019-1789 from the Ministry of Science and Higher Education of the Russian Federation allocated to the Center for Precision Genome Editing and Genetic Technologies for Biomedicine. . - Article in press. - ISSN 1087-0156. - ISSN 1546-1696

РУБ Biotechnology & Applied Microbiology
Рубрики:
METABOLISM
LIBRARY
Аннотация: Autoluminescent plants engineered to express a bacterial bioluminescence gene cluster in plastids have not been widely adopted because of low light output. We engineered tobacco plants with a fungal bioluminescence system that converts caffeic acid (present in all plants) into luciferin and report self-sustained luminescence that is visible to the naked eye. Our findings could underpin development of a suite of imaging tools for plants.

WOS
Держатели документа:
Planta LLC, Moscow, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia.
IST Austria, Klosterneuburg, Austria.
Pirogov Russian Natl Res Med Univ, Moscow, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.
Aivok LLC, Moscow, Russia.
Bot Garden Lomonosov Moscow State Univ, Moscow, Russia.
MRC, Synthet Biol Grp, London Inst Med Sci, London, England.
Imperial Coll London, Inst Clin Sci, Fac Med, London, England.
Imperial Coll London, Imperial Coll Ctr Synthet Biol, London, England.

Доп.точки доступа:
Mitiouchkina, Tatiana; Mishin, Alexander S.; Somermeyer, Louisa Gonzalez; Markina, Nadezhda M.; Chepurnyh, Tatiana, V; Guglya, Elena B.; Karataeva, Tatiana A.; Palkina, Kseniia A.; Shakhova, Ekaterina S.; Fakhranurova, Liliia, I; Chekova, Sofia, V; Tsarkova, Aleksandra S.; Golubev, Yaroslav, V; Negrebetsky, Vadim V.; Dolgushin, Sergey A.; Shalaev, Pavel, V; Shlykov, Dmitry; Melnik, Olesya A.; Shipunova, Victoria O.; Deyev, Sergey M.; Bubyrev, Andrey, I; Pushin, Alexander S.; Choob, Vladimir V.; Dolgov, Sergey, V; Kondrashov, Fyodor A.; Yampolsky, Ilia, V; Sarkisyan, Karen S.; Tsarkova, Aleksandra; Planta LLC; Skolkovo Innovation Centre; MRC London Institute of Medical Sciences [UKRI MC-A658-5QEA0]; Imperial College Research Fellowship; Institute of Bioorganic Chemistry of the Russian Academy of Sciences.ore Facility (CKP IBCH - Russian Ministry of Education and Science Grant) [RFMEFI62117X0018]; ERC grant [771209-CharFL]; European Union's Horizon 2020 Research and Innovation Programme under Marie Sklodowska-Curie Grant [665385]; Russian Science Foundation grantRussian Science Foundation (RSF) [19-74-10102, 17-14-01169p, 16-14-00052p]; Ministry of Science and Higher Education of the Russian Federation [075-15-2019-1789]; [075-15-2019-411]

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19.

A noninvasive and qualitative bioluminescent assay for express diagnostics of athletes' responses to physical exertion / V. A. Kratasyuk, L. V. Stepanova, R. Ranjan [et al.] // Luminescence. - 2020, DOI 10.1002/bio.3954. - Cited References:33. - The Ministry of Science and Higher Education of the Russian Federation, Grant/Award Number: FSRZ-2020-0006; Krasnoyarsk Regional Foundation of Science, Grant/Award Number: KF-537 . - Article in press. - ISSN 1522-7235. - ISSN 1522-7243

РУБ Chemistry, Analytical
Рубрики:
SALIVARY BIOMARKERS
EXERCISE
Кл.слова (ненормированные):
athletes -- BLuc‐ -- Red coupled enzyme system -- catalase activity -- saliva -- training load
Аннотация: Upcoming professional sports authorities seek rapid noninvasive biosensing tools for regular monitoring of athletes' physiological states. The analysis of saliva through luminescence-based biosensors has been perceived as a suitable candidate for such purposes. The present study reports a qualitative bioluminescence assay based on a coupled enzyme system that consists of bacterial luciferase (BLuc) and nicotinamide adenine dinucleotide (NADH):flavin mononucleotide (FMN) oxidoreductase (Red), BLuc-Red, for the express diagnostics of athletes' stress levels before and after physical exertion. The volunteers who participated in the study were grouped as freestyle wrestlers and students who adapted to different levels of physical activities. Under physical exertion modelling conditions, the influence of participant saliva on BLuc-Red catalyzed light emission was investigated. Results showed a significant increase in residual luminescence (I-exp, mean maximum bioluminescence intensity of the experimental measurement (I-exp); I-c, luminescence intensity in control; I-exp/I-c, %) values for participants in the wrestler group while a decrease in the student group (P < 0.05). Such contrasting residual luminescence values in both groups were found to be dependent on the catalase activity of saliva. The proposed bioluminescence assay can be utilized as a potential nonspecific biosensing tool for determining the physical state of athletes under high loads.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Dept Biophys, Svobodny Prospect 79, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Akademgorodok 50-50, Akademgorodok, Russia.
Krasnoyarsk State Med Univ, Minist Hlth Russian Federat, Av Partizan Zheleznyak 1, Krasnoyarsk, Russia.
Krasnoyarsk Matern & Childhood Protect Ctr, Kirenskogo St 2a, Krasnoyarsk, Russia.
Siberian Fed Univ, Sch Nonferrous Met & Mat Sci, Svobodny Prospect 79, Krasnoyarsk, Russia.
Sci Res Inst Med Problems North, Av Partizan Zheleznyak 3g, Krasnoyarsk, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Stepanova, Lyudmila, V; Ranjan, Rajeev; Sutormin, Oleg S.; Pande, Shubhra; Zhukova, Galina, V; Miller, Olga M.; Maznyak, Natalya, V; Kolenchukova, Oksana A.; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; Krasnoyarsk Regional Foundation of Science [KF-537]

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20.

Luminescence Activity Decreases When v-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein—A Theoretical and Experimental Study / B. -W. Ding, E. V. Eremeeva, E. S. Vysotski, Y. -J. Liu // Photochem. Photobiol. - 2020, DOI 10.1111/php.13280 . - Article in press. - ISSN 0031-8655
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

Scopus
Держатели документа:
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Ding, B. -W.; Eremeeva, E. V.; Vysotski, E. S.; Liu, Y. -J.

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