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Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase [Text] / G. A. Stepanyuk [et al.] // Anal. Bioanal. Chem. - 2010. - Vol. 398, Is. 4. - P1809-1817, DOI 10.1007/s00216-010-4106-9. - Cited References: 39. - This work was supported by grant 09-04-12022 of the Russian Foundation for Basic Research, "Molecular and Cell Biology" program of Russian Academy of Sciences, by the SB RAS grant No. 2, and by the SB RAS Lavrentiev grant for Young Scientists. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
GREEN-FLUORESCENT PROTEIN
   BIOLUMINESCENT REPORTER
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   RECOMBINANT OBELIN
   GENE-EXPRESSION
   IN-VIVO
   CDNA
   CLONING
   PURIFICATION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Calcium -- Imaging
Аннотация: It has been shown that the coelenterazine analog, coelenterazine-v, is an efficient substrate for a reaction catalyzed by Renilla luciferase. The resulting bioluminescence emission maximum is shifted to a longer wavelength up to 40 nm, which allows the use of some "yellow" Renilla luciferase mutants for in vivo imaging. However, the utility of coelenterazine-v in small-animal imaging has been hampered by its instability in solution and in biological tissues. To overcome this drawback, we ligated coelenterazine-v to Ca2+-triggered coelenterazine-binding protein from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The coelenterazine-v bound within coelenterazine-binding protein has revealed a greater long-term stability at both 4 and 37 degrees C. In addition, the coelenterazine-binding protein ligated by coelenterazine-v yields twice the total light over free coelenterazine-v as a substrate for the red-shifted R. muelleri luciferase. These findings suggest the possibility for effective application of coelenterazine-v in various in vitro assays.

Держатели документа:
[Stepanyuk, Galina A.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Unch, James] Promega Biosci LLC, San Luis Obispo, CA 93401 USA
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Unch, J...; Malikova, N.P.; Markova, S.V.; Lee, J...; Vysotski, E.S.

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On possible biological function of cadmium as analog of calcium [Текст] / V. S. Bondar // Dokl. Akad. Nauk. - 1997. - Vol. 352, Is. 5. - С. 693-694. - Cited References: 12 . - ISSN 0869-5652

РУБ Multidisciplinary Sciences
Рубрики:
PHOTOPROTEIN OBELIN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondar, V.S.

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CompX, a luciferin-related tyrosine derivative from the bioluminescent earthworm Fridericia heliota. Structure elucidation and total synthesis / V. N. Petushkov [et al.] // Tetrahedron Letters. - 2014. - Vol. 55, Is. 2. - P460-462, DOI 10.1016/j.tetlet.2013.11.064 . - ISSN 0040-4039
Кл.слова (ненормированные):
Bioluminescence -- Enchytraeid -- Luciferin -- Total synthesis
Аннотация: A luciferin analog, CompX, was isolated from the extracts of the bioluminescent earthworm Fridericia heliota. Its structure was determined as (Z)-5-(2-carboxy-2-methoxyvinyl)-2-hydroxybenzoic acid by spectroscopic data analysis and was confirmed by total synthesis. The (Z)-configuration of the double bond was established by comparing the ROESY spectra of CompX with those of its synthetic (E)-isomer. CompX represents a tyrosine analog, not previously found in natural sources, and is probably derived from tyrosine by deamination, O-methylation of the resulting alpha-keto acid, and carboxylation at the aromatic core. © 2013 Elsevier Ltd. All rights reserved.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi, 79, Krasnoyarsk 660041, Russian Federation
Laboratory of Photobiology, Institute of Biophysics, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation
Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, Campo Alegre St. 687, Porto 4169-007, Portugal
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Tsarkova, A.S.; Dubinnyi, M.A.; Rodionova, N.S.; Marques, S.M.; Esteves Da Silva, J.C.G.; Shimomura, O.; Yampolsky, I.V.

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THE LOCALIZATION OF LUMINESCENT SYSTEM OF LUMINOUS BACTERIA [Текст] / O. A. KUDRYAVTSEVA [и др.] // Biofizika. - 1993. - Vol. 38, Is. 3. - P. 435-439. - Cited References: 10 . - ISSN 0006-3029

РУБ Biophysics

Аннотация: A method for localization of a light source near the interface of two media is described. The method is based on an optical analog of tunnel effect when the radiation source is at the distance smaller than the wavelength from the interface. Application of the tunnel effect permits to obtain high resolution. The developed method was used to determine the localization of a bacterial luminescent system. It has been found that the sources of bioluminescence are located at thin subsurfase lager with width about 70 nm. This result is in favour of the peripheral (periplasmatic or membrane) localization of the bacterial luminescent system. This method makes it possible to investigate processes pelated to light radiation (luminescence, fluorescence and other optical processes) in a thin surface layer of various biological and physical objects.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
KUDRYAVTSEVA, O.A.; BARTSEV, S.I.; OKHONIN, V.A.; MEZHEVIKIN, V.V.

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Biochemical changes causes lack of bioluminescence in fruiting bodies of Armillaria / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2017. - Vol. 8, Is. 1. - P9-17, DOI 10.5943/mycosphere/8/1/2 . - ISSN 2077-7000
Кл.слова (ненормированные):
Enzymes and substrate of luminescent reaction -- Kinetics of luminescence -- Luminous mycelia -- Nonluminous fruiting bodies of fungus
Аннотация: Mycelium of Armillaria species exhibit bioluminescence in nature and when cultivated on artificial nutrient media. However, fruiting bodies do not emit visible light. The present study investigates biochemical changes which cause this phenomenon. Light emission was studied in experiments with mixtures of cold and hot extracts of the luminous mycelium of Armillaria borealis IBSO 2328 and nonluminous fruiting bodies of this fungus and an unidentified species of the genus (Armillaria sp.). Hot extracts of fruiting bodies of the nonluminous Pholiota squarrosa were used as the substrate analog of the luminescent reaction, as previously this fungus had been found to contain a high amount of this substance. Control experiments showed that cold extracts of A. borealis IBSO 2328 mycelium contained enzymes for the luminescent reaction, which is initiated after addition hot extracts of P. squarrosa fruiting bodies. Parallel experiments with extracts of the fruiting bodies of Armillaria showed that: (i) - cold extracts did not contain enzymes of the luminescent reaction or contain very small amounts of these enzymes and (ii) - hot extracts did not contain substrate of the luminescent reaction. Thus, the reason why fruiting bodies of Armillaria do not emit light is that they do not contain components required for visible luminescence. The study discusses possible causes why the enzymes and substrate of the luminescent reaction are not synthesized in fruiting bodies of Armillaria. © Guizhou Academy of Agricultural Sciences.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Akademgorodok, Krasnoyarsk, Russian Federation

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

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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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α-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp. / M. A. Dubinnyi, I. A. Ivanov, N. S. Rodionova [et al.] // ChemistrySelect. - 2020. - Vol. 5, Is. 42. - P13155-13159, DOI 10.1002/slct.202003075 . - ISSN 2365-6549
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Henlea -- Natural products -- NMR spectroscopy
Аннотация: Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as ?-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophan-containing compounds are possible participants of bioluminescence-related metabolism in Henlea sp. © 2020 Wiley-VCH GmbH

Scopus
Держатели документа:
Shemyakin-Ovchinnikov Institute of bioorganic chemistry, Russian academy of Sciences GSP-7, Miklukho-Maklaya str., 16/10, Moscow, 117997, Russian Federation
Institute of Biophysics, Krasnoyarsk Research Center, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Pirogov Russian National Research Medical University, 1 Ostrovityanova st., Moscow, 117997, Russian Federation

Доп.точки доступа:
Dubinnyi, M. A.; Ivanov, I. A.; Rodionova, N. S.; Kovalchuk, S. I.; Kaskova, Z. M.; Petushkov, V. N.

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alpha-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp. / M. A. Dubinnyi, I. A. Ivanov, N. S. Rodionova [et al.] // ChemistrySelect. - 2020. - Vol. 5, Is. 42. - P13155-13159, DOI 10.1002/slct.202003075. - Cited References:49. - This work was supported by the State Assignment for Basic Research of the Russian Academy of Sciences (project no. 0356-2019-0019) and the Russian Foundation for Basic Research (project no. 19-04-00348-a). . - ISSN 2365-6549

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
   MANNOSYLATION
   TRYPTOPHAN
   PROTEIN
   COMPLEMENT
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Henlea -- Natural products -- NMR spectroscopy
Аннотация: Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as alpha-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophan-containing compounds are possible participants of bioluminescence-related metabolism in Henlea sp.

WOS
Держатели документа:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, GSP-7,Miklukho Maklaya Str 16-10, Moscow 117997, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Res Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Pirogov Russian Natl Res Med Univ, 1 Ostrovityanova St, Moscow 117997, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Ivanov, Igor A.; Rodionova, Natalia S.; Kovalchuk, Sergey I.; Kaskova, Zinaida M.; Petushkov, Valentin N.; State Assignment for Basic Research of the Russian Academy of Sciences [0356-2019-0019]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-04-00348-a]

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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.

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

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

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