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Spectral composition of light and plant productivity / A. A. Tikhomirov // Advances in Space Research. - 1996. - Vol. 18, Is. 4-5. - P259-263 . - ISSN 0273-1177
Кл.слова (ненормированные):
article -- biology -- cucumber -- growth, development and aging -- illumination -- light -- maize -- photon -- photosynthesis -- plant -- radiation exposure -- spectroscopy -- sunflower -- tomato -- wheat -- Cucumis sativus -- Helianthus -- Light -- Lighting -- Lycopersicon esculentum -- Photobiology -- Photons -- Photosynthesis -- Plants -- Spectrum Analysis -- Triticum -- Zea mays

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Academgorodok, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tikhomirov, A.A.

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

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

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

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

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LC-MS and microscale NMR analysis of luciferin-related compounds from the bioluminescent earthworm Fridericia heliota / S. M. Marques [et al.] // Journal of Photochemistry and Photobiology B: Biology. - 2011. - Vol. 102, Is. 3. - P218-223, DOI 10.1016/j.jphotobiol.2010.12.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Fridericia heliota -- Luciferin -- Microscale NMR -- RP-HPLC-MS -- alkene -- alkyl group -- benzothiazole -- carboxylic acid -- hydroxyl group -- luciferin -- pterin -- absorption -- article -- bioluminescence -- earthworm -- Fridericia heliota -- isomer -- molecular weight -- nonhuman -- nuclear magnetic resonance -- priority journal -- reversed phase high performance liquid chromatography -- ultraviolet radiation -- Animals -- Chromatography, High Pressure Liquid -- Chromatography, Reverse-Phase -- Firefly Luciferin -- Luminescent Agents -- Magnetic Resonance Spectroscopy -- Mass Spectrometry -- Oligochaeta -- Fridericia heliota
Аннотация: This paper presents the main results of RP-HPLC-MS and microscale NMR analysis performed on Accompanying similar to Luciferin (AsLn(x)), compounds present in extracts of the bioluminescent earthworm Fridericia heliota that display similarities with Fridericia's luciferin, the substrate of the bioluminescent reaction. Three isomers of AsLn were discovered, AsLn(1), AsLn(2) and AsLn(3), all of which present a molecular weight of 529 Da. Their UV-Vis absorption spectra show maxima at 235 nm for AsLn(1), 238 and 295 nm for AsLn(2) and 241 and 295 nm for AsLn(3). MS n fragmentation patterns suggest the existence of carboxylic acid and hydroxyl moieties, and possibly chemical groups found in other luciferins like pterin or benzothiazole. The major isomer, AsLn(2), presents an aromatic ring and alkene and alkyl moieties. These luciferin-like compounds can be used as models that could give further insights into the structure of this newly discovered luciferin. В© 2010 Elsevier Inc. All rights reserved.

Scopus
Держатели документа:
Department of Chemistry and Biochemistry, Faculty of Sciences, Universidade Do Porto, Rua do Campo Alegre 687, 4169-007 Porto, Portugal
Laboratory of Photobiology, Institute of Biophysics, Russian Academy of Sciences, Akademgorodok, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Marques, S.M.; Petushkov, V.N.; Rodionova, N.S.; Esteves Da Silva, J.C.G.

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Purification and partial spectral characterization of a novel luciferin from the luminous enchytraeid Fridericia heliota / V. N. Petushkov, N. S. Rodionova // Journal of Photochemistry and Photobiology B: Biology. - 2007. - Vol. 87, Is. 2. - P130-136, DOI 10.1016/j.jphotobiol.2007.03.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Enchytraeid -- Luciferase -- Luciferin -- adenosine triphosphate -- luciferase -- luciferin -- animal cell -- anion exchange chromatography -- annelid worm -- article -- controlled study -- earthworm -- firefly -- luminance -- luminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- radiation absorption -- reversed phase liquid chromatography -- ultraviolet radiation -- Adenosine Triphosphate -- Animals -- Luciferases -- Luminescent Agents -- Oligochaeta -- Spectrum Analysis -- Enchytraeidae -- Fridericia heliota
Аннотация: A homogeneous luciferin preparation has been obtained from the luminous soil enchytraeid Fridericia heliota, which has an ATP-dependent luminescent system. A procedure for luciferin purification without losing fractions of active luciferase has been developed. The luciferin specific activity is 4000 times increased; its UV absorption spectrum maximum is 294 nm with a local minimum at 262 nm. The luciferin of the enchytraeid F. heliota is significantly different from firefly luciferin, whose luminescent reaction also requires ATP, and it also appears to have no similarities to other known luciferins. В© 2007 Elsevier B.V. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Rodionova, N.S.

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Effect of different salts and detergents on luciferin-luciferase luminescence of the enchytraeid Fridericia heliota / N. S. Rodionova, V. N. Petushkov // Journal of Photochemistry and Photobiology B: Biology. - 2006. - Vol. 83, Is. 2. - P123-128, DOI 10.1016/j.jphotobiol.2005.12.014 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Ions -- Luciferin-luciferase systems -- Triton X-100 -- adenosine triphosphate -- anion -- bromine -- calcium ion -- carbonic acid -- cation -- chloride -- chromium derivative -- detergent -- dodecyl sulfate sodium -- inorganic salt -- iodine -- iron derivative -- luciferase -- luciferin -- magnesium ion -- manganese -- nitrate -- phosphate -- sulfate -- sulfite -- triton x 100 -- annelid worm -- article -- bioluminescence -- concentration (parameters) -- controlled study -- enzyme activation -- enzyme activity -- enzyme inhibition -- enzyme mechanism -- in vitro study -- nonhuman -- priority journal -- qualitative analysis -- quantitative analysis -- Adenosine Triphosphate -- Animals -- Cations, Divalent -- Cations, Monovalent -- Detergents -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescence -- Metals -- Oligochaeta -- Photobiology -- Salts -- Annelida -- Clitellata -- earthworms (sp.) -- Enchytraeidae -- Fridericia heliota -- Oligochaeta (Metazoa) -- Pheretima sieboldi
Аннотация: The study addresses the effect produced by different inorganic salts and detergents (SDS, Triton X-100, the Tween series) on the ATP-dependent bioluminescent reaction catalyzed by the luciferase of the new earthworm species Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae). It has been shown that the effect of divalent metal salts on luminescence is determined by the action of cations. Three of them - Mg2+, Mn2+ and Ca2+ - can stimulate luciferase activity at concentrations varying within a wide range, and Mn2+ can act as a 100%-effective substitute for Mg2+ in F. heliota luminescence reaction in vitro. The inhibitory effect of monovalent metal salts on luminescence is largely determined by the action of the anion part of the molecule. The effectiveness of the inhibitory effect of anions increases in the following order: {Mathematical expression}. Of the sodium salts, dodecyl sulfate, which is an anionic detergent, produces the strongest inhibitory effect on luciferase. On the contrary, nonionic detergents produce a stimulatory effect on the F. heliota luciferase. The action of the most effective of them - Triton X-100 - is determined by its ability to reduce the actual concentration of lipid inhibitors in the reaction mixture. В© 2006 Elsevier B.V. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodionova, N.S.; Petushkov, V.N.

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Estimation of energy of the upper electron-excited states of the bacterial bioluminescent emitter [Text] / N. S. Kudryasheva [et al.] // J. Photochem. Photobiol. B-Biol. - 2002. - Vol. 68, Is. 02.03.2013. - P. 88-92, DOI 10.1016/S1011-1344(02)00360-3. - Cited References: 25 . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MECHANISM
Кл.слова (ненормированные):
bioluminescence -- electron-excited states -- energy transfer
Аннотация: The hypothesis of activity of the upper electron-excited states of the bacterial bioluminescent emitter was verified using dye molecules as foreign energy acceptors. Six compounds were selected having fluorescent state energies ranging from 25 700 to 32 000 cm(-1) (anthracene, pyrene, 1.4-bis(5-phenyloxasol-2-yl)benzene (POPOP), p-bis(o-methylstyryl)benzene (MSB), 2-methoxy-naphtalene, p-terphenyl), exceeding that of the bioluminescent emitter (22 000 cm(-1)). Their absorption spectra do not overlap with the bioluminescence spectrum; the trivial light absorption and the intermolecular resonance S-S energy transfer were excluded. Bacterial bioluminescent spectra of the coupled enzyme system NADH:FMN-oxidoreductase-luciferase in the presence of MSB were presented as an example. The weak sensitized fluorescence of MSB was registered. The results obtained have confirmed the activity of the energetic precursor in the bacterial bioluminescence. Its energy can be located in the interval of 26 000-27 000 cm(-1). (C) 2002 Published by Elsevier Science B.V.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Akademgorodok 660036, Krasnoyarsk, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660049, Russia
Wageningen Univ, Microspect Ctr, Dept Biomol Sci, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Nemtseva, E.V.; Sizykh, A.G.; Kratasyuk, V.A.; Visser, AJWG

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Effects of potassium halides on bacterial bioluminescence [Text] / M. A. Gerasimova, N. S. Kudryasheva // J. Photochem. Photobiol. B-Biol. - 2002. - Vol. 66, Is. 3. - P. 218-222, DOI 10.1016/S1011-1344(02)00240-3. - Cited References: 20 . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
COMPONENTS
SEWAGE
Кл.слова (ненормированные):
bioluminescence -- halides -- heavy atom -- inhibition -- activation
Аннотация: The effects of potassium halides KCl, KBr and KI on NADH:FMN-oxidoreductase-luciferase bioluminescent coupled enzyme system were studied. The influence of salt additions on bioluminescence intensity and bioluminescence light yield was investigated. The inhibition and activation parameters of the salts were calculated using their dependencies on concentration of the salts. The correlation between the inhibition of bioluminescence intensity and the halide mass was demonstrated: the inhibiting ability of the salts increases with the increase of atomic weight of the anions. The inhibition parameters increase and the activation parameters decrease, accordingly. (C) 2002 Elsevier Science B.V. All rights reserved.

WOS
Держатели документа:
Krasnoyarsk State Univ, Dept Quantum Elect, Krasnoyarsk 660041, Russia
RAS, SB, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gerasimova, M.A.; Kudryasheva, N.S.

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

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

Доп.точки доступа:
Malikova, N. P.; Borgdorff, A. J.; Vysotski, E. S.
Свободных экз. нет
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All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

Scopus,
WOS
Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
Свободных экз. нет
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10.

Creation of artificial luciferases to expand their analytical potential / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioimaging -- Bioluminescence -- Luciferase -- Luciferase-based assay -- Luciferin -- Mutagenesis -- Photoprotein -- Reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescencebased analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnii ave., 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Frank, L. A.

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11.

Simultaneous genotyping of four single nucleotide polymorphisms associated with risk factors of hemostasis disorders / E. E. Bashmakova, V. V. Krasitskaya, L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P930-936 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescent microassay -- Multiplex PCR -- PEXT reaction -- Photoprotein obelin -- SNP detection
Аннотация: Multiplex simultaneous genotyping technique was developed for four polymorphisms in genes coding for blood coagulation factors and homocysteine metabolism which are considered as thrombophilia related mutations: FV Leiden, FII G20210A, MTHFR C677T, and FVII G10976A. It is based on primer extension reaction with the following bioluminescent solid-phase microassay. At that, two different in bioluminescence obelin mutants were applied to simultaneous detection of two gene allelic variants. The assay is carried out in microtiter plate format and provides fast and reliable genotyping of four single nucleotide polymorphisms in four different genes within 2.5 hours. A large number of clinical samples were analyzed and the obtained results were found to be in complete correlation with those obtained by using conventional RT-PCR techniques. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Bashmakova, E. E.; Krasitskaya, V. V.; Frank, L. A.

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12.

Applications of luminous bacteria enzymes in toxicology / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescence -- Bioluminescent toxicity enzymatic assay -- Immobilization of enzymes -- Luciferase -- Total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation
Photobiology Laboratory, Russian Academy of Sciences, Siberian Branch, Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kratasyuk, V. A.; Esimbekova, E. N.

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13.

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

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

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

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14.

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

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

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

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15.

Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 162. - P286-297, DOI 10.1016/j.jphotobiol.2016.06.054 . - ISSN 1011-1344
Аннотация: The full-length cDNA genes encoding five new isoforms of Ca2 +-regulated photoprotein mitrocomin from a small tissue sample of the outer bell margin containing photocytes of only one specimen of the luminous jellyfish Mitrocoma cellularia were cloned, sequenced, and characterized after their expression in Escherichia coli and subsequent purification. The analysis of cDNA nucleotide sequences encoding mitrocomin isoforms allowed suggestion that two isoforms might be the products of two allelic genes differing in one amino acid residue (64R/Q) whereas other isotypes appear as a result of transcriptional mutations. In addition, the crystal structure of mitrocomin was determined at 1.30 A resolution which expectedly revealed a high similarity with the structures of other hydromedusan photoproteins. Although mitrocomin isoforms reveal a high degree of identity of amino acid sequences, they vary in specific bioluminescence activities. At that, all isotypes displayed the identical bioluminescence spectra (473–474 nm with no shoulder at 400 nm). Fluorescence spectra of Ca2 +-discharged mitrocomins were almost identical to their light emission spectra similar to the case of Ca2 +-discharged aequorin, but different from Ca2 +-discharged obelins and clytin which fluorescence is red-shifted by 25–30 nm from bioluminescence spectra. The main distinction of mitrocomin from other hydromedusan photoproteins is an additional Tyr at the C-terminus. Using site-directed mutagenesis, we showed that this Tyr is not important for bioluminescence because its deletion even increases specific activity and efficiency of apo-mitrocomin conversion into active photoprotein, in contrast to C-terminal Pro of other photoproteins. Since genes in a population generally exist as different isoforms, it makes us anticipate the cloning of even more isoforms of mitrocomin and other hydromedusan photoproteins with different bioluminescence properties. © 2016 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
iHuman Institute, ShanghaiTech University, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Markova, S. V.; Eremeeva, E. V.; Malikova, N. P.; Cheng, C.; Liu, Z. -J.; Vysotski, E. S.

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16.

Dissolution and mixing of flavin mononucleotide in microfluidic chips for bioassay / K. I. Belousov [et al.] // J. Phys. Conf. Ser. - 2016. - Vol. 741, Is. 1, DOI 10.1088/1742-6596/741/1/012058 . - ISSN 1742-6588
Кл.слова (ненормированные):
Bioassay -- Biomolecules -- Dissolution -- Flow of fluids -- Fluidic devices -- Microfluidics -- Nanostructures -- Optoelectronic devices -- Oscillating flow -- Photonics -- Analysis of liquids -- Concentration distributions -- Constant flow rates -- Flavin mono nucleotides (FMN) -- Flavin mononucleotides -- Frequency of oscillation -- Uniform distribution -- Variable flow rate -- Mixing
Аннотация: Dissolution and mixing of flavin mononucleotide (FMN), which activates a luminescent reaction, were considered in various designs of microfluidic chip for pollution analysis of liquid samples. The aim was to determine the velocity mode of fluid flow ensured the uniform distribution of the FMN in the reaction chamber. Simulation of concentration distribution of FMN in various designs of microfluidic chips was conducted. It was shown that the passive mixing techniques based on the constant flow rate didn't provide mixing of FMN in acceptable time (3 seconds). The most efficient mixing was achieved using variable flow rate with a gradually increasing frequency of oscillation. © Published under licence by IOP Publishing Ltd.

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Держатели документа:
Department of Material Science and Nanotechnology, ITMO University, St. Petersburg, Russian Federation
Department of Biophysics, Siberian Federal University, Krasnoyarsk, Russian Federation
Nanobiotech Lab, St. Petersburg Academic University, St. Petersburg, Russian Federation
Laboratory of Photobiology, Institute of Biophysics SB RAS, Krasnoyarsk, Russian Federation
Laboratory of Information and Measurement Biosensor and Chemosensor Microsystems, Institute for Analytical Instrumentation RAS, St. Petersburg, Russian Federation

Доп.точки доступа:
Belousov, K. I.; Denisov, I. A.; Lukyanenko, K. A.; Yakimov, A. S.; Bukatin, A. S.; Kukhtevich, I. V.; Sorokin, V. V.; Esimbekova, E. N.; Belobrov, P. I.; Evstrapov, A. A.

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17.

Mutants of Ca2+-regulated Photoprotein Obelin for Site-specific Conjugation / V. V. Krasitskaya [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P553-557, DOI 10.1111/php.12712 . - ISSN 0031-8655
Аннотация: Color variants of Ca2+-regulated photoprotein obelin were shown to be an important tool for dual-analyte binding assay. To provide site-directed conjugation with biospecific molecules, several obelin color mutants carrying unique cysteine residues were obtained and characterized for their novel properties. A pair of obelins Y138F,A5C and W92F,H22E,D12C was found to be most suitable (in terms of high bioluminescent activity and stability) as reporters in simultaneous assay of two targets in a sample. Availability of SH-groups, accessible for chemical modification, essentially simplifies the synthesis of biospecific conjugates, increases their yield and conserves obelins' bioluminescence activity. Conjugates with immunoglobulin and oligonucleotide were produced and successfully applied in single nucleotide polymorphism genotyping. © 2017 The American Society of Photobiology

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Burakova, L. P.; Komarova, A. A.; Bashmakova, E. E.; Frank, L. A.

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18.

Bioluminescence: Basic and Applied Research.: Introduction to the Special Issue on Bioluminescence / E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P387-388, DOI 10.1111/php.12736 . - ISSN 0031-8655

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

Доп.точки доступа:
Vysotski, E. S.

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19.

Hybrid Minimal Core Streptavidin–Obelin as a Versatile Reporter for Bioluminescence-based Bioassay / E. E. Bashmakova [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P548-552, DOI 10.1111/php.12648 . - ISSN 0031-8655
Аннотация: Ca2+-regulated photoprotein obelin was genetically fused with a minimum-sized core streptavidin. Hybrid protein (SAV–OL) was produced by bacterial expression and applied as a specific bioluminescent probe in diverse solid-phase assays. The obtained results clearly demonstrate specific activity of each domain indicating its proper folding with favorable space orientation. SAV–OL has been shown to be a much more sensitive label than the chemical conjugate of a full-length streptavidin with obelin. © 2016 The American Society of Photobiology

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Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Chemistry Department, Lomonosov Moscow State University, Moscow, Russian Federation

Доп.точки доступа:
Bashmakova, E. E.; Krasitskaya, V. V.; Kudryavtsev, A. N.; Grigorenko, V. G.; Frank, L. A.

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20.

Progress in the Study of Bioluminescent Earthworms / N. S. Rodionova [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P416-428, DOI 10.1111/php.12709 . - ISSN 0031-8655
Аннотация: Even though bioluminescent oligochaetes rarely catch people's eyes due to their secretive lifestyle, glowing earthworms sighting reports have come from different areas on all continents except Antarctica. A major breakthrough in the research of earthworm bioluminescence occurred in the 1960s with the studies of the North American Diplocardia longa. Comparative studies conducted on 13 earthworm species belonging to six genera showed that N-isovaleryl-3-aminopropanal (Diplocardia luciferin) is the common substrate for bioluminescence in all examined species, while luciferases appeared to be responsible for the color of bioluminescence. The second momentous change in the situation has occurred with the discovery in Siberia (Russia) of two unknown luminous enchytraeids. The two bioluminescent systems belong to different types, have different spectral characteristics and localization, and different temperature and pH optima. They are unique, and this fact is confirmed by the negative results of all possible cross-reactions. The bioluminescent system of Henlea sp. comprises four essential components: luciferase, luciferin, oxygen and calcium ion. For Friderica heliota, the luminescent reaction requires five components: luciferase, luciferin, ATP, magnesium ion and oxygen. Along with luciferin, more than a dozen analogues were isolated from worm biomass. These novel peptide-like natural compounds represent an unprecedented chemistry found in terrestrial organisms. © 2017 The American Society of Photobiology

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Держатели документа:
Laboratory of Photobiology, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Department of Physics, Earth and Environmental Sciences, University of Siena, Siena, Italy
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
Pirogov Russian National Research Medical University, Moscow, Russian Federation

Доп.точки доступа:
Rodionova, N. S.; Rota, E.; Tsarkova, A. S.; Petushkov, V. N.

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