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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Esimbekova E. N., Nemtseva E. V., Kirillova M. A., Asanova A. A., Kratasyuk V. A.
Заглавие : Bioluminescent assay for toxicological assessment of nanomaterials
Колич.характеристики :4 с
Коллективы : Russian Science Foundation [16-14-10115]
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2017. - Vol. 472, Is. 1. - С. 60-63. - ISSN 1607-6729, DOI 10.1134/S1607672917010173. - ISSN 1608-3091(eISSN)
Примечания : Cited References:15. - We are sincerely grateful to the staff of the Institute of Physiological Active Compounds (Kharkiv, Ukraine) for providing fullerene samples. This study was supported by the Russian Science Foundation (project no. 16-14-10115).
Предметные рубрики: LUMINOUS BACTERIA
TOXICITY
Аннотация: A new method for assessing biotoxicity of nanomaterials, based on the use of soluble bioluminescent coupled enzyme system NAD(P)ai...H:FMN oxidoreductase and luciferase, is proposed. The results of this study indicate a significant adverse biological effect exerted by nanoparticles at the molecular level. It was found that the most toxic nanoparticles the nanoparticles are based on copper and copper oxide, as well as single-walled carbon nanotubes and multi-walled carbon nanofibers, which are referred to hazard class II.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryasheva, Nadezhda S., Kovel, Ekaterina S., Sachkova, Anna S., Vorobeva, Anna A., Isakova, Viktoriya G., Churilov, Grigoriy N.
Заглавие : Bioluminescent Enzymatic Assay as a Tool for Studying Antioxidant Activity and Toxicity of Bioactive Compounds
Колич.характеристики :5 с
Коллективы : Russian Foundation for Basic Research [15-03-06786, 15-43-04377-sibir]; Russian Academy of Sciences [01201351504]
Место публикации : Photochem. Photobiol.: WILEY, 2017. - Vol. 93, Is. 2. - С. 536-540. - ISSN 0031-8655, DOI 10.1111/php.12639. - ISSN 1751-1097(eISSN)
Примечания : Cited References:40. - The work was supported by the Russian Foundation for Basic Research, Grants 15-03-06786 and 15-43-04377-sibir; the state budget allocated to the fundamental research at the Russian Academy of Sciences (project 01201351504).
Предметные рубрики: LUMINOUS MARINE-BACTERIA
HUMIC SUBSTANCES
DETOXIFICATION PROCESSES
Аннотация: A bioluminescent assay based on a system of coupled enzymatic reactions catalyzed by bacterial luciferase and NADH:FMN-oxidoreductase was developed to monitor toxicity and antioxidant activity of bioactive compounds. The assay enables studying toxic effects at the level of biomolecules and physicochemical processes, as well as determining the toxicity of general and oxidative types. Toxic and detoxifying effects of bioactive compounds were studied. Fullerenols, perspective pharmaceutical agents, nanosized particles, water-soluble polyhydroxylated fullerene-60 derivatives were chosen as bioactive compounds. Two homologous fullerenols with different number and type of substituents, C60O2-4(OH)(20-24) and Fe0.5C60(OH) O-x(y) (x + y = 40-42), were used. They suppressed bioluminescent intensity at concentrations 0.01 g L-1 and 0.001 g L-1 for C60O2-4(OH)(20-24) and Fe0.5C60(OH)(x)O-y, respectively; hence, a lower toxicity of C60O2-4(OH)(20-24) was demonstrated. Antioxidant activity of fullerenols was studied in model solutions of organic and inorganic oxidizers; changes in toxicities of general and oxidative type were determined; detoxification coefficients were calculated. Fullerenol C60O2-4(OH)(20-24) revealed higher antioxidant ability at concentrations 10(-17)-10(-5) g L-1. The difference in the toxicity and antioxidant activity of fullerenols was explained through their electron donor/acceptor properties and different catalytic activity. Principles of bioluminescent enzyme assay application for evaluating the toxic effect and antioxidant activity of bioactive compounds were summarized and the procedure steps were described.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko, Kirill A., Belousov, Kirill I., Denisov, Ivan A., Yakimov, Anton S., Esimbekova, Elena N., Bukatin, Anton S., Evstrapov, Anatoly A., Belobrov, Peter I.
Заглавие : Active mixing of immobilised enzymatic system in microfluidic chip
Колич.характеристики :5 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Micro Nano Lett.: INST ENGINEERING TECHNOLOGY-IET, 2017. - Vol. 12, Is. 6. - С. 377-381. - ISSN 1750-0443, DOI 10.1049/mnl.2016.0646
Примечания : Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041).
Предметные рубрики: POLY(METHYL METHACRYLATE)
SURFACE MODIFICATION
POINT
DEVICES
PMMA
Аннотация: Parameters for sample introduction, dried reagents dissolution and mixing with sample for bienzyme system NAD(H):FMN-oxidoreductase and luciferase immobilised in microfluidic chip were successfully determined. Numerical simulations of reaction chamber geometry, flavin mononucleotide (FMN) escape from starch gel and mixing options were conducted to achieve higher sensitivity of bioluminescent reaction. Results of numerical simulations were verified experimentally. The active mixer for dried reagents was made from an electro-mechanical speaker's membrane which was connected to the input of the chip. Such a mixer provided better efficiency than a passive mixing, and it is simple enough for use in point-of-care devices with any systems based on immobilised enzymes in chips.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Purtov K. V., Petushkov V. N., Rodionova N. S., Gitelson J. I.
Заглавие : Why does the bioluminescent fungus Armillaria mellea have luminous mycelium but nonluminous fruiting body?
Место публикации : Doklad. Biochem. Biophys.: Maik Nauka Publishing / Springer SBM, 2017. - Vol. 474, Is. 1. - С. 217-219. - ISSN 16076729 (ISSN) , DOI 10.1134/S1607672917030176
Аннотация: By determining the components involved in the bioluminescence process in luminous and nonluminous organs of the honey fungus Armillaria mellea, we have established causes of partial luminescence of this fungus. The complete set of enzymes and substrates required for bioluminescence is formed only in the mycelium and only under the conditions of free oxygen access. Since the synthesis of luciferin precursor (hispidin) and 3-hydroxyhispidin hydroxylase in the fruiting bodies is blocked, the formation of luciferin—the key component of fungal bioluminescent system—was not observed. That is why the fruiting body of Armillaria mellea is nonluminous despite the presence of luciferase, the enzyme that catalyzes the oxidation of luciferin with a photon emission. © 2017, Pleiades Publishing, Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kaskova, Zinaida M., Dorr, Felipe A., Petushkov, Valentin N., Purtov, Konstantin V., Tsarkova, Aleksandra S., Rodionova, Natalja S., Mineev, Konstantin S., Guglya, Elena B., Kotlobay, Alexey, Baleeva, Nadezhda S., Baranov, Mikhail S., Arseniev, Alexander S., Gitelson, Josef I., Lukyanov, Sergey, Suzuki, Yoshiki, Kanie, Shusei, Pinto, Ernani, Di Mascio, Paolo, Waldenmaier, Hans E., Pereira, Tatiana A., Carvalho, Rodrigo P., Oliveira, Anderson G., Oba, Yuichi, Bastos, Erick L., Stevani, Cassius V., Yampolsky, Ilia V.
Заглавие : Mechanism and color modulation of fungal bioluminescence
Колич.характеристики :8 с
Коллективы : Sao Paulo Research Foundation [FAPESP] [10/11578-5, 13/16885-1, 14/14866-2, 13/07914-8, 2012/12663-1]; CEPID Redoxoma [2013/07937-8]; National Council for Scientific and Technological Development (CNPq) [301307/2013-0]; NAP Redoxoma (PRPUSP) [2011.1.9352.1.8]; Japan Society for the Promotion of Science [16K07715]; Chubu University [AII28II M01]; Russian Science Foundation [16-14-00052]
Место публикации : Sci. Adv.: AMER ASSOC ADVANCEMENT SCIENCE, 2017. - Vol. 3, Is. 4. - Ст.e1602847. - ISSN 2375-2548, DOI 10.1126/sciadv.1602847
Примечания : Cited References:40. - This work was supported by the Sao Paulo Research Foundation [FAPESP grants 10/11578-5 (to A.G.O.), 13/16885-1 (to C.V.S.), 14/14866-2 (to E.L.B.), 13/07914-8 (to E.P. and F.A.D.), and 2012/12663-1 (to P.D.M.) and CEPID Redoxoma 2013/07937-8 (to P.D.M.)], the National Council for Scientific and Technological Development (CNPq) [301307/2013-0 (to P.D.M.)], NAP Redoxoma (PRPUSP) [2011.1.9352.1.8. (to P.D.M.)], the Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research (KAKENHI) [grant no. 16K07715 (to Y.O.)], Chubu University [grant AII28II M01 (to Y.O.)], and the Russian Science Foundation (grant 16-14-00052 to all Russian authors).
Предметные рубрики: SINGLET MOLECULAR-OXYGEN
QUANTUM YIELDS
CHEMILUMINESCENCE
Аннотация: Bioluminescent fungi are spread throughout the globe, but details on their mechanism of light emission are still scarce. Usually, the process involves three key components: an oxidizable luciferin substrate, a luciferase enzyme, and a light emitter, typically oxidized luciferin, and called oxyluciferin. We report the structure of fungal oxyluciferin, investigate the mechanism of fungal bioluminescence, and describe theuseof simple synthetic alpha-pyrones as luciferins to produce multicolor enzymatic chemiluminescence. A high-energy endoperoxide is proposed as an intermediate of the oxidation of the native luciferin to the oxyluciferin, which is a pyruvic acid adduct of caffeic acid. Luciferase promiscuity allows the use of simple alpha-pyrones as chemiluminescent substrates.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana V., Vysotski, Eugene S.
Заглавие : Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa
Колич.характеристики :8 с
Коллективы : Russian Science Foundation [14-14-01119]
Место публикации : Photochem. Photobiol.: WILEY, 2017. - Vol. 93, Is. 2. - С. 503-510. - ISSN 0031-8655, DOI 10.1111/php.12694. - ISSN 1751-1097(eISSN)
Примечания : Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V. A., Esimbekova E. N.
Заглавие : Applications of luminous bacteria enzymes in toxicology
Место публикации : Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - С. 952-959. - ISSN 13862073 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L. A.
Заглавие : Creation of artificial luciferases to expand their analytical potential
Место публикации : Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - С. 919-929. - ISSN 13862073 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva E. V., Lashchuk O. O., Gerasimova M. A.
Заглавие : Similarity of decay-associated spectra for tryptophan fluorescence of proteins with different structures
Место публикации : Biophysics. - 2016. - Vol. 61, Is. 2. - С. 193-199. - ISSN 00063509 (ISSN) , DOI 10.1134/S0006350916020111
Ключевые слова (''Своб.индексиров.''): denaturation--dielectric relaxation--fluorescence lifetime--tertiary protein structure--tryptophan
Аннотация: Tryptophan fluorescence lifetimes were analyzed for three proteins: human serum albumin, bovine serum albumin, and bacterial luciferase, which contain one, two, and seven tryptophan residues, respectively. For all of the proteins, the fluorescence decays were fitted by three lifetimes: ?1 = 6–7 ns, ?2 = 2.0–2.3 ns, and ?3 ? 0.1 ns (the native state), and ?1 = 4.4–4.6 ns, ?2 = 1.7–1.8 ns, and ?3 ? 0.1 ns (the denatured state). Corresponding decay-associated spectra had similar peak wavelengths and spectrum half-widths both in the native state (??1max = 342 nm, ??2max = 328 nm, and ??3max = 315 nm), and in the denatured state (??1max = 350 nm, ??2max= 343 nm, and ??3max= 317 nm). The differences in the steady-state spectra of the studied proteins were accounted for the individual ratio of the lifetime component contributions. The lifetime components were compared with a classification of tryptophan residues in the structure of these proteins within the discrete states model. © 2016, Pleiades Publishing, Inc.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodionova N. S., Rota E., Tsarkova A. S., Petushkov V. N.
Заглавие : Progress in the Study of Bioluminescent Earthworms
Место публикации : Photochem. Photobiol.: Blackwell Publishing Inc., 2017. - Vol. 93, Is. 2. - С. 416-428. - ISSN 00318655 (ISSN) , DOI 10.1111/php.12709
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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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana V., Vysotski, Eugene S.
Заглавие : The novel extremely psychrophilic luciferase from Metridia longa: Properties of a high-purity protein produced in insect cells
Колич.характеристики :7 с
Коллективы : Bayer AG (Germany); Russian Academy of Sciences [01201351504]; RFBR; Government of Krasnoyarsk Territory [16-44-242099]
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017. - Vol. 483, Is. 1. - С. 772-778. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2016.12.067. - ISSN 1090-2104(eISSN)
Примечания : Cited References:24. - The cloning of cDNAs encoding MLuc2 isoforms of M. longa was supported by Bayer AG (Germany) and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 01201351504); all other studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099.
Предметные рубрики: CDNA CLONING
EXPRESSION
ENZYME
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--bioluminescent reporter--psychrophilic--enzyme--molecular adaptation
Аннотация: The bright bioluminescence of copepod Metridia longa is conditioned by a small secreted coelenterazinedependent luciferase (MLuc). To date, three isoforms of MLuc differing in length, sequences, and some properties were cloned and successfully applied as high sensitive bioluminescent reporters. In this work, we report cloning of a novel group of genes from M. longa encoding extremely psychrophilic isoforms of MLuc (MLuc2-type). The novel isoforms share only similar to 54-64% of protein sequence identity with the previously cloned isoforms and, consequently, are the product of a separate group of paralogous genes. The MLuc2 isoform with consensus sequence was produced as a natively folded protein using baculovirus/ insect cell expression system, purified, and characterized. The MLuc2 displays a very high bioluminescent activity and high thermostability similar to those of the previously characterized M. longa luciferase isoform MLuc7. However, in contrast to MLuc7 revealing the highest activity at 12-17 degrees C and 0.5 M NaCl, the bioluminescence optima of MLuc2 isoforms are at similar to 5 degrees C and 1 M NaCl. The MLuc(2) adaptation to cold is also accompanied by decrease of melting temperature and affinity to substrate suggesting a more conformational flexibility of a protein structure. The luciferase isoforms with different temperature optima may provide adaptability of the M. longa bioluminescence to the changes of water temperature during diurnal vertical migrations. (C) 2016 Elsevier Inc. All rights reserved.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Yampolsky I.
Заглавие : Fungal bioluminescence system: luciferin, luciferase and luciferin biosynthesis
Колич.характеристики :1 с
Коллективы : Russian Science Foundation [16-14-00052]
Место публикации : FEBS J.: WILEY, 2017. - Vol. 284: 42nd Congress of the Federation-of-European-Biochemical-Societies (FEBS) (SEP 10-14, 2017, Jerusalem, ISRAEL). - С. 189-189. - ISSN 1742-464X. - ISSN 1742-4658(eISSN)
Примечания : Cited References:0. - This work was supported by the Russian Science Foundation grant 16-14-00052.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Denisov I., Lukyanenko K., Yakimov A., Kukhtevich I., Esimbekova E., Belobrov P.
Заглавие : Disposable luciferase-based microfluidic chip for rapid assay of water pollution
Место публикации : Lumin. - 2018. - Vol. 33, Is. 6. - С. 1054-1061. - ISSN 15227235 (ISSN) , DOI 10.1002/bio.3508
Ключевые слова (''Своб.индексиров.''): bioassay--lab-on-a-chip--luciferase--microfluidics--solvent bonding
Аннотация: In the present study, we demonstrate the use of a disposable luciferase-based microfluidic bioassay chip for environmental monitoring and methods for fabrication. The designed microfluidic system includes a chamber with immobilized enzymes of bioluminescent bacteria Photobacterium leiognathi and Vibrio fischeri and their substrates, which dissolve after the introduction of the water sample and thus activate bioluminescent reactions. Limits of detection for copper (II) sulfate, 1,3-dihydroxybenzene and 1,4-benzoquinone for the proposed microfluidic biosensor measured 3 ?M, 15 mM, and 2 ?M respectively, and these values are higher or close to the level of conventional environmental biosensors based on lyophilized bacteria. Approaches for entrapment of enzymes on poly(methyl methacrylate) (PMMA) plates using a gelatin scaffold and solvent bonding of PMMA chip plates under room temperature were suggested. The proposed microfluidic system may be used with some available luminometers and future portable luminescence readers. © 2018 John Wiley & Sons, Ltd.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova M. D., Markova S. V., Vysotski E. S.
Заглавие : Luminescent properties and application of luciferase isoforms from copepod Metridia longa
Колич.характеристики :1 с
Коллективы : RFBR; Government of Krasnoyarsk Territory [16-44-242099]
Место публикации : FEBS Open Bio: WILEY, 2018. - Vol. 8. - С. 166-166. - ISSN 2211-5463
Примечания : Cited References:0. - These studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099.
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sutormin O. S., Sukovataya I. E., Pande S., Kratasyuk V. A.
Заглавие : Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase
Место публикации : Mol. Cat.: Elsevier B.V., 2018. - Vol. 458. - С. 60-66. - ISSN 24688231 (ISSN) , DOI 10.1016/j.mcat.2018.08.012
Ключевые слова (''Своб.индексиров.''): bioluminescence--coupling of enzymes--in vivo simulated media--metabolic chain--protein stability
Аннотация: One of the current trends of the modern biology figures out cellular enzyme behaviour. Numerous researches look more closely at the chemical composition of creating in vivo simulated media conditions. The aim of this work was to find out a thermodynamic cooperativity of enzymes in a triple-enzyme chain (lactate dehydrogenase + NAD(P)H: FMN-oxidoreductase + bacterial luciferase) under in vivo simulated condition. The thermodynamic cooperativity effects were found out based on the influence of the viscogens (glycerol and sucrose) on the thermal stability of the triple-enzyme system. The results showed that the viscogens do not lead to an increase in the thermal stability of the triple-enzyme system. In addition, organic solvents (sucrose and glycerol) added as viscous agents to the reaction medium altered the kinetics of this triple-enzyme chain, including changing the light emission decay constant (kdec) and quantum yield of luminescence (Q). Plus, sucrose was found to be more efficient in limiting the flexibility of enzymes than glycerol. The high sensitivity of the triple-enzyme system to the viscogens may be connected with a fact that lactate dehydrogenase does not bound with couple enzyme system NAD(P)H: FMN-oxidoreductase + bacterial luciferase inside the real cell. Since this approach may be used as a method to understand the real connection between enzymes in cellular multi-enzyme metabolic chains inside the luminous bacteria cell. © 2018 Elsevier B.V.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko, Kirin A., Denisov, Ivan A., Sorokin, Vladimir V., Yakimov, Anton S., Esimbekova, Elena N., Belobrov, Peter, I
Заглавие : Handheld Enzymatic Luminescent Biosensor for Rapid Detection of Heavy Metals in Water Samples
Колич.характеристики :10 с
Коллективы : Russian Foundation for Basic Research, Government of Krasnoyarsk Territory [18-44-242003]
Место публикации : Chemosensors: MDPI, 2019. - Vol. 7, Is. 1. - Ст.16. - ISSN 2227-9040, DOI 10.3390/chemosensors7010016
Примечания : Cited References:39. - This research was funded by Russian Foundation for Basic Research, Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, to the research project #18-44-242003: "Designing an enzyme reagent for bioluminescent analysis: mechanisms for increasing sensitivity and accuracy".
Предметные рубрики: ON-A-CHIP
SILICON PHOTOMULTIPLIER
OPTICAL BIOSENSORS
CELL
Аннотация: Enzymatic luminescent systems are a promising tool for rapid detection of heavy metals ions for water quality assessment. Nevertheless, their widespread use is limited by the lack of test procedure automation and available sensitive handheld luminometers. Herein we describe integration of disposable microfluidic chips for bioluminescent enzyme-inhibition based assay with a handheld luminometer, which detection system is based on a thermally stabilized silicon photomultiplier (SiPM). Microfluidic chips were made of poly(methyl methacrylate) by micro-milling method and sealed using a solvent bonding technique. The composition of the bioluminescent system in microfluidic chip was optimized to achieve higher luminescence intensity and storage time. Results indicate that developed device provided comparable sensitivity with bench-scale PMT-based commercial luminometers. Limit of detection for copper (II) sulfate reached 2.5 mg/L for developed biosensor. Hereby we proved the concept of handheld enzymatic optical biosensors with disposable chips for bioassay. The proposed biosensor can be used as an early warning field-deployable system for rapid detection of heavy metals salts and other toxic chemicals, which affect bioluminescent signal of enzymatic reaction.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kotlobay A. A., Sarkisyan K. S., Mokrushina Y. A., Marcet-Houben M., Serebrovskaya E. O., Markina N. M., Somermeyer L. G., Gorokhovatsky A. Y., Vvedensky A., Purtov K. V., Petushkov V. N., Rodionova N. S., Chepurnyh T. V., Fakhranurova L. I., Guglya E. B., Ziganshin R., Tsarkova A. S., Kaskova Z. M., Shender V., Abakumov M., Abakumova T. O., Povolotskaya I. S., Eroshkin F. M., Zaraisky A. G., Mishin A. S., Dolgov S. V., Mitiouchkina T. Y., Kopantzev E. P., Waldenmaier H. E., Oliveira A. G., Oba Y., Barsova E., Bogdanova E. A., Gabaldon T., Stevani C. V., Lukyanov S., Smirnov I. V., Gitelson J. I., Kondrashov F. A., Yampolsky I. V.
Заглавие : Genetically encodable bioluminescent system from fungi
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: National Academy of Sciences, 2018. - Vol. 115, Is. 50. - С. 12728-12732. - ISSN 00278424 (ISSN) , DOI 10.1073/pnas.1803615115
Ключевые слова (''Своб.индексиров.''): bioluminescence--fungal luciferase--fungal luciferin biosynthesis
Аннотация: Bioluminescence is found across the entire tree of life, conferring a spectacular set of visually oriented functions from attracting mates to scaring off predators. Half a dozen different luciferins, molecules that emit light when enzymatically oxidized, are known. However, just one biochemical pathway for luciferin biosynthesis has been described in full, which is found only in bacteria. Here, we report identification of the fungal luciferase and three other key enzymes that together form the biosynthetic cycle of the fungal luciferin from caffeic acid, a simple and widespread metabolite. Introduction of the identified genes into the genome of the yeast Pichia pastoris along with caffeic acid biosynthesis genes resulted in a strain that is autoluminescent in standard media. We analyzed evolution of the enzymes of the luciferin biosynthesis cycle and found that fungal bioluminescence emerged through a series of events that included two independent gene duplications. The retention of the duplicated enzymes of the luciferin pathway in nonluminescent fungi shows that the gene duplication was followed by functional sequence divergence of enzymes of at least one gene in the biosynthetic pathway and suggests that the evolution of fungal bioluminescence proceeded through several closely related stepping stone nonluminescent biochemical reactions with adaptive roles. The availability of a complete eukaryotic luciferin biosynthesis pathway provides several applications in biomedicine and bioengineering. © 2018 National Academy of Sciences. All Rights Reserved.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Purtov K. V., Gorokhovatsky, A. Yu., Kotlobay A. A., Osipova Z. M., Petushkov V. N., Rodionova N. S., Tsarkova A. S., Chepurnykh T. V., Yampolsky I. V., Gitelson J. I.
Заглавие : Isolation and Purification of Fungal Luciferase from Neonothopanus nimbi
Колич.характеристики :4 с
Коллективы : Russian Science Foundation [16-14-00052]
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2018. - Vol. 480, Is. 1. - С. 177-180. - ISSN 1607-6729, DOI 10.1134/S1607672918030134. - ISSN 1608-3091(eISSN)
Примечания : Cited References:6. - The study was supported by Russian Science Foundation Grant No. 16-14-00052. This research was carried out using the equipment provided by the Collective Use Center (CKP IBCH, ID of the agreement with Ministry of Education and Science of the Russian Federation: RFMEFI 62117X0018).
Аннотация: This is the first study to obtain a high-purity luciferase from the fungus Neonothopanus nambi bio-mass that is suitable for subsequent sequencing.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Esimbekova, Elena N., Nemtseva, Elena V., Bezrukikh, Anna E., Jukova, Galina V., Lisitsa, Albert E., Lonshakova-Mukina, Viktoriya I., Rimatskaya, Nadezhda V., Sutormin, Oleg S., Kratasyuk, Valentina A.
Заглавие : Bioluminescent enzyme inhibition-based assay to predict the potential toxicity of carbon nanomaterials
Колич.характеристики :6 с
Коллективы : Russian Science Foundation [16-14-10115]
Место публикации : Toxicol. Vitro: PERGAMON-ELSEVIER SCIENCE LTD, 2017. - Vol. 45. - С. 128-133. - ISSN 0887-2333, DOI 10.1016/j.tiv.2017.08.022
Примечания : Cited References:55. - This study was supported by the Russian Science Foundation (project no. 16-14-10115).
Предметные рубрики: IN-VIVO
ENGINEERED NANOPARTICLES
NANOTUBE TOXICITY
C-60
FULLERENE
Ключевые слова (''Своб.индексиров.''): nanotoxicity--enzyme inhibition-based assay--bioluminescence--luciferase--nanomaterials--nanotubes
Аннотация: A bioluminescent enzyme inhibition-based assay was applied to predict the potential toxicity of carbon nanomaterials (CNM) presented by single- and multi-walled nanotubes (SWCNT and MWCNT) and aqueous solutions of hydrated fullerene C-60 (C(60)HyFn). This assay specifically detects the influence of substances on parameters of the soluble or immobilised coupled enzyme system of luminescent bacteria: NAD(P)H:FMN-oxidoreductase + luciferase (Red + Luc). A protocol based on the optical properties of CNM for correcting the results of the bioluminescent assay was also developed. It was shown that the inhibitory activity of CNM on Red + Luc decreased in the following order: MWCNT SWCNT C(60)HyFn. The soluble enzyme system Red + Luc had high sensitivity to MWCNT and SWCNT, with values of the inhibition parameter IC50 equal to 0.012 and 0.16 mg/L, respectively. The immobilised enzyme system was more vulnerable to C(60)HyFn than its soluble form, with an IC50 equal to 1.4 mg/L. Due to its technical simplicity, rapid response time and high sensitivity, this bioluminescent method has the potential to be developed as a general enzyme inhibition-based assay for a wide variety of nanomaterials.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova, Svetlana V., Larionova, Marina D., Gorbunova, Darya A., Vysotski, Eugene S.
Заглавие : The disulfide-rich Metridia luciferase refolded from E. coli inclusion bodies reveals the properties of a native folded enzyme produced in insect cells
Колич.характеристики :7 с
Коллективы : RFBR; Government of Krasnoyarsk Territory [16-44-242099]; Russian Academy of Sciences [0356-2016-0712]
Место публикации : J. Photochem. Photobiol. B-Biol.: ELSEVIER SCIENCE SA, 2017. - Vol. 175. - С. 51-57. - ISSN 1011-1344, DOI 10.1016/j.jphotobiol.2017.08.024
Примечания : Cited References:30. - These studies were funded by RFBR and the Government of Krasnoyarsk Territory according to the research project No. 16-44-242099 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 0356-2016-0712).
Предметные рубрики: GAUSSIA-PRINCEPS LUCIFERASE
ESCHERICHIA-COLI
EXPRESSION
PROTEIN
Ключевые слова (''Своб.индексиров.''): copepod luciferase--disulfide bonds--cysteine-rich protein--oxidative--refolding
Аннотация: The bioluminescence of a marine copepod Metridia Tonga is determined by a small secreted coelenterazine-dependent luciferase that uses coelenterazine as a substrate of enzymatic reaction to generate light (lambda(max) = 480 nm). To date, four different isoforms of the luciferase differing in size, sequences, and properties have been cloned by functional screening. All of them contain ten conserved Cys residues that suggests up to five S-S intramolecular bonds per luciferase molecule. Whereas the use of copepod luciferases as bioluminescent reporters in biomedical research in vivo is growing from year to year, their application for in vitro assays is still limited by the difficulty in obtaining significant amounts of luciferase. The most cost-effective host for producing recombinant proteins is Escherichia coli. However, prokaryotic and eukaryotic cells maintain the reductive environment in cytoplasm that hinders the disulfide bond formation and consequently the proper folding of luciferase. Here we report the expression of the MLuc7 isoform of M. longa luciferase in E. colt cells and the efficient procedure for refolding from inclusion bodies yielding a high-active monomeric protein. Furthermore, in a set of identical experiments we demonstrate that bioluminescent and structural features of MLuc7 produced in bacterial cells are identical to those of MLuc7 isoform produced from culture medium of insect cells. Although the yield of high-purity protein is only 6 mg/L, the application of E. coil cells to produce the luciferase is simpler and more cost-effective than the use of insect cells. We expect that the suggested technology of Metridia luciferase production allows obtaining of sufficient amounts of protein both for the development of novel in vitro analytical assays with the use of MLuc7 as a label and for structural studies.
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