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^a314.27.17^2VINITI
П 31

Петушков, В. Н.
Изучение эффективности работы биферментной системы NADH: FMN-оксидоредуктаза-люцифераза светящихся бактерий [Текст] : научное издание / В. Н. Петушков, Н. С. Родионова, П. И. Белобров // Биохимия. - 1985. - Т. 50, N 3. - С. 401-405 . - ISSN 0320-9725

ГРНТИ

31.27.17

РУБ 314.27.17
Рубрики:
НАДН:ФМН-ОКСИДОРЕДУКТАЗА-ЛЮЦИФЕРАЗА
   МЕХАНИЗМ РАБОТЫ
   БАКТЕРИИ
   СВЕТЯЩИЕСЯ
   NADH:FMN-OXIDOREDUCTASE-LUCIFERASE
   LUMINESCENT BACTERIA
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Родионова, Н.С.; Белобров, П.И.

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Towards biological quantity theory for nominal property metrology in polyenzymatic devices with living cells / P. I. Belobrov, A. A. Evstrapov, E. N. Esimbekova [et al.] // Journal of Physics: Conference Series : Institute of Physics Publishing, 2019. - Vol. 1379: Joint IMEKO TC1-TC7-TC13-TC18 Symposium 2019 (2 July 2019 through 5 July 2019, ) Conference code: 156337, Is. 1. - Ст. 012036, DOI 10.1088/1742-6596/1379/1/012036
Кл.слова (ненормированные):
Fluidic devices -- Industrial waste disposal -- Biological measurement -- Bioluminescent systems -- Continuous measurements -- Droplet-based microfluidics -- Industrial enterprise -- Microfluidic platforms -- Numerical variables -- Silicon photomultiplier -- Microfluidics
Аннотация: Here we discuss the concepts of "biological quantity" and "nominal property" within the framework of the problem of biological measurements based on new specific results of biological analysis using a microfluidic platform and chips developed by our team earlier. It was shown that based on different microfluidic platforms it is possible to develop chips with a polyenzymatic bioluminescent system NAD(P)H:FMN-oxidoreductase-luciferase (Red + Luc), which can be used in various areas of biological analysis. Thus, disposable microfluidic chips with Red + Luc system suitable for field and indoor use were developed using continuous flow microfluidic platform. The use of droplet-based microfluidic platform allowed to develop microfluidic chips with Red + Luc system for long-term continuous measurements of water samples, for example, in places of waste disposal by industrial enterprises. The reference for comparing different biological quantities with each other in the proposed system was a photodetector, which converted non-numeric values and nominal properties recorded by a biological module Red + Luc into numerical variables. Such a reference was implemented as a portable luminometer based on silicon photomultiplier. The results allow to perform other biological measurements and to start the discussion of modern biological concepts in the language of biological measures. © 2019 IOP Publishing Ltd. All rights reserved.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute for Analytical Instrumentation RAS, St.-Petersburg, 190103, Russian Federation
Laboratory of Photobiology, Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Laboratory for Digital Controlled Drugs and Theranostics, Federal Research Center krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Research Institute of Molecular Medicine and Pathobiochemistry, Krasnoyarsk State Medical University Named after Prof. V.F. Voino-Yasenetsky, Krasnoyarsk, 660022, Russian Federation

Доп.точки доступа:
Belobrov, P. I.; Evstrapov, A. A.; Esimbekova, E. N.; Denisov, I. A.; Lukyanenko, K. A.; Osipova, E. D.; Yakimov, A. S.

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Towards biological quantity theory for nominal property metrology in polyenzymatic devices with living cells / P. I. Belobrov, A. A. Evstrapov, E. N. Esimbekova [et al.] // JOINT IMEKO TC1-TC7-TC13-TC18 SYMPOSIUM : IOP PUBLISHING LTD, 2019. - Vol. 1379: Joint IMEKO TC1-TC7-TC13-TC18 Symposium (JUL 02-05, 2019, St Petersburg, RUSSIA). - Ст. 012036. - (Journal of Physics Conference Series), DOI 10.1088/1742-6596/1379/1/012036. - Cited References:19 . -

РУБ Instruments & Instrumentation + Mathematics, Applied + Physics, Applied

Аннотация: Here we discuss the concepts of "biological quantity" and "nominal property" within the framework of the problem of biological measurements based on new specific results of biological analysis using a microfluidic platform and chips developed by our team earlier. It was shown that based on different microfluidic platforms it is possible to develop chips with a polyenzymatic bioluminescent system NAD(P)H:FMN-oxidoreductase-luciferase (Red + Luc), which can be used in various areas of biological analysis. Thus, disposable microfluidic chips with Red + Luc system suitable for field and indoor use were developed using continuous flow microfluidic platform. The use of droplet-based microfluidic platform allowed to develop microfluidic chips with Red + Luc system for long-term continuous measurements of water samples, for example, in places of waste disposal by industrial enterprises. The reference for comparing different biological quantities with each other in the proposed system was a photodetector, which converted non-numeric values and nominal properties recorded by a biological module Red + Luc into numerical variables. Such a reference was implemented as a portable luminometer based on silicon photomultiplier. The results allow to perform other biological measurements and to start the discussion of modern biological concepts in the language of biological measures.

WOS
Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia.
RAS, Inst Analyt Instrumentat, St Petersburg 190103, Russia.
SB RAS, Lab Photobiol, Inst Biophys, Krasnoyarsk 660036, Russia.
SB RAS, Krasnoyarsk Sci Ctr, Fed Res Ctr, Lab Digital Controlled Drugs & Theranost, Krasnoyarsk 660036, Russia.
Krasnoyarsk State Med Univ, Res Inst Mol Med & Pathobiochem, Krasnoyarsk 660022, Russia.

Доп.точки доступа:
Belobrov, P., I; Evstrapov, A. A.; Esimbekova, E. N.; Denisov, I. A.; Lukyanenko, K. A.; Osipova, E. D.; Yakimov, A. S.; Belobrov, Peter I; Yakimov, Anton

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The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems / V. A. Kratasyuk [et al.] // Chemosphere. - 2001. - Vol. 42, Is. 8. - P909-915, DOI 10.1016/S0045-6535(00)00177-6 . - ISSN 0045-6535
Кл.слова (ненормированные):
Alcohol dehydrogenase -- Bacterial luciferase -- Bioluminescence -- Blooming -- Pollution -- Trypsin -- Water toxicity -- alcohol dehydrogenase -- benzoquinone -- luciferase -- trypsin -- aquatic ecosystem -- bioluminescence -- water quality -- article -- bacterium culture -- bioluminescence -- blue green alga -- ecosystem -- pond -- seasonal variation -- water pollution -- water quality -- Benzoquinones -- Biological Assay -- Cyanobacteria -- Ecosystem -- Environmental Monitoring -- Eutrophication -- FMN Reductase -- Indicators and Reagents -- Luminescent Measurements -- NADH, NADPH Oxidoreductases -- Water Pollutants -- Russian Federation -- algae -- Bacteria (microorganisms) -- Chlorophyta -- Cyanobacteria -- uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.

Scopus
Держатели документа:
Krasnoyarsk State University, pr. Svobodnii 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Esimbekova, E.N.; Gladyshev, M.I.; Khromichek, E.B.; Kuznetsov, A.M.; Ivanova, E.A.

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The influence of quinones and phenols on the triple NAD(H)-dependent enzyme systems [Text] / N. S. Kudryasheva [et al.] // Chemosphere. - 1999. - Vol. 38, Is. 4. - P. 751-758, DOI 10.1016/S0045-6535(98)00218-5. - Cited References: 7 . - ISSN 0045-6535

РУБ Environmental Sciences

Аннотация: Kinetics of the triple bioluminescent enzyme system: alcohol dehydrogenase - NADH:FMN-oxidoreductase - luciferase in the presence of quinones and phenols has been studied. The correspondence between the bioluminescent kinetic parameters, redox potentials and concentrations of the quinones and phenols has been estimated. The substances have been shown to change bioluminescent kinetics through moving off the NAD(+)/NADH balance in the enzyme processes. This system is proposed to be used as enzymatic biotest in ecological monitoring. (C) 1998 Elsevier Science Ltd. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
Irkutsk State Univ, Biol Res Inst, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Kudinova, I.Y.; Esimbekova, E.N.; Kratasyuk, V.A.; Stom, D.I.

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Set of Enzymatic Bioassays for Assessment of Soil Contamination / E. M. Kolosova, O. S. Sutormin, E. N. Esimbekova [et al.] // Dokl. Biol. Sci. - 2019. - Vol. 489, Is. 1. - P165-168, DOI 10.1134/S0012496619060024 . - ISSN 1608-3105
Аннотация: A concept of the comprehensive assessment of soil contamination is proposed. According to it, the conclusion regarding the presence of toxic substances in the analyzed sample is based on the inhibition of enzymatic reactions responsible for various functions of a living organism, such as luminescence, respiration, etc. These functions are taken as test functions in classical bioassays with the use of living objects (luminous bacteria, daphnia, algae, and others). The regularities of the impact of different classes of toxicants on the activity of particular enzymes or coupled oligo-enzyme chains have been established. These enzyme reactions are selected as potential test objects: markers of contamination. Three enzyme systems with the maximal sensitivity to different classes of toxicants have been chosen for the set of enzymatic bioassays: butyrylcholinesterase, NAD(P)H:FMN-oxidoreductase + luciferase, and lactate dehydrogenase + NAD(P)H:FMN-oxidoreductase + luciferase. The possibility to use enzymes instead of living organisms in the bioassay of natural complex systems has been shown.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kolosova, E. M.; Sutormin, O. S.; Esimbekova, E. N.; Lonshakova-Mukina, V. I.; Kratasyuk, V. A.

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Principles for Construction of Bioluminescent Enzyme Biotests for Analysis of Complex Media / V. P. Kalyabina [et al.] // Dokl. Biochem. Biophys. - 2019. - Vol. 485, Is. 1. - P107-110, DOI 10.1134/S1607672919020042. - Cited References:10. - The study was supported by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science and RFBR (project no. 18-44-242003). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VEGETABLES
ELEMENTS
Аннотация: In this study, we formulated the principles of designing bioluminescent enzyme tests for assessing the quality of complex media, which consist in providing the maximum sensitivity to potentially toxic chemicals at a minimal impact of uncontaminated complex media. The developed principles served as a basis for designing a new bioluminescent method for an integrated rapid assessment of chemical safety of fruits and vegetables, which is based on using the luminous bacteria enzymes (NAD(P)H:FMN oxidoreductase and luciferase) as a test system.

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

Доп.точки доступа:
Kalyabina, V. P.; Esimbekova, E. N.; Torgashina, I. G.; Kopylova, K. V.; Kratasyuk, V. A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; RFBR [18-44-242003]

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On monitoring the bacterial component as an indicator of the state of small man-made ecosystems / A. B. Sarangova, L. A. Somova, N. S. Pechurkin // Advances in Space Research. - 2001. - Vol. 27, Is. 9. - P1605-1609, DOI 10.1016/S0273-1177(01)00256-3 . - ISSN 0273-1177
Кл.слова (ненормированные):
Bacteria -- Ecosystems -- Substrates -- Intracellular substrate concentration -- Space research -- catalase -- oxidoreductase -- artificial ecosystem -- article -- bacterial phenomena and functions -- biomass -- culture medium -- ecosystem -- enzymology -- growth, development and aging -- metabolism -- microbiology -- oxygen consumption -- Pseudomonas -- Bacterial Physiology -- Biomass -- Catalase -- Culture Media -- Ecosystem -- Oxidoreductases -- Oxygen Consumption -- Pseudomonas -- Water Microbiology
Аннотация: High reproduction rates make the bacterial component of ecosystems a good indicator of the state of the system on the whole. This determines the necessity to develop rapid monitoring of the functional state of the bacterial component of small ecosystems. Information about substrate concentration in the population is indicative of the state of the bacterial culture. Conventional methods of monitoring the concentration of integral substrate in the system take time much longer than the changes in the ecosystem. The paper presents theoretical foundations for the logical sequence "catalase activity - intracellular substrate concentration - estimate of substrate consumed by bacteria" for experimental verification and as a consequence of development of the integral method of monitoring the bacterial population on the basis of determining bacterial catalase activity. В© 2001 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

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

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.; Pechurkin, N.S.

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NAD(P)H:FMN-Oxidoreductase Functioning Under Macromolecular Crowding: In Vitro Modeling / A. E. Govorun, E. N. Esimbekova, V. A. Kratasyuk // Doklad. Biochem. Biophys. - 2019. - Vol. 486, Is. 1. - P213-215, DOI 10.1134/S160767291903013X . - ISSN 1607-6729
Аннотация: The functioning of NAD(P)H:FMN‑oxidoreductase (Red) from Vibrio fischeri under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin) was studied. The dissociation rate constants and the activation energies of dissociation of Red to the subunits were calculated, and the process of denaturation of Red was analyzed. It is shown that the functioning of Red both under conditions of MMC and in diluted solutions is the same. This result refutes the common belief that the native conformation of enzymes in vivo is stabilized due to MMC as compared to the in vitro conditions. © 2019, Pleiades Publishing, Ltd.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

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

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10.

Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another / N. S. Rodionova, V. N. Petushkov, P. I. Belobrov // Biophysics. - 1988. - Vol. 33, Is. 3. - P424-430 . - ISSN 0006-3509
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.

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

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

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11.

Impact of enzyme stabilizers on the characteristics of biomodules for bioluminescent biosensors / V. Lonshakova-Mukina, E. Esimbekova, V. Kratasyuk // Sens Actuators, B Chem. - 2015. - Vol. 213. - P244-247, DOI 10.1016/j.snb.2015.02.061 . - ISSN 0925-4005
Кл.слова (ненормированные):
Bioluminescence -- Body fluids -- Carrier concentration -- Enzymes -- Starch -- Bioluminescent biosensor -- Bovine serum albumins -- Dithiothreitol -- Maximum permissible concentration -- Mercaptoethanol -- Oxidoreductases -- Storage stability -- Toxic substances -- Biosensors
Аннотация: The biomodule of bioluminescent biosensor based on a coupled enzyme system NADH:FMN-oxidoreductase and luciferase, co-immobilized with substrates in dried starch or gelatin gels, has been developed. We studied the impact of several stabilizers - dithiothreitol (DTT), bovine serum albumin (BSA) and mercaptoethanol (ME) on the biomodule's activity, storage stability and sensitivity to toxic substances. The inclusion of stabilizers increases the activity of the biological module by more than 150%. To achieve the combination of high activity, prolonged storage time and acute sensitivity to toxic substances within maximum permissible concentration we used starch gel as a carrier adding 100 ?M DTT to the immobilized preparation. The gelatin-based biological module had greater storage stability than the starch-based one but demonstrated less sensitivity to toxic substances. © 2015 Elsevier B.V. All rights reserved.

Scopus,
WOS
Держатели документа:
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50Krasnoyarsk, Russian Federation
ИБФ СО РАН

Доп.точки доступа:
Lonshakova-Mukina, V.; Esimbekova, E.; Kratasyuk, V.

Найти похожие

12.

Gelatin and Starch: What Better Stabilizes the Enzyme Activity? / E. N. Esimbekova, A. E. Govorun, V. I. Lonshakova-Mukina, V. A. Kratasyuk // Dokl. Biol. Sci. - 2020. - Vol. 491, Is. 1. - P43-46, DOI 10.1134/S0012496620020039 . - ISSN 0012-4966
Кл.слова (ненормированные):
butyrylcholinesterase -- enzyme stabilization -- gelatin -- luciferase -- NAD(P)H:FMN oxidoreductase -- starch -- thermal inactivation of enzymes
Аннотация: Abstract: The regularities of the functioning of a number of enzymes in a viscous environment created by natural polymers, starch and gelatin are examined. Based on the analysis of kinetic curves of thermal inactivation, mechanisms of thermal inactivation of enzymes in a viscous microenvironment are proposed. Using the example of butyrylcholinesterase, NAD(P)H:FMN oxidoreductase, and coupled system of the luminous bacteria (NAD(P)H:FMN oxidoreductase + luciferase), the conditions, under which starch and gelatin have a stabilizing effect on enzyme activity during storage and exposure to various physical and chemical environmental factors, were found. A significant increase in the stabilizing effect is achieved by eliminating water during drying the enzyme preparations immobilized in starch and gelatin polymer gels. © 2020, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Govorun, A. E.; Lonshakova-Mukina, V. I.; Kratasyuk, V. A.

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13.

Gelatin and Starch Media Stabilize Bacterial Luciferase and Oxidoreductase [Text] / A. . Bezrukikh, E. . Esimbekova, V. . Kratasyuk // Luminescence. - 2014. - Vol. 29. - P73-74. - Cited References: 2 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Bezrukikh, Anna
Esimbekova, Elena
Kratasyuk, Valentina] Siberian Fed Univ, Krasnoyarsk, Russia
[Esimbekova, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

Найти похожие

14.

Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase [Text] / A. . Bezrukikh [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5743-5747, DOI 10.1007/s00216-014-7987-1. - Cited References: 14. - The work was supported by the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11.G34.31.0058), the Russian Academy of Sciences (program "Molecular and Cell Biology", grant no. 6.8), and the state contract between the Ministry of Education and Science and Siberian Federal University, no. 1762. . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
IMMOBILIZATION
CHEMISTRY
Кл.слова (ненормированные):
Bacterial luciferase -- NADH:FMN-oxidoreductase -- Bioluminescence -- Stabilization of enzymes -- Gelatin -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 A degrees C and 25 A degrees C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 A degrees C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions.

WOS
Держатели документа:
[Bezrukikh, Anna
Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A...; Esimbekova, E...; Nemtseva, E...; Kratasyuk, V...; Shimomura, O...; Government of Russian Federation [11.G34.31.0058]; Russian Academy of Sciences [6.8]; Ministry of Education and Science [1762]; Siberian Federal University [1762]

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15.

Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase / A. Bezrukikh [et al.] // . - 2014, DOI 10.1007/s00216-014-7987-1 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bacterial luciferase -- Bioluminescence -- Gelatin -- NADH:FMN-oxidoreductase -- Stabilization of enzymes -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 °C and 25 °C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 °C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions. © 2014 Springer-Verlag Berlin Heidelberg.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A.; Esimbekova, E.; Nemtseva, E.; Kratasyuk, V.; Shimomura, O.

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16.

Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria / A. A. Deeva [et al.] // Proteins. - 2019. - Vol. 87, Is. 9. - P723-729, DOI 10.1002/prot.25696. - Cited References:39. - The Russian Foundation for Basic Research and Krasnoyarsk Region Science and Technology Support Fund, Grant/Award Number: 18-44-243009; Ministry of Education and Science of the Russian Federation, Grant/Award Numbers: 0356-2019-0019, 6.7734.2017 . - ISSN 0887-3585. - ISSN 1097-0134

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
ESCHERICHIA-COLI
FLAVIN OXIDOREDUCTASE
CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
bacterial bioluminescence -- Fre -- functional divergence -- gene duplication -- LuxG -- NAD(P)H -- flavin-oxidoreductase
Аннотация: In luminous bacteria NAD(P)H:flavin-oxidoreductases LuxG and Fre, there are homologous enzymes that could provide a luciferase with reduced flavin. Although Fre functions as a housekeeping enzyme, LuxG appears to be a source of reduced flavin for bioluminescence as it is transcribed together with luciferase. This study is aimed at providing the basic conception of Fre and LuxG evolution and revealing the peculiarities of the active site structure resulted from a functional variation within the oxidoreductase family. A phylogenetic analysis has demonstrated that Fre and LuxG oxidoreductases have evolved separately after the gene duplication event, and consequently, they have acquired changes in the conservation of functionally related sites. Namely, different evolutionary rates have been observed at the site responsible for specificity to flavin substrate (Arg 46). Also, Tyr 72 forming a part of a mobile loop involved in FAD binding has been found to be conserved among Fre in contrast to LuxG oxidoreductases. The conservation of different amino acid types in NAD(P)H binding site has been defined for Fre (arginine) and LuxG (proline) oxidoreductases.

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Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Svobodny Prosp 79, Krasnoyarsk 660041, Russia.
RAS, Inst Cell Biophys, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia.
State Inst Informat Technol & Telecommun SIIT & T, Dept Appl Res Informatizat, Moscow, Russia.
RAS, Fed Res Ctr, Krasnoyarsk Sci Ctr SB, Lab Photobiol,Inst Biophys SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Deeva, Anna A.; Zykova, Evgenia A.; Nemtseva, Elena V.; Kratasyuk, Valentina A.; Nemtseva, Elena; Russian Foundation for Basic Research [18-44-243009]; Ministry of Education and Science of the Russian Federation [0356-2019-0019, 6.7734.2017]; Krasnoyarsk Region Science and Technology [18-44-243009]

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17.

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.

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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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18.

Enzymatic responses to low-intensity radiation of tritium / T. V. Rozhko, E. V. Nemtseva, M. V. Gardt [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 22. - Ст. 8464. - P1-15, DOI 10.3390/ijms21228464 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Enzymes -- Fluorescent protein -- Hormesis -- Low-dose radiation -- Oxidoreductase -- Tritium
Аннотация: The present study considers a possible role of enzymatic reactions in the adaptive response of cells to the beta-emitting radionuclide tritium under conditions of low-dose exposures. Effects of tritiated water (HTO) on the reactions of bacterial luciferase and NAD(P)H:FMN-oxidoreductase, as well as a coupled system of these two reactions, were studied at radioactivity concentrations ? 200 MBq/L. Additionally, one of the simplest enzymatic reactions, photobiochemical proton transfer in Coelenteramide-containing Fluorescent Protein (CLM-FP), was also investigated. We found that HTO increased the activity of NAD(P)H:FMN-oxidoreductase at the initial stage of its reaction (by up to 230%); however, a rise of luciferase activity was moderate (<20%). The CLM-FP samples did not show any increase in the rate of the photobiochemical proton transfer under the exposure to HTO. The responses of the enzyme systems were compared to the ‘hormetic’ response of luminous marine bacterial cells studied earlier. We conclude that (1) the oxidoreductase reaction contributes significantly to the activation of the coupled enzyme system and bacterial cells by tritium, and (2) an increase in the organization level of biological systems promotes the hormesis phenomenon. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Department of Medical and Biological Physics, Krasnoyarsk State Medical Academy, Krasnoyarsk, 660022, Russian Federation
Biophysics Department, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Department of Chemistry, Moscow State University, Moscow, 119991, Russian Federation

Доп.точки доступа:
Rozhko, T. V.; Nemtseva, E. V.; Gardt, M. V.; Raikov, A. V.; Lisitsa, A. E.; Badun, G. A.; Kudryasheva, N. S.

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19.

Enzymatic Responses to Low-Intensity Radiation of Tritium / T. V. Rozhko, E. V. Nemtseva, M. V. Gardt [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 22. - Ст. 8464, DOI 10.3390/ijms21228464. - Cited References:59. - This work was supported by RFBR-Krasnoyarsk Regional Foundation N 18-44-240004, 18-44-242002. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
LUMINOUS MARINE-BACTERIA
IONIZING-RADIATION
DISCHARGED-OBELIN
Кл.слова (ненормированные):
hormesis -- low-dose radiation -- tritium -- enzymes -- bacterial luciferase -- oxidoreductase -- fluorescent protein
Аннотация: The present study considers a possible role of enzymatic reactions in the adaptive response of cells to the beta-emitting radionuclide tritium under conditions of low-dose exposures. Effects of tritiated water (HTO) on the reactions of bacterial luciferase and NAD(P)H:FMN-oxidoreductase, as well as a coupled system of these two reactions, were studied at radioactivity concentrations <= 200 MBq/L. Additionally, one of the simplest enzymatic reactions, photobiochemical proton transfer in Coelenteramide-containing Fluorescent Protein (CLM-FP), was also investigated. We found that HTO increased the activity of NAD(P)H:FMN-oxidoreductase at the initial stage of its reaction (by up to 230%); however, a rise of luciferase activity was moderate (<20%). The CLM-FP samples did not show any increase in the rate of the photobiochemical proton transfer under the exposure to HTO. The responses of the enzyme systems were compared to the 'hormetic' response of luminous marine bacterial cells studied earlier. We conclude that (1) the oxidoreductase reaction contributes significantly to the activation of the coupled enzyme system and bacterial cells by tritium, and (2) an increase in the organization level of biological systems promotes the hormesis phenomenon.

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Держатели документа:
Krasnoyarsk State Med Acad, Dept Med & Biol Phys, Krasnoyarsk 660022, Russia.
Siberian Fed Univ, Biophys Dept, Krasnoyarsk 660041, Russia.
RAS, Inst Biophys, SB, FRC,KSC, Krasnoyarsk 660036, Russia.
Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119991, Russia.

Доп.точки доступа:
Rozhko, Tatiana V.; Nemtseva, Elena V.; Gardt, Maria V.; Raikov, Alexander V.; Lisitsa, Albert E.; Badun, Gennadii A.; Kudryasheva, Nadezhda S.; Nemtseva, Elena; Kudryasheva, Nadezhda; Rozko, Tat'ana; Lisitsa, Albert; RFBR-Krasnoyarsk Regional Foundation [N 18-44-240004, 18-44-242002]

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20.

Enzymatic bioassay of soil: Sensitivity comparison of mono-, double- And triple-enzyme systems to soil toxicants / O. S. Sutormin [и др.] // Tsitologiya. - 2018. - Vol. 60, Is. 10. - С. 826-829, DOI 10.7868/S0041377118100132 . - ISSN 0041-3771
Кл.слова (ненормированные):
Bacterial luciferase -- Bioluminescent analysis -- Coupled enzyme systems -- Ecological monitoring -- Enzymatic toxicity bioassays -- Lactate dehydrogenase -- NADH:FMN-oxidoreductase -- Soil
Аннотация: In this paper, we have investigated the possibilities of application of enzymatic systems with increasing chain length as a bioassay to evaluate the soil contamination status. The sensitivity of monoenzyme reaction as well as double- and triple-enzyme chains based on NAD(P)H:FMN-oxidoreductase and luciferase of luminous bacteria and lactate dehydrogenase to pesticides and copper ions in water and water extracts from soils were estimated. For this, the toxicological parameter IC 20 reflecting the sensitivity limit of the enzyme system to the to-xicant was used. It was revealed that elongation of the coupled enzyme chain (from mono- to triple-enzyme) increases the sensitivity of the bioassay, in some cases by several orders of magnitude. This pattern can be used as a tool to improve the properties of enzymic bioassays. The effect of extracts from uncontaminated soils of various types on enzymatic systems also differs, which makes possible to design the specialized enzymatic bioassays as well. © 2018 Sankt Peterburg.All rights reserved.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics Siberian Branch of RAS, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Sutormin, O. S.; Kolosova, E. M.; Nemtseva, A. V.; Iskorneva, I. V.; Lisitsa, A. A.; Matvienko, V. S.; Esimbekova, A. N.; Kratasyuk, V. A.

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