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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.

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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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PROSPECTS FOR APPLICATION OF BIOLUMINESCENCE METHOD IN MEDICINE [Текст] / I. I. GITELZON, T. P. SANDALOVA // VESTNIK AKADEMII MEDITSINSKIKH NAUK SSSR. - 1990. - Is. 9. - С. 31-35. - Cited References: 41 . - ISSN 0002-3027

РУБ Medicine, General & Internal
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   VIBRIO-HARVEYI
   BACTERIAL LUCIFERASE
   FIREFLY LUCIFERASE
   SUBUNIT
   CELLS
   GENE
   PHOTOPROTEINS
   EXPRESSION
Аннотация: Major advances in the development and application of the bioluminescent analysis to detect certain biologically active substances are discussed. The main merit of the method lies in its high sensitivity and specificity along with its simplicity and rapid performance. The available methodologies allow for detection of substances of varying nature: Ca2+, ATP, FMN, NAD(P), long-chain aldehydes, ATP- and NAD(P)-dependent enzymes and their substrates, many xenobiotics and antibiotics, and mutagens. The bioluminescence methodologies may be widely applied in clinical laboratory diagnosis.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GITELZON, I.I.; SANDALOVA, T.P.

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^a343.15.19^2VINITI
Б 63

Биолюминесцентный метод определения активности NAD(P)H-зависимых дегидрогеназ [Текст] : научное издание / В. Н. Петушков [и др.] // Прикл. биохимия и микробиол. - 1987. - Т. 23, N 2. - С. 270-274 . - ISSN 0555-1099

ГРНТИ

34.15.19

РУБ 343.15.19
Рубрики:
НАД(Ф)Н ДЕГИДРОГЕНАЗА
   АКТИВНОСТЬ
   ОПРЕДЕЛЕНИЕ
   БИОЛЮМИНЕСЦЕНТНЫЙ МЕТОД
   ЛЮЦЕФЕРАЗА
   СОПРЯЖЕННАЯ ФЕРМЕНТНАЯ СИСТЕМА
   ПРИМЕНЕНИЕ
   BIOLUMINESCENT METHOD
   Е МЕ АСТ Т ЕТЕ М АТ О
   С Е А Е
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Петушков, В.Н.; Шефер, Л.П.; Родионова, Н.С.; Фиш, А.М.

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Patterns of inhibition of bacterial bioluminescence in vitro by quinones and phenols - Components of sewage / N. S. Kudryasheva [et al.] // Biophysics. - 1994. - Vol. 39, Is. 3. - P. 441-451 . - ISSN 0006-3509
Аннотация: Quenching of bioluminescence of the bienzyme system bacterial luciferase-NAD В· H:FMN-oxidoreductaseвЂ вЂ NADВ·H is reduced nicotinamide adenine dinucleotide and FMN is flavine manonucleotide. is considered in terms of the patterns of intermolecular transfer of an electron and hydrogen between donor (bioluminescent centre) and acceptor (compound to be analysed) taking into account the structure of the acceptor molecule. The link between the induction period of bioluminescence and the redox potential of the quinone-acceptor has been confirmed. It is shown that the induction period and the time of passage to the bioluminescence maximum in the presence of quinones are determined by the size of the aromatic and aliphatic fragments of the quinone molecule; the intensity of bioluminescence depends on the efficiency of the processes of intermolecular electron transfer (donor-acceptor) and the competition of the compound being analysed with aldehyde for the binding site on luciferase. В© 1994.

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Держатели документа:
Institute of Biophysics, the Siberian Division, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Irkutsk State University Biology Research Institute, Irkutsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Shalayeva, Ye.V.; Zadorozhnaya, Ye.N.; Kratasyuk, V.A.; Balayan, A.E.; Stom, D.I.

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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.

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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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Effects of quinones on NADH-dependent enzymatic bioluminescent systems [Text] / N. S. Kudryasheva [et al.] // Appl. Biochem. Microbiol. - 2000. - Vol. 36, Is. 4. - P. 409-413, DOI 10.1007/BF02738052. - Cited References: 13 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The effects of a number of quinones on the bioluminescence characteristics of a three-component enzymatic system containing alcohol dehydrogenase, bacterial luciferase, and NADH-FMN oxidoreductase were studied to find the most sensitive kinetic parameters of the system intended to be used in biological testing. Both direct and back reactions catalyzed by alcohol dehydrogenase were studied in the presence and in the absence of quinones. The kinetic parameters of the bioluminescent system were found to depend on the redox potentials and concentrations of quinones. The quinone-induced effects were shown to be associated with changes in the NAD(+)/NADH ratio in the chain of NADH-dependent enzymes, The three-enzyme system based on alcohol dehydrogenase is suggested as a bioluminescence test for ecological monitoring of waste water.

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

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

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Characteristics of enclogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fischeri NAD(P)H : FMN-oxidoreductase [Text] / E. V. Vetrova [et al.] // Luminescence. - 2005. - Vol. 20: 11th International Symposium on Luminescence Spectrometry - Detection Techniques in Biomedical and Environmental Analysis (MAY 05-08, 2004, Beijing, JAPAN), Is. 3. - P. 205-209, DOI 10.1002/bio.815. - Cited References: 22 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology
Рубрики:
FLAVODOXIN
   ANISOTROPY
   REDUCTASE
   DYNAMICS
   SYSTEM
Кл.слова (ненормированные):
bacterial bioluminescence -- flavin fluorescence
Аннотация: The bioluminescent bacterial enzyme system NAD(P)H:FMN-oxidoreductase-luciferase has been used as a test system for ecological monitoring. One of the modes to quench bioluminescence is the interaction of xenobiotics with the enzymes, which inhibit their activity. The use of endogenous flavin fluorescence for investigation of the interactions of non-fluorescent compounds with the bacterial luciferase from Photobacterium leiognathi and NAD(P)H:FMN-oxidoreductase from Vibrio fischeri has been proposed. Fluorescence spectroscopy methods have been used to study characteristics of endogenous flavin fluorescence (fluorophore lifetime, the rotational correlation time). The fluorescence anisotropy behaviour of FMN has been analysed and compared to that of the enzyme-bound flavin. The fluorescence characteristics of endogenous flavin of luciferase and NAD(P)H:FMN-oxidoreductase have been shown to be applicable in studying enzymes' interactions with non-fluorescent compounds. Copyright (c) 2005 John Wiley & Sons, Ltd.

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Держатели документа:
RAS, SB, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Wageningen & Res Ctr, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vetrova, E.V.; Kudryasheva, N.S.; Visser, AJWG; van Hoek, A...

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Antioxidant activity of humic substances via bioluminescent monitoring in vitro [Text] / A. S. Tarasova, D. I. Stom, N. S. Kudryasheva // Environ. Monit. Assess. - 2015. - Vol. 187, Is. 3. - Ст. 89, DOI 10.1007/s10661-015-4304-1. - Cited References:51. - This work was supported by the Russian Foundation for Basic Research, Grant No. 15-03-06786a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. . - ISSN 0167-6369. - ISSN 1573-2959

РУБ Environmental Sciences
Рубрики:
DETOXIFICATION PROCESSES
   TOXICITY
   BIOASSAYS
   BACTERIA
   ASSAY
Кл.слова (ненормированные):
Antioxidant activity -- Oxidative toxicity -- General toxicity -- Humic -- substances -- Bioassay -- Bioluminescence
Аннотация: This work considers antioxidant properties of natural detoxifying agents-humic substances (HS) in solutions of model inorganic and organic compounds of oxidative nature-complex salt K-3[Fe(CN)(6)] and 1,4-benzoquinone. Bioluminescent system of coupled enzymatic reactions catalyzed by NAD(P) H:FMN-oxidoreductase and bacterial luciferase was used as a bioassay in vitro to monitor toxicity of the oxidizer solutions. Toxicities of general and oxidative types were evaluated using bioluminescent kinetic parameters-bioluminescence intensity and induction period, respectively. Antioxidant activity of HS was attributed to their ability to decrease both general and oxidative toxicities; the HS antioxidant efficiency was characterized with detoxification coefficients D-GT and D-OxT, respectively. Dependencies of D-GT and D-OxT on HS concentration and time of preliminary incubation of the oxidizers with HS were demonstrated. The optimal conditions for detoxification of the oxidizers were >20-min incubation time and 0.5x10(-4) to 2x10(-4) M of HS concentration. The present study promotes application of the enzymatic luminescent bioassay to monitor toxicity of pollutants of oxidative nature in environmental and waste waters in remediation procedures.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Irkutsk State Univ, Irkutsk 664003, Russia.
ИБФ СО РАН

Доп.точки доступа:
Tarasova, A.S.; Stom, D.I.; Kudryasheva, N.S.; Russian Foundation for Basic Research [15-03-06786a]; Russian Academy of Sciences [VI 57.1.1]

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Bioluminescent assay for toxicological assessment of nanomaterials / E. N. Esimbekova [et al.] // Dokl. Biochem. Biophys. - 2017. - Vol. 472, Is. 1. - P60-63, DOI 10.1134/S1607672917010173. - 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). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
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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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Krasnoyarsk State Agr Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Esimbekova, E. N.; Nemtseva, E. V.; Kirillova, M. A.; Asanova, A. A.; Kratasyuk, V. A.; Russian Science Foundation [16-14-10115]

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10.

Active mixing of immobilised enzymatic system in microfluidic chip / K. A. Lukyanenko [et al.] // Micro Nano Lett. - 2017. - Vol. 12, Is. 6. - P377-381, DOI 10.1049/mnl.2016.0646. - Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041). . - ISSN 1750-0443

РУБ Nanoscience & Nanotechnology + Materials Science, Multidisciplinary
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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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ITMO Univ, St Petersburg 197101, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, Kirill A.; Belousov, Kirill I.; Denisov, Ivan A.; Yakimov, Anton S.; Esimbekova, Elena N.; Bukatin, Anton S.; Evstrapov, Anatoly A.; Belobrov, Peter I.; Russian Science Foundation [15-19-10041]

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11.

Bioluminescent enzyme inhibition-based assay to predict the potential toxicity of carbon nanomaterials / E. N. Esimbekova [et al.] // Toxicol. Vitro. - 2017. - Vol. 45. - P128-133, DOI 10.1016/j.tiv.2017.08.022. - Cited References:55. - This study was supported by the Russian Science Foundation (project no. 16-14-10115). . - ISSN 0887-2333

РУБ Toxicology
Рубрики:
IN-VIVO
   ENGINEERED NANOPARTICLES
   NANOTUBE TOXICITY
   C-60
   FULLERENE
Кл.слова (ненормированные):
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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Держатели документа:
SB RAS, Fed Res Ctr, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
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.; Esimbekova, Elena; Nemtseva, Elena; Russian Science Foundation [16-14-10115]

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12.

Analytical Enzymatic Reactions in Microfluidic Chips / K. A. Lukyanenko [et al.] // Appl. Biochem. Microbiol. - 2017. - Vol. 53, Is. 7. - P775-780, DOI 10.1134/S0003683817070043. - Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041). . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
BIOAVAILABLE HEAVY-METALS
   DEVICES
   POINT
   LAB
Кл.слова (ненормированные):
bioluminescence -- luciferase -- microfluidics -- microfluidic chip -- enzymatic -- bioassay
Аннотация: A number of approaches have been proposed and tested to transfer enzymatic reactions into the functional elements of microfluidic chips on the example of the bienzyme bioluminescent reaction involving NAD(P)H:FMN-oxidoreductase and luciferase. Measurement of the catalytic activity of these enzymes (under the influence of pollutants) is the basis of enzymatic bioassay of various liquids. It was found that all of the components of the reaction must be placed in the same cell of the chip to improve the reproducibility of the measurements. The use of starch gel as a carrier for immobilization and gelatin as a scaffold in the reactor of the chip enables the preservation of enzyme activity in the course of sealing the chip at room temperature. It is shown that the components of the reaction should be vigorously stirred in a microfluidic chip reactor to improve the efficiency of the analysis. As a result of the studies, a prototype of microfluidic chip based on the enzymatic bioluminescent reaction is proposed. It is characterized by a detection limit of copper sulfate of 3 mu M that corresponds to the sensitivity of traditional lux-biosensors based on living cells. The analysis time is reduced to 1 min, and the analysis can be performed by individuals without special laboratory skills.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
St Petersburg Inst Fine Mech & Opt, St Petersburg 197101, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, K. A.; Denisov, I. A.; Yakimov, A. S.; Esimbekova, E. N.; Belousov, K. I.; Bukatin, A. S.; Kukhtevich, I. V.; Sorokin, V. V.; Evstrapov, A. A.; Belobrov, P. I.; Russian Science Foundation [15-19-10041]

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13.

Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase / O. S. Sutormin [et al.] // Mol. Cat. - 2018. - Vol. 458. - P60-66, DOI 10.1016/j.mcat.2018.08.012 . - ISSN 2468-8231
Кл.слова (ненормированные):
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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Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Sutormin, O. S.; Sukovataya, I. E.; Pande, S.; Kratasyuk, V. A.

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14.

Nutritional biomarkers: Current view and future perspectives / S. Pande [et al.] // Crit. Rev. Food Sci. Nutr. - 2018. - Vol. 58, Is. 18. - P3055-3069, DOI 10.1080/10408398.2017.1350136. - Cited References:163. - The research was partially supported by the Russian Foundation for Basic Research [Grant No 16-06-00-439], the Russian Ministry of Education, Post-Doctoral Program of Project "5-100" [Grant No. M 2.2.3] and the Russian Foundation for Basic Research in collaboration with Krasnoyarsk Regional Fund for Scientific and Technical Activity Support [project No 16-44-242126]. . - ISSN 1040-8398. - ISSN 1549-7852

РУБ Food Science & Technology + Nutrition & Dietetics
Рубрики:
PROMOTES CELL-SURVIVAL
FATTY-ACID OXIDATION
CALORIE RESTRICTION
Кл.слова (ненормированные):
Sirtuins -- NAD -- biomarker -- proteomics -- calorie restriction -- longitivity
Аннотация: There is a poor relationship between nutrient intake and existing nutritional biomarkers due to variety of factors affecting their sensitivity and specificity. To explore the impact of nutrients at molecular level and devising a sensitive biomarker, proteomics is a central technology with sirtuins as one of the most promising nutritional biomarker. Sirtuins (seven mammalian sirtuins reported so far) have been reported to perform protein deacetylases and ADP-ribosyltransferases activity. It is distributed in different cellular compartments thereby controlling several metabolic processes. Sirtuins are oxidized nicotinamide adenine dinucleotide dependent, which implicates a direct effect of the metabolic state of the cell on its activity. Calorie restriction upregulates the mammalian sirtuin protein levels in variety of tissues and organs where it acts upon both histone and nonhistone substrates. Sirtuin senses nutrient availability and impacts gluconeogenesis, glycolysis, and insulin sensitivity. It deacetylates and inhibits the nuclear receptor that activates fat synthesis and adipogenesis in the body, leading to fat loss and bringing favorable cellular and health changes. Sirtuins mediates intracellular response that promotes cell survival, DNA damage repair thereby increasing the cell longitivity. The activation of sirtuins brings a wide spectrum of other health benefits and its activity levels are indicative of nutritional status as well as disease progression in cancer, inflammation, obesity, cardiovascular diseases, and viral infections. There are several foods that activate sirtuin activity and offer significant health benefits by their consumption.

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Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Dept Biophys, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia.
Krasnoyarsk State Med Univ, Krasnoyarsk, Russia.
RAS, Siberian Branch, Inst Biophys, Fed State Budgetary Sci Inst, Krasnoyarsk, Russia.
Fed State Budgetary Sci Inst, Sci Res Inst Med Problems North, Krasnoyarsk, Russia.

Доп.точки доступа:
Pande, Shubhra; Kratasyuk, Valentina A.; Medvedeva, Nadezhda N.; Kolenchukova, Oxana A.; Salmina, Alla B.; Kratazyuk, Valentina; KAYITESI, EUGENIE; Russian Foundation for Basic Research [16-06-00-439]; Russian Ministry of Education [M 2.2.3]; Russian Foundation for Basic Research; Krasnoyarsk Regional Fund for Scientific and Technical Activity Support [16-44-242126]

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15.

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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16.

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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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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17.

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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18.

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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19.

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.

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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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20.

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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