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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 / T. G. Volova [et al.] // Applied Biochemistry and Microbiology. - 2004. - Vol. 40, Is. 2. - P170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5 . - ISSN 0003-6838
Кл.слова (ненормированные):
acetyl coenzyme A acyltransferase -- bacterial enzyme -- carbon -- carbon dioxide -- fructose -- hydrogen -- hydroxybutyrate dehydrogenase -- oxidoreductase -- poly(3 hydroxybutyric acid) -- polyhydroxyalkanoic acid -- synthetase -- article -- bacterial metabolism -- carbon source -- catalysis -- controlled study -- degradation -- depolymerization -- enzyme activity -- enzyme analysis -- molecular dynamics -- nonhuman -- protein function -- Ralstonia eutropha -- recording -- statistical significance -- synthesis -- Bacteria (microorganisms) -- Ralstonia -- Wautersia eutropha
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (?-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of ?-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide / T. G. Volova, G. S. Kalacheva, O. V. Altukhova // Applied Microbiology and Biotechnology. - 2002. - Vol. 58, Is. 5. - P675-678, DOI 10.1007/s00253-002-0941-8 . - ISSN 0175-7598
Кл.слова (ненормированные):
3 hydroxybutyric acid -- acetoacetyl coenzyme a reductase -- acetyl coenzyme A acyltransferase -- beta hydroxyvalerate -- butyrate dehydrogenase -- carbon monoxide -- electrolyte -- hydrogen -- oxidoreductase -- poly(3 hydroxybutyric acid) -- poly(3 hydroxybutyric acid)synthase -- polyhydroxyalkanoic acid -- polymer -- unclassified drug -- valeric acid -- bacterium -- article -- autotrophy -- bacterial growth -- bacterial strain -- biomass production -- controlled study -- crystallization -- enzyme activity -- molecular weight -- nonhuman -- synthesis -- temperature -- Wautersia eutropha -- Carbon Monoxide -- Culture Media -- Cupriavidus necator -- Fatty Acids -- Lipids -- Polyesters -- Bacteria (microorganisms) -- Negibacteria -- Ralstonia -- Wautersia eutropha
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxy-alkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO (v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (?-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly ?-hydroxybutyrate (more than 99 mol%) with trace amounts of ?-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Altukhova, O.V.

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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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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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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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EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV, N. S. RODIONOVA, P. I. BELOBROV // Biochem.-Moscow. - 1985. - Vol. 50, Is. 3. - P338-342. - Cited References: 13 . - 5. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; RODIONOVA, N.S.; BELOBROV, P.I.

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2-ENZYME NADH-FMN-OXIDOREDUCTASE-LUCIFERASE SYSTEM FROM LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV [et al.] // Biochem.-Moscow. - 1984. - Vol. 49, Is. 4. - P593-603. - Cited References: 24 . - 11. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

Держатели документа:
LV KIRENSKII PHYS INST,KRASNOYARSK,USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; KRATASYUK, G.A.; RODIONOVA, N.S.; FISH, A.M.; BELOBROV, P.I.

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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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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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10.

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

11.

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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12.

EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV, N. S. RODIONOVA, P. I. BELOBROV // Biochem.-Moscow. - 1985. - Vol. 50, Is. 3. - P. 338-342. - Cited References: 13 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; RODIONOVA, N.S.; BELOBROV, P.I.

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13.

A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL [Text] / V. A. KRATASYUK, V. V. ABAKUMOVA, N. B. KIM // Biochem.-Moscow. - 1994. - Vol. 59, Is. 7. - P. 761-765. - Cited References: 11 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENT
Кл.слова (ненормированные):
BIOLUMINESCENCE -- LUCIFERASE -- NADH, FMN-OXIDOREDUCTASE -- IMMOBILIZATION
Аннотация: A gel model for the functioning of luciferase in cells has been constructed using bacterial NADH:FMN-oxidoreductase and luciferase immobilized in starch gel disks. The characteristics of the immobilized luciferase depend on the duration of drying, the amount and concentration of the gel, the nature of the support used for drying, and the properties of the initial enzyme preparation. Functionally important enzyme groups remain intact in the immobilized preparation, and luciferase retains its high specificity with respect to aldehydes. The gel microenvironment appears to be optimal for luciferase, judging from its high activity and increased stability. Conditions allowing repeated use of the preparation have been found. The approach permits co-immobilization of luciferase with other enzymes and their substrates. The error in bioluminescence measurements using the disks is 5-10%. A procedure for stabilization of the immobilized luciferase during repeated use has been devised.

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

Доп.точки доступа:
KRATASYUK, V.A.; ABAKUMOVA, V.V.; KIM, N.B.

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14.

A biological luciferase test for the bioluminescent assay of wheat grain infection with Fusarium [Text] / V. A. Kratasyuk [et al.] // Appl. Biochem. Microbiol. - 1998. - Vol. 34, Is. 6. - P. 622-624. - Cited References: 7 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The extent of inhibition of the bioluminescence reaction by wheat grain extracts was studied as a function of the scabby kernel content in wheat. The NADH : flavine mononucleotide oxidoreductase-luciferase bienzyme bioluminescence system was found to be the most sensitive to mycotoxins produced by fungi of the genus Fusarium. A biological luciferase test was developed for monitoring wheat grain infection with Fusarium.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
All Russia Res Inst Grain & Grain Prod, Moscow 127434, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Egorova, O.I.; Esimbekova, E.N.; Kudryashova, N.S.; Orlova, N.Y.; L'vova, L.S.

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15.

Effect of Fusarium mycotoxins an a bacterial bioluminescence system in vitro [Text] / V. A. Kratasyuk [et al.] // Appl. Biochem. Microbiol. - 1998. - Vol. 34, Is. 2. - P. 190-192. - Cited References: 7 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The effects of the mycotoxins produced by fungi of the genus Fusarium on the NADH : Ravine mononucleotide oxidoreductase-luciferase bacterial bioluminescence system was studied. The sensitivity of the bioluminescence system to mycotoxins decreases in the following order: zearalenone, deoxynivalenol, toxin T-2, and diacetoxiscripenol. These results allow the development of a luciferase bioluminescence test system for rapid control of grain infection with Fusarium.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
All Russian Res Inst Grain & Grain Prod, Moscow 127434, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660062, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; L'vova, L.S.; Egorova, O.I.; Kudryasheva, N.S.; Orlova, N.Y.; Bytev, V.O.

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16.

Bioluminescent water quality monitoring of salt lake Shira [Text] / V. A. Kratasyuk, E. V. Vetrova, N. S. Kudryasheva // Luminescence. - 1999. - Vol. 14: 10th International Symposium on Bioluminescence and Chemiluminescence (1998, BOLOGNA, ITALY), Is. 4. - P. 193-195, DOI 10.1002/(SICI)1522-7243(199907/08)14:4193::AID-BIO5283.3.CO;2-J. - Cited References: 9 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bioluminescence -- biotest -- ecological monitoring -- salt lake
Аннотация: The coupled bioluminescent enzyme system luciferase-NADH:FMN-oxidoreductase was used as a biotest in ecological monitoring of the health resort salt lake Shira (South Siberia, Russia). The technique was adapted to saltwater conditions. Bioluminescence kinetic parameters sensitive to pollutants were determined. Conditions for the use of bacterial bioluminescence biotests in salty environmental media were established. Copyright (C) 1999 John Wiley & Sons, Ltd.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, SB, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Vetrova, E.V.; Kudryasheva, N.S.

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17.

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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18.

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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19.

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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20.

Bioluminescence assays: Effects of quinones and phenols [Text] / N. . Kudryasheva [et al.] // Ecotox. Environ. Safe. - 2002. - Vol. 53, Is. 2. - P. 221-225, DOI 10.1006/eesa.2002.2214. - Cited References: 18 . - ISSN 0147-6513

РУБ Environmental Sciences + Toxicology

Кл.слова (ненормированные):
bioluminescence assays -- quinones -- phenols
Аннотация: The influence of a series of quinones and phenols on bacterial bioluminescence systems was investigated. Three bioluminescence systems used in ecological monitoring were compared: (1) water-soluble; (2) immobilized in starch gel coupled enzyme systems: NADH:FMN-oxidoreductase-luciferase; (3) luminescent bacteria. Bioluminescence inhibition constants of quinones and phenols and bioluminescence induction periods were compared. These kinetic parameters are proportional to quinone concentrations and depend on the quinone redox potential. Different effects of the substances are related to structure and properties of the bioluminescence systems. The set of bioluminescence assays for quinones and phenols monitoring should include two bioluminescence systems: 1 (or 2) and 3. (C) 2002 Elsevier Science (USA).

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, 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...; Vetrova, E...; Kuznetsov, A...; Kratasyuk, V...; Stom, D...

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