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Enzymatic Biotesting: Scientific Basis and Application / E. N. Esimbekova, I. G. Torgashina, V. P. Kalyabina, V. A. Kratasyuk // Contemp. Probl. Ecol. - 2021. - Vol. 14, Is. 3. - P290-304, DOI 10.1134/S1995425521030069. - Cited By :1 . - ISSN 1995-4255
Кл.слова (ненормированные):
bioluminescence -- biotesting -- environmental monitoring -- enzymatic bioassays -- heavy metals -- pesticides
Аннотация: Abstract: The paper provides a review of the current state of research in the field of biotesting, and the problems of environmental studies and ways to solve them are discussed. The basic principles and examples of using enzymes for detecting toxicants in various environmental samples are considered. Based on an analysis of numerous published data, the advantages and limitations, as well as the prospects for using enzymes for performing biotesting tasks, are assessed. A separate section of the review is devoted to bioluminescent enzymatic bioassays developed by the authors and successfully used for environmental monitoring of water, soil, and air. The necessity of developing a battery of enzymatic bioassays is substantiated. It allows one to have the most complete and accurate information about the degree of pollution of environmental objects. © 2021, Pleiades Publishing, Ltd.

Scopus
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:
Esimbekova, E. N.; Torgashina, I. G.; Kalyabina, V. P.; Kratasyuk, V. A.

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Enzymatic Biotesting: Scientific Basis and Application / E. N. Esimbekova, I. G. Torgashina, V. P. Kalyabina, V. A. Kratasyuk // Contemp. Probl. Ecol. - 2021. - Vol. 14, Is. 3. - P290-304, DOI 10.1134/S1995425521030069. - Cited References:128. - This study was carried out with financial support from the Russian Foundation for Basic Research, project no. 19-14-50238\19. . - ISSN 1995-4255. - ISSN 1995-4263

РУБ Ecology
Рубрики:
ORGANOPHOSPHORUS PESTICIDES
CHRONIC EXPOSURE
BIOSENSOR
Кл.слова (ненормированные):
biotesting -- enzymatic bioassays -- bioluminescence -- environmental -- monitoring -- pesticides -- heavy metals
Аннотация: The paper provides a review of the current state of research in the field of biotesting, and the problems of environmental studies and ways to solve them are discussed. The basic principles and examples of using enzymes for detecting toxicants in various environmental samples are considered. Based on an analysis of numerous published data, the advantages and limitations, as well as the prospects for using enzymes for performing biotesting tasks, are assessed. A separate section of the review is devoted to bioluminescent enzymatic bioassays developed by the authors and successfully used for environmental monitoring of water, soil, and air. The necessity of developing a battery of enzymatic bioassays is substantiated. It allows one to have the most complete and accurate information about the degree of pollution of environmental objects.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Esimbekova, E. N.; Torgashina, I. G.; Kalyabina, V. P.; Kratasyuk, V. A.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-14-50238\19]

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Detecting bioluminescence conditions in fruit bodies of two species of Armillaria basidiomycetes / A. P. Puzyr, A. E. Burov, V. S. Bondar // IOP Conference Series: Earth and Environmental Science : IOP Publishing Ltd, 2021. - Vol. 677: 4th International Scientific Conference on Agribusiness, Environmental Engineering and Biotechnologies, AGRITECH-IV 2020 (18 November 2020 through 20 November 2020, ) Conference code: 167873, Is. 5. - Ст. 052081, DOI 10.1088/1755-1315/677/5/052081
Кл.слова (ненормированные):
Bioluminescence -- Biotechnology -- Fungi -- Phosphorescence -- Armillaria -- Armillaria species -- Fruit body -- Possible mechanisms -- Fruits
Аннотация: Mycelia of various Armillaria fungi are bioluminescent while the fruit bodies do not emit light. The presence in fruit bodies of Armillaria species of enzymes involved in the fungal bioluminescence was investigated by treating them with an exogenous analogue of the substrate for the light-emitting reaction. For this, hot extracts from nonluminous fungus Pholiota squarrosa were used. Upon spraying the pristine and transversely cut fruit bodies with the extracts, light emitting regions of different intensity were revealed. This suggests that the fruit bodies of the studied species are nonluminous due to lack of the substrate for light luminescent reaction. The prolonged incubation of the fruit bodies in water elevated the bioluminescence level. A possible mechanism which can explain this phenomenon is discussed. © 2021 Institute of Physics Publishing. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Federal Research Center for Information and Computational Technologies, Krasnoyarsk, 660049, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Burov, A. E.; Bondar, V. S.

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Design of bioluminescent biosensors for assessing contamination of complex matrices / E. N. Esimbekova, V. P. Kalyabina, K. V. Kopylova [et al.] // Talanta. - 2021. - Vol. 233. - Ст. 122509, DOI 10.1016/j.talanta.2021.122509. - Cited By :1 . - ISSN 0039-9140
Кл.слова (ненормированные):
Bioluminescent biosensor -- Complex matrices -- Enzyme inhibition-based assay -- Heavy metals -- Pesticides
Аннотация: The presence of potentially toxic xenobiotics in complex matrices has become rather the rule than the exception. Therefore, there is a need for highly sensitive inexpensive techniques for analyzing environmental and food matrices for toxicants. Enzymes are selectively sensitive to various toxic compounds, and, thus, they can be used as the basis for detection of contaminants in complex matrices. There are, however, a number of difficulties associated with the analysis of complex matrices using enzyme assays, including the necessity to take into account properties and effects of the natural components of the test media for accurate interpretation of results. The present study describes the six-stage procedure for designing new enzyme sensors intended for assessing the quality of complex matrices. This procedure should be followed both to achieve the highest possible sensitivity of the biosensor to potentially toxic substances and to minimize the effect of the uncontaminated components of complex mixtures on the activity of the biosensor. The proposed strategy has been tested in designing a bioluminescent biosensor for integrated rapid assessment of the safety of fruits and vegetables. The biosensor is based on the coupled enzyme system NAD(P)H:FMN-oxidoreductase and luciferase as the biorecognition element. The study describes methods and techniques for attaining the desired result in each stage. The proposed six-stage procedure for designing bioluminescent enzyme biosensors can be used to design the enzymatic biosensors based on other enzymes. © 2021 Elsevier B.V.

Scopus
Держатели документа:
Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Kalyabina, V. P.; Kopylova, K. V.; Torgashina, I. G.; Kratasyuk, V. A.

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Mechanisms of Viscous Media Effects on Elementary Steps of Bacterial Bioluminescent Reaction / A. E. Lisitsa, L. A. Sukovatyi, S. I. Bartsev [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 16. - Ст. 8827, DOI 10.3390/ijms22168827. - Cited References:59. - The research was funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (project No. 20-44-243002); by RFBR according to the research project No. 20-34-90118. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
FLAVIN INTERMEDIATE
   REDUCED FLAVIN
   RATE CONSTANTS
   LUCIFERASE
Кл.слова (ненормированные):
bacterial luciferase -- non-steady-state reaction kinetics -- viscosity -- diffusion limitation
Аннотация: Enzymes activity in a cell is determined by many factors, among which viscosity of the microenvironment plays a significant role. Various cosolvents can imitate intracellular conditions in vitro, allowing to reduce a combination of different regulatory effects. The aim of the study was to analyze the media viscosity effects on the rate constants of the separate stages of the bacterial bioluminescent reaction. Non-steady-state reaction kinetics in glycerol and sucrose solutions was measured by stopped-flow technique and analyzed with a mathematical model developed in accordance with the sequence of reaction stages. Molecular dynamics methods were applied to reveal the effects of cosolvents on luciferase structure. We observed both in glycerol and in sucrose media that the stages of luciferase binding with flavin and aldehyde, in contrast to oxygen, are diffusion-limited. Moreover, unlike glycerol, sucrose solutions enhanced the rate of an electronically excited intermediate formation. The MD simulations showed that, in comparison with sucrose, glycerol molecules could penetrate the active-site gorge, but sucrose solutions caused a conformational change of functionally important alpha Glu175 of luciferase. Therefore, both cosolvents induce diffusion limitation of substrates binding. However, in sucrose media, increasing enzyme catalytic constant neutralizes viscosity effects. The activating effect of sucrose can be attributed to its exclusion from the catalytic gorge of luciferase and promotion of the formation of the active site structure favorable for the catalysis.

WOS
Держатели документа:
Siberian Fed Univ, Biophys Dept, Svobodny 79, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lisitsa, Albert E.; Sukovatyi, Lev A.; Bartsev, Sergey, I; Deeva, Anna A.; Kratasyuk, Valentina A.; Nemtseva, Elena, V; Nemtseva, Elena; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science [20-44-243002]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]

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Development of Cellular and Enzymatic Bioluminescent Assay Systems to Study Low-Dose Effects of Thorium / O. V. Kolesnik, T. V. Rozhko, M. A. Lapina [et al.] // Bioengineering-Basel. - 2021. - Vol. 8, Is. 12. - Ст. 194, DOI 10.3390/bioengineering8120194. - Cited References:77 . - ISSN 2306-5354

РУБ Biotechnology & Applied Microbiology + Engineering, Biomedical

Кл.слова (ненормированные):
bioassay -- bioluminescence -- luminous bacteria -- enzymes -- reactive oxygen -- species -- thorium -- low-dose exposure -- radiation hormesis
Аннотация: Thorium is one of the most widespread radioactive elements in natural ecosystems, along with uranium, it is the most important source of nuclear energy. However, the effects of thorium on living organisms have not been thoroughly studied. Marine luminescent bacteria and their enzymes are optimal bioassays for studying low-dose thorium exposures. Luminescent bioassays provide a quantitative measure of toxicity and are characterized by high rates, sensitivity, and simplicity. It is known that the metabolic activity of bacteria is associated with the production of reactive oxygen species (ROS). We studied the effects of thorium-232 (10(-11)-10(-3) M) on Photobacterium phosphoreum and bacterial enzymatic reactions; kinetics of bacterial bioluminescence and ROS content were investigated in both systems. Bioluminescence activation was revealed under low-dose exposures (<0.1 Gy) and discussed in terms of "radiation hormesis". The activation was accompanied by an intensification of the oxidation of a low-molecular reducer, NADH, during the enzymatic processes. Negative correlations were found between the intensity of bioluminescence and the content of ROS in bacteria and enzyme systems; an active role of ROS in the low-dose activation by thorium was discussed. The results contribute to radioecological potential of bioluminescence techniques adapted to study low-intensity radioactive exposures.

WOS
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Inst Biophys SB, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Biophys Dept, Krasnoyarsk 660041, Russia.
Krasnoyarsk State Med Acad, Krasnoyarsk 660022, Russia.
Natl Res Tomsk Polytech Univ, Tomsk 634050, Russia.

Доп.точки доступа:
Kolesnik, Olga V.; Rozhko, Tatiana V.; Lapina, Maria A.; Solovyev, Vladislav S.; Sachkova, Anna S.; Kudryasheva, Nadezhda S.; Kolesnik, Olga

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Design of bioluminescent biosensors for assessing contamination of complex matrices / E. N. Esimbekova, V. P. Kalyabina, K. V. Kopylova [et al.] // Talanta. - 2021. - Vol. 233. - Ст. 122509, DOI 10.1016/j.talanta.2021.122509. - Cited References:87. - The reported study was funded by Russian Foundation for Basic Research, Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, to the research project No. 20-44-242001 and Ministry of Science and Higher Education of Russian Federation No. FSRZ-2020-0006. . - ISSN 0039-9140. - ISSN 1873-3573

РУБ Chemistry, Analytical
Рубрики:
SAMPLE PREPARATION
   PESTICIDES
   FOOD
   BIOMOLECULES
   SENSITIVITY
Кл.слова (ненормированные):
Bioluminescent biosensor -- Enzyme inhibition-based assay -- Complex -- matrices -- Pesticides -- Heavy metals
Аннотация: The presence of potentially toxic xenobiotics in complex matrices has become rather the rule than the exception. Therefore, there is a need for highly sensitive inexpensive techniques for analyzing environmental and food matrices for toxicants. Enzymes are selectively sensitive to various toxic compounds, and, thus, they can be used as the basis for detection of contaminants in complex matrices. There are, however, a number of difficulties associated with the analysis of complex matrices using enzyme assays, including the necessity to take into account properties and effects of the natural components of the test media for accurate interpretation of results. The present study describes the six-stage procedure for designing new enzyme sensors intended for assessing the quality of complex matrices. This procedure should be followed both to achieve the highest possible sensitivity of the biosensor to potentially toxic substances and to minimize the effect of the uncontaminated components of complex mixtures on the activity of the biosensor. The proposed strategy has been tested in designing a bioluminescent biosensor for integrated rapid assessment of the safety of fruits and vegetables. The biosensor is based on the coupled enzyme system NAD(P)H:FMN-oxidoreductase and luciferase as the biorecognition element. The study describes methods and techniques for attaining the desired result in each stage. The proposed six-stage procedure for designing bioluminescent enzyme biosensors can be used to design the enzymatic biosensors based on other enzymes.

WOS
Держатели документа:
Siberian Fed Univ, 79 Svobodny Prospect, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Esimbekova, Elena N.; Kalyabina, Valeriya P.; Kopylova, Kseniya, V; Torgashina, Irina G.; Kratasyuk, Valentina A.; Kopylova, Kseniya; Esimbekova, Elena; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR); Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science [20-44-242001]; Ministry of Science and Higher Education of Russian Federation [FSRZ-2020-0006]

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Mechanisms of viscous media effects on elementary steps of bacterial bioluminescent reaction / A. E. Lisitsa, L. A. Sukovatyi, S. I. Bartsev [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 16. - Ст. 8827, DOI 10.3390/ijms22168827 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Diffusion limitation -- Non-steady-state reaction kinetics -- Viscosity
Аннотация: Enzymes activity in a cell is determined by many factors, among which viscosity of the microenvironment plays a significant role. Various cosolvents can imitate intracellular conditions in vitro, allowing to reduce a combination of different regulatory effects. The aim of the study was to analyze the media viscosity effects on the rate constants of the separate stages of the bacterial biolumi-nescent reaction. Non-steady-state reaction kinetics in glycerol and sucrose solutions was measured by stopped-flow technique and analyzed with a mathematical model developed in accordance with the sequence of reaction stages. Molecular dynamics methods were applied to reveal the effects of cosolvents on luciferase structure. We observed both in glycerol and in sucrose media that the stages of luciferase binding with flavin and aldehyde, in contrast to oxygen, are diffusion-limited. More-over, unlike glycerol, sucrose solutions enhanced the rate of an electronically excited intermediate formation. The MD simulations showed that, in comparison with sucrose, glycerol molecules could penetrate the active-site gorge, but sucrose solutions caused a conformational change of functionally important ?Glu175 of luciferase. Therefore, both cosolvents induce diffusion limitation of substrates binding. However, in sucrose media, increasing enzyme catalytic constant neutralizes viscosity effects. The activating effect of sucrose can be attributed to its exclusion from the catalytic gorge of luciferase and promotion of the formation of the active site structure favorable for the catalysis. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Biophysics Department, Siberian Federal University, Svobodny 79, Krasnoyarsk, 660041, Russian Federation
The Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Lisitsa, A. E.; Sukovatyi, L. A.; Bartsev, S. I.; Deeva, A. A.; Kratasyuk, V. A.; Nemtseva, E. V.

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Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465. - P1-31, DOI 10.3390/ijms21207465 . - ISSN 1661-6596
Кл.слова (ненормированные):
Analytical systems -- Bioluminescence -- Ca2+-regulated photoprotein -- Coelenterazine -- Luciferase
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

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

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10.

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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11.

Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties / N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko [et al.] // Dokl. Biochem. Biophys. - 2020. - Vol. 490, Is. 1. - P38-42, DOI 10.1134/S1607672920010135. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASE-ACTIVITY
LIGHT-EMISSION
Кл.слова (ненормированные):
extracellular oxidases -- basidiomycete Neonothopanus nambi -- beta-glucosidase -- gel-filtration chromatography -- veratryl alcohol -- phenol -- FAD
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.

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

Доп.точки доступа:
Ronzhin, N. O.; Mogilnaya, O. A.; Artemenko, K. S.; Posokhina, E. D.; Bondar, V. S.

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12.

Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

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13.

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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14.

15.

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.

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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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16.

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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17.

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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18.

Nanodiamonds as an effective adsorbent for immobilization of extracellular peroxidases from luminous fungus Neonothopanus nambi to construct a phenol detection system / O. Mogilnaya [et al.] // Biocatal. Biotransform. - 2019. - Vol. 37, Is. 2. - P97-105, DOI 10.1080/10242422.2018.1472586. - Cited References:50. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences [project no. 0356-2016-0709]. . - ISSN 1024-2422. - ISSN 1029-2446

РУБ Biochemistry & Molecular Biology + Biotechnology & Applied Microbiology
Рубрики:
CARBON NANOTUBES
   ARMILLARIA-BOREALIS
   LIGHT-EMISSION
   DEGRADATION
Кл.слова (ненормированные):
Nanodiamonds -- immobilization -- luminous fungus -- beta-glucosidase -- peroxidase -- indicator system
Аннотация: Modified nanodiamonds (MNDs) produced by detonation synthesis can be used as an effective adsorbent to immobilize extracellular peroxidases of the luminous basidiomycete Neonothopanus nambi. The enzymes are firmly immobilized on MND particles and exhibit catalytic activity. The indicator system (the MND-enzyme complex) reused many times retains its ability to catalyze reaction of co-oxidation of phenol and 4-aminoantipirine in the presence of hydrogen peroxide and remains functionally active during long-term storage (for 1 month or longer) in aqueous suspensions at 4 degrees C. MNDs and enzymes of higher fungi can be effectively used to construct new reusable indicator systems for analytical applications such as monitoring contamination of aquatic environments by phenolic compounds.

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Держатели документа:
RAS, Inst Biophys, Fed Res Ctr, Krasnoyarsk Sci Ctr,SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Artemenko, Karina; Bondar, Vladimir; Russian Academy of Sciences [0356-2016-0709]

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19.

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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20.

Monitoring of Low-Intensity Exposures via Luminescent Bioassays of Different Complexity: Cells, Enzyme Reactions, and Fluorescent Proteins / N. S. Kudryasheva, E. S. Kovel // Int J Mol Sci. - 2019. - Vol. 20, Is. 18. - Ст. 4451, DOI 10.3390/ijms20184451 . - ISSN 1422-0067
Кл.слова (ненормированные):
antioxidant activity -- bacterial cells, enzymes -- bioactive compounds -- fluorescent protein -- hormesis -- low-intensity factors -- luminescence bioassays -- radiation
Аннотация: The current paper reviews the applications of luminescence bioassays for monitoring the results of low-intensity exposures which produce a stimulative effect. The impacts of radioactivity of different types (alpha, beta, and gamma) and bioactive compounds (humic substances and fullerenols) are under consideration. Bioassays based on luminous marine bacteria, their enzymes, and fluorescent coelenteramide-containing proteins were used to compare the results of the low-intensity exposures at the cellular, biochemical, and physicochemical levels, respectively. High rates of luminescence response can provide (1) a proper number of experimental results under comparable conditions and, therefore, proper statistical processing, with this being highly important for "noisy" low-intensity exposures; and (2) non-genetic, i.e., biochemical and physicochemical mechanisms of cellular response for short-term exposures. The results of cellular exposures were discussed in terms of the hormesis concept, which implies low-dose stimulation and high-dose inhibition of physiological functions. Dependencies of the luminescence response on the exposure time or intensity (radionuclide concentration/gamma radiation dose rate, concentration of the bioactive compounds) were analyzed and compared for bioassays of different organization levels.

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Держатели документа:
Institute of Biophysics, Federal Research Center "Krasnoyarsk Science Center, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Physics, Federal Research Center "Krasnoyarsk Science Center, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kudryasheva, N. S.; Kovel, E. S.

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