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А.с. 1035962 СССР, МКИ C 12 N 9/02.

Способ получения препарата бактериальной люциферазы [Текст] / В. В. Межевикин [и др.] ; Ин-т биофиз. СО АН СССР. - № 3402201/28-13 ; Заявл. 21.01.19821983. -

ГРНТИ

34.27.51

РУБ 343.27.51
Рубрики:
ЛЮЦЕФЕРАЗА
   ПОЛУЧЕНИЕ
   СПОСОБ
   PHOTOBACTERIUM LEIOGNATHI
   БАКТЕРИИ
   ENZYME ISOLATION
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Межевикин, В.В.; Высоцкий, Е.С.; Заворуев, В.В.; Родичева, Э.К.; Ин-т биофиз. СО АН СССР
Свободных экз. нет
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Toxicity and antioxidant activity of fullerenol c60,70 with low number of oxygen substituents / E. S. Kovel, A. G. Kicheeva, N. G. Vnukova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 12. - Ст. 6382, DOI 10.3390/ijms22126382 . - ISSN 1661-6596
Кл.слова (ненормированные):
Antioxidant activity -- Bioluminescent assay -- Fullerenol -- Hormesis -- Reactive oxygen species -- Toxicity
Аннотация: Fullerene is a nanosized carbon structure with potential drug delivery applications. We studied the bioeffects of a water-soluble fullerene derivative, fullerenol, with 10-12 oxygen groups (F10-12); its structure was characterized by IR and XPS spectroscopy. A bioluminescent enzyme system was used to study toxic and antioxidant effects of F10-12 at the enzymatic level. Antioxidant characteristics of F10-12 were revealed in model solutions of organic and inorganic oxidizers. Low-concentration activation of bioluminescence was validated statistically in oxidizer solutions. Toxic and antioxidant characteristics of F10-12 were compared to those of homologous fullerenols with a higher number of oxygen groups:F24-28 and F40-42. No simple dependency was found between the toxic/antioxidant characteristics and the number of oxygen groups on the fullerene’s carbon cage. Lower toxicity and higher antioxidant activity of F24-28 were identified and presumptively attributed to its higher solubility. An active role of reactive oxygen species (ROS) in the bioeffects of F10-12 was demonstrated. Correlations between toxic/antioxidant characteristics of F10-12 and ROS content were evaluated. Toxic and antioxidant effects were related to the decrease in ROS content in the enzyme solutions. Our results reveal a complexity of ROS effects in the enzymatic assay system. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Physics SB RAS, FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Kovel, E. S.; Kicheeva, A. G.; Vnukova, N. G.; Churilov, G. N.; Stepin, E. A.; Kudryasheva, N. 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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Toxicity and Antioxidant Activity of Fullerenol C-60,C-70 with Low Number of Oxygen Substituents / E. S. Kovel, A. G. Kicheeva, N. G. Vnukova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 12. - Ст. 6382, DOI 10.3390/ijms22126382. - Cited References:93. - This research was funded by RFBR, N18-29-19003; RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science, N20-44-243001; and partly supported by the Program of the Federal Service for Surveillance on Consumer Rights Protection and HumanWellbeing, Fundamental Study 2020-2025 (Russian Federation). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
HUMIC SUBSTANCES
DETOXIFICATION PROCESSES
BIOLOGICAL-ACTIVITY
Кл.слова (ненормированные):
fullerenol -- toxicity -- antioxidant activity -- reactive oxygen species -- bioluminescent assay -- hormesis
Аннотация: Fullerene is a nanosized carbon structure with potential drug delivery applications. We studied the bioeffects of a water-soluble fullerene derivative, fullerenol, with 10-12 oxygen groups (F10-12); its structure was characterized by IR and XPS spectroscopy. A bioluminescent enzyme system was used to study toxic and antioxidant effects of F10-12 at the enzymatic level. Antioxidant characteristics of F10-12 were revealed in model solutions of organic and inorganic oxidizers. Low-concentration activation of bioluminescence was validated statistically in oxidizer solutions. Toxic and antioxidant characteristics of F10-12 were compared to those of homologous fullerenols with a higher number of oxygen groups:F24-28 and F40-42. No simple dependency was found between the toxic/antioxidant characteristics and the number of oxygen groups on the fullerene's carbon cage. Lower toxicity and higher antioxidant activity of F24-28 were identified and presumptively attributed to its higher solubility. An active role of reactive oxygen species (ROS) in the bioeffects of F10-12 was demonstrated. Correlations between toxic/antioxidant characteristics of F10-12 and ROS content were evaluated. Toxic and antioxidant effects were related to the decrease in ROS content in the enzyme solutions. Our results reveal a complexity of ROS effects in the enzymatic assay system.

WOS
Держатели документа:
FRC KSC SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
FRC KSC SB RAS, Inst Phys SB RAS, Krasnoyarsk 660036, Russia.
FRC KSC SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Kovel, Ekaterina S.; Kicheeva, Arina G.; Vnukova, Natalia G.; Churilov, Grigory N.; Stepin, Evsei A.; Kudryasheva, Nadezhda S.; Kovel, Ekaterina; RFBRRussian Foundation for Basic Research (RFBR) [N18-29-19003]; RFBR, Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science [N20-44-243001]; Program of the Federal Service for Surveillance on Consumer Rights Protection and Human Wellbeing, Fundamental Study 2020-2025 (Russian Federation)

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Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications / O. Mogilnaya, N. Ronzhin, E. Posokhina, V. Bondar // Protein J. - 2021, DOI 10.1007/s10930-021-10010-z. - Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, Project No. 0356-2019-0022. . - Article in press. - ISSN 1572-3887. - ISSN 1573-4943

РУБ Biochemistry & Molecular Biology
Рубрики:
ARYL-ALCOHOL OXIDASE
   GLUCOSE-OXIDASE
   PEROXIDASES
   MECHANISM
Кл.слова (ненормированные):
Extracellular oxidase -- Flavoprotein -- Fungi -- Phenol
Аннотация: The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with beta-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H2O2, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55-70 degrees C and pH 5.0. Kinetic parameters K-m and V-max of the oxidase for phenol were 0.21 mM and 0.40 mu M min(-1). We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Posokhina, Ekaterina; Bondar, Vladimir; [0356-2019-0022]

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Software for Matching Standard Activity Enzyme Biosensors for Soil Pollution Analysis / V. A. Kratasyuk, E. M. Kolosova, O. S. Sutormin [et al.] // Sensors. - 2021. - Vol. 21, Is. 3. - Ст. 1017, DOI 10.3390/s21031017. - Cited References:20. - This research was funded by RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science, Grant number 20-44-243001 and the Ministry of Science and Higher Education of the Russian Federation, Grant number FSRZ-2020-0006. . - ISSN 1424-8220

РУБ Chemistry, Analytical + Engineering, Electrical & Electronic + Instruments

Кл.слова (ненормированные):
biosensors -- enzyme -- butyrylcholinesterase -- lactic dehydrogenase -- bacterial luciferase -- soil pollution -- software
Аннотация: This work is dedicated to developing enzyme biosensor software to solve problems regarding soil pollution analysis. An algorithm and specialised software have been developed which stores, analyses and visualises data using JavaScript programming language. The developed software is based on matching data of 51 non-commercial standard soil samples and their inhibitory effects on three enzyme systems of varying complexity. This approach is able to identify the influence of chemical properties soil samples, without toxic agents, on enzyme biosensors. Such software may find wide use in environmental monitoring.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechol, Dept Biophys, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Fed Res Ctr,Siberian Branch,Inst Biophys, 50-50 Akagemgorodok, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Dept High Efficiency Calculat, 26 ULK Bldg Kirensky St, Krasnoyarsk 660074, Russia.
Russian Acad Sci, Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk Res Inst Agr, Siberian Branch,Fed Res Ctr, 66 Svobodny Pr, Krasnoyarsk 660037, Russia.
Siberian Fed Univ, Inst Fundamental Biol & Biotechol, Dept Aquat & Terr Ecosyst, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Kolosova, Elizaveta M.; Sutormin, Oleg S.; Lonshakova-Mukina, Viktoriya, I; Baygin, Matvey M.; Rimatskaya, Nadezhda, V; Sukovataya, Irina E.; Shpedt, Alexander A.; RFBRRussian Foundation for Basic Research (RFBR); Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science [20-44-243001]; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]

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Software for matching standard activity enzyme biosensors for soil pollution analysis / V. A. Kratasyuk, E. M. Kolosova, O. S. Sutormin [et al.] // Sensors. - 2021. - Vol. 21, Is. 3. - Ст. 1017. - P1-10, DOI 10.3390/s21031017 . - ISSN 1424-8220
Кл.слова (ненормированные):
Bacterial luciferase -- Biosensors -- Butyrylcholinesterase -- Enzyme -- Lactic dehydrogenase -- Software -- Soil pollution -- Biosensors -- Soil pollution -- Soil surveys -- Soils -- Commercial standards -- Environmental Monitoring -- Enzyme biosensors -- Enzyme systems -- Inhibitory effect -- JavaScript programming -- Soil sample -- Toxic agents -- Enzyme activity
Аннотация: This work is dedicated to developing enzyme biosensor software to solve problems regarding soil pollution analysis. An algorithm and specialised software have been developed which stores, analyses and visualises data using JavaScript programming language. The developed software is based on matching data of 51 non-commercial standard soil samples and their inhibitory effects on three enzyme systems of varying complexity. This approach is able to identify the influence of chemical properties soil samples, without toxic agents, on enzyme biosensors. Such software may find wide use in environmental monitoring. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechology, Siberian Federal University, 79 Svobodny pr, Krasnoyarsk, 660041, Russian Federation
Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, 50/50 Akagemgorodok, Krasnoyarsk, 660036, Russian Federation
Department of High-Efficiency Calculations, Siberian Federal University, 26-ULK building Kirensky St, Krasnoyarsk, 660074, Russian Federation
Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk Research Institute of Agriculture, Russian Academy of Sciences, Siberian Branch, 66 Svobodny pr, Krasnoyarsk, 660037, Russian Federation
Federal Research Center ‘Krasnoyarsk Scientific Center SB RAS’, Krasnoyarsk Research Institute of Agricultural, Siberian Federal University, 79 Svobodny pr, Krasnoyarsk, 660041, Russian Federation

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

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Rational Design and Mutagenesis of Fungal Luciferase from Neonothopanus nambi / K. A. Beregovaya, N. M. Myshkina, T. V. Chepurnykh [et al.] // Doklad. Biochem. Biophys. - 2021. - Vol. 496, Is. 1. - P14-17, DOI 10.1134/S1607672921010026 . - ISSN 1607-6729
Кл.слова (ненормированные):
bioluminescence -- luciferase -- Neonothopanus nambi -- rational design
Аннотация: Abstract: The recently described bioluminescent system from fungi has great potential for developing highly efficient tools for biomedical research. Luciferase enzyme is one of the most crucial components of this system. The luciferase from Neonothopanus nambi fungus belongs to the novel still undescribed protein family. The structure data for this protein is almost absent. A detailed study of the N. nambi luciferase properties is necessary for the improvement of analytical methods based on the fungal bioluminescent system. Here we present the positions of key amino acid residues and their effect on enzyme function described using bioinformatic and experimental approaches. These results are useful for further fungal luciferase structure determination. © 2021, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Beregovaya, K. A.; Myshkina, N. M.; Chepurnykh, T. V.; Kotlobay, A. A.; Purtov, K. V.; Petushkov, V. N.; Rodionova, N. S.; Yampolsky, I. V.

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Thermal Inactivation of Butyrylcholinesterase in Starch and Gelatin Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Catalysts. - 2021. - Vol. 11, Is. 4. - Ст. 492, DOI 10.3390/catal11040492. - Cited References:39. - The research was funded by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, and the Russian Foundation for Basic Research [project No 20-44-242001]. . - ISSN 2073-4344

РУБ Chemistry, Physical

Кл.слова (ненормированные):
butyrylcholinesterase -- thermal inactivation -- enzyme stability -- kinetics -- starch -- gelatin
Аннотация: The present study demonstrates a simple approach to enhancing thermal stability of butyrylcholinesterase (BChE) by using natural polymers. Analysis of thermal inactivation of the tetrameric BChE in starch and gelatin gels at 50-64 degrees C showed that thermal inactivation followed second-order kinetics and involved two alternating processes of BChE inactivation, which occurred at different rates (fast and slow processes). The activation enthalpy Delta H-# and the activation entropy Delta S-# for BChE in starch and gelatin gels were evaluated. The values of Delta H-# for the fast and the slow thermal inactivation of BChE in starch gel were 61 +/- 3, and 22 +/- 2 kcal/mol, respectively, and the values of Delta S-# were 136 +/- 12 and -2.03 +/- 0.05 cal center dot K-1 center dot mol(-1), respectively. Likewise, the values of Delta H-# for BChE in gelatin gel were 58 +/- 6 and 109 +/- 11 kcal/mol, and the values of Delta S-# were 149 +/- 16 and 262 +/- 21 cal center dot K-1 center dot mol(-1), respectively. The values of the activation parameters obtained in this study suggest that starch gel produced a stronger stabilizing effect on BChE exposed to elevated temperatures over long periods compared with gelatin gel.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Biophys Dept, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lonshakova-Mukina, Victoria I.; Esimbekova, Elena N.; Kratasyuk, Valentina A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-44-242001]

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10.

Rational Design and Mutagenesis of Fungal Luciferase from Neonothopanus nambi / K. A. Beregovaya, N. M. Myshkina, T. V. Chepurnykh [et al.] // Dokl. Biochem. Biophys. - 2021. - Vol. 496, Is. 1. - P14-17, DOI 10.1134/S1607672921010026. - Cited References:12. - This work was supported by the grant from the Russian Science Foundation no. 16-14-00052P, alanine screening was performed by the President grant for leading scientific schools NSh-2605.2020.4. . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics

Кл.слова (ненормированные):
bioluminescence -- luciferase -- Neonothopanus nambi -- rational design
Аннотация: The recently described bioluminescent system from fungi has great potential for developing highly efficient tools for biomedical research. Luciferase enzyme is one of the most crucial components of this system. The luciferase from Neonothopanus nambi fungus belongs to the novel still undescribed protein family. The structure data for this protein is almost absent. A detailed study of the N. nambi luciferase properties is necessary for the improvement of analytical methods based on the fungal bioluminescent system. Here we present the positions of key amino acid residues and their effect on enzyme function described using bioinformatic and experimental approaches. These results are useful for further fungal luciferase structure determination.

WOS
Держатели документа:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia.
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Beregovaya, K. A.; Myshkina, N. M.; Chepurnykh, T., V; Kotlobay, A. A.; Purtov, K., V; Petushkov, V. N.; Rodionova, N. S.; Yampolsky, I., V; Russian Science FoundationRussian Science Foundation (RSF) [16-14-00052P]; President grant for leading scientific schoolsLeading Scientific Schools Program [NSh-2605.2020.4]

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11.

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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12.

РУБ Biotechnology & Applied Microbiology + Engineering, Environmental
Рубрики:
FLUORIDE
   BIOASSAYS
   POLLUTION
   METALS
   WATER
Кл.слова (ненормированные):
Urbostratozems -- Soil pollution -- Industrial contamination -- Bioassay -- Bioluminescence
Аннотация: There is a need for rapid simple and informative environmental assessment methods. The present investigation is aimed at assessing the possibility of using the combined enzyme system of luminescent bacteria: NAD(P)H:FMN-oxidoreductase + luciferase (Red + Luc) for predicting the potential toxicity of industrial urbostratozems sampled in the city of Krasnoyarsk. Three groups of urbostratozems polluted with fluorine, arsenic and lead, were tested by the methods of chemical analysis and enzymatic bioassay. Only the assessment of the arsenic-contaminated soil samples showed the dependence between the reduced activity of the enzyme system and the arsenic concentration variations. The results reveal that the sensitivity of the Red + Luc enzyme system to the soil pollutants depends on the properties of the studied soil samples. Moreover, the solubility of lead in the soil samples affects the accuracy of the enzymatic bioassays for soil toxicity testing. The results of the enzymatic bioassay of the fluoride-contaminated soil samples are ambiguous. The obtained data show the relevance of the sample preparation during integral bioassays. In addition, soil properties should be taken into account as well. The current study emphasizes the importance of conducting chemical and biological testing as a combined set to obtain comprehensive information about the anthropogenic load. (C) 2021 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
Siberian Fed Univ, Dept Biophys, 79 Svobodny St, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Krasnoyarsk Agr Res Inst, Fed Res Ctr Krasnoyarsk Sci Ctr Siberian Branch, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Dept Aquat & Terr Ecosyst, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Photobiol Lab, Inst Biophys, Fed Res Ctr `Krasnoyarsk Sci Ctr Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kolosova, Elizaveta M.; Sutormin, Oleg S.; Stepanova, L. V.; Shpedt, Aleksandr A.; Rimatskaya, N. V.; Sukovataya, Irina E.; Kratasyuk, Valentina A.; Russian Foundation for Basic Research, the Government of the Krasnoyarsk Region, Russia; Krasnoyarsk Regional Foundation for Supporting Scientific and Technological Activities, Russia [18-47-240005]; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]

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13.

Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy / E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 19. - Ст. 10449, DOI 10.3390/ijms221910449. - Cited References:45. - The research was partially funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by the RFBR and Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (projects No. 20-44-243002 and 20-44-240006); and by the RFBR (project No. 20-34-90118). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
TRYPTOPHAN FLUORESCENCE
   CRYSTAL-STRUCTURE
   SUBUNIT
   BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- urea-induced denaturation -- time-resolved -- spectroscopy -- conformational stability -- FRET -- tryptophan fluorescence -- molecular dynamics -- unfolding pathway
Аннотация: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of alpha-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Russia.

Доп.точки доступа:
Nemtseva, Elena, V; Gulnov, Dmitry, V; Gerasimova, Marina A.; Sukovatyi, Lev A.; Burakova, Ludmila P.; Karuzina, Natalya E.; Melnik, Bogdan S.; Kratasyuk, Valentina A.; Burakova, Lyudmila; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]; Krasnoyarsk Regional Fund of Science [20-44-243002, 20-44-240006]; RFBRRussian Foundation for Basic Research (RFBR)

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14.

SIMILARITIES AND DIFFERENCES BETWEEN THE CHAETOPTERUS VARIOPEDATUS POLYCHAETE LUCIFERASES DEPENDING ON THE TYPE OF HABITAT / K. V. Purtov, V. N. Petushkov, N. S. Rodionova [et al.] // Bull. Russ. State Med. Univ. - 2021. - Is. 5. - P41-46, DOI 10.24075/vrgmu.2021.049. - Cited References:20 . - ISSN 2500-1094. - ISSN 2542-1204

РУБ Medicine, General & Internal
Рубрики:
BIOLUMINESCENCE
ANNELIDA
SYSTEM
Кл.слова (ненормированные):
bioluminescence -- luciferase -- polychaetes -- Chaetopterus variopedatus -- marine worms
Аннотация: The marine polychaete Chaetopterus variopedatus (Renier) (family Chaetopteridae) is a cosmopolitan species complex, consisting of distinct populations/subspecies. The worms release glowing (460 nm) clouds of mucus when disturbed, and their parapodia often glow brightly. Currently, it is still unclear how exactly the bioluminescence system of these polychaetes functions. It has been previously assumed that the C. variopedatus luciferase may be used for detection of ferroptosis, the recently explored pathway of programmed cell death, resulting from accumulation of the ferrous ions. This study was aimed to extract and characterize the C. variopedatus luciferases, as well as to compare luciferases obtained from C. variopedatus of different populations. When extracting the enzyme responsible for bioluminescence from the frozen samples of Brazilian C. variopedatus using the improved method, two active luciferases, L1 and L2, were obtained. We assumed that one of the listed above luciferases was responsible for luminescence of the mucus and the other luciferase was responsible for luminescence in parapodia, and used the method for the distinct samples of mucus and parapodia of the living Far Eastern C. variopedatus. However, mucus of the latter turned out to be non-glowing. It is shown that luciferase L2 is responsible for luminescence in the parapodia of the C. variopedatus polychaete, since this luciferase has been found in the total biomass of Brazilian polychaetes and parapodia of Far Eastern polychaetes. Luminescence of the Brazilian C. variopedatus mucus is attributed to the functioning of luciferase L1, which is lacking in the mucus of the Far Eastern subspecies. The range of luciferase isoforms in polychaetes C. variopedatus depends on the place of origin.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Krasnoyarsk Sci Ctr, Siberian Branch, Moscow, Russia.
Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia.
Pacific State Med Univ, Vladivostok, Russia.
Pirogov Russian Natl Res Med Univ, Moscow, Russia.

Доп.точки доступа:
Purtov, K., V; Petushkov, V. N.; Rodionova, N. S.; Chepurnykh, T., V; Kozhemyako, V. B.; Zagitova, R., I; Shcheglov, A. S.; Ziganshin, R. H.; Tsarkova, A. S.

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15.

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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16.

Crystal structure of semisynthetic obelin-v / M. D. Larionova, L. J. Wu, E. V. Eremeeva [et al.] // Protein Sci. - 2021, DOI 10.1002/pro.4244. - Cited References:69. - National Natural Science Foundation of China, Grant/Award Number: 32011530076; Russian Foundation for Basic Research, Grant/Award Numbers: 20-04-00085, 20-44-240006, 20-54-53011 . - Article in press. - ISSN 0961-8368. - ISSN 1469-896X

РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
PHOTOLUMINESCENCE QUANTUM YIELD
Кл.слова (ненормированные):
analog -- bioluminescence -- coelenterazine -- coelenterazine-v -- obelin -- photoprotein -- protein structure
Аннотация: Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca2+-regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca2+-regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 angstrom resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (phi(FL)) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (phi(R)) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (phi(S)). In turn, the low phi(S) value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.

WOS
Держатели документа:
SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia.
ShanghaiTech Univ, iHuman Inst, Ren Bldg,393 Middle Huaxia Rd, Shanghai 201210, Peoples R China.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk, Russia.
ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China.

Доп.точки доступа:
Larionova, Marina D.; Wu, Lijie; Eremeeva, Elena, V; Natashin, Pavel, V; Gulnov, Dmitry, V; Nemtseva, Elena, V; Liu, Dongsheng; Liu, Zhi-Jie; Vysotski, Eugene S.; Eremeeva, Elena; Nemtseva, Elena; Vysotski, Eugene; Gulnov, Dmitry; Natashin, Pavel; Larionova, Marina; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [32011530076]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 20-44-240006, 20-54-53011]

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17.

Reusable System for Phenol Detection in an Aqueous Medium Based on Nanodiamonds and Extracellular Oxidase from Basidiomycete Neonothopanus nambi / N. O. Ronzhin, O. A. Mogilnaya, E. D. Posokhina, V. S. Bondar // Dokl. Biochem. Biophys. - 2021. - Vol. 499, Is. 1. - P220-224, DOI 10.1134/S1607672921040141. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASES
EXPRESSION
Кл.слова (ненормированные):
nanodiamond -- extracellular oxidase -- basidiomycete Neonothopanus nambi -- indication system -- phenol
Аннотация: A reusable system for phenol determination in an aqueous medium was obtained by adsorption of extracellular oxidase from fungus Neonothopanus nambi onto modified nanodiamonds (MND) synthesized by detonation. It was found that the enzyme strongly binds to MND and exhibits catalytic activity in the reaction of co-oxidation of phenol with 4-aminoantipyrine without the addition of hydrogen peroxide. In the presence of the MND-oxidase complex, a significantly (by an order of magnitude) higher yield of the reaction product is recorded as compared to the yield in the presence of a free enzyme; the mechanism of the revealed effect is discussed. Model experiments have demonstrated the multiple use of the MND-oxidase complex for testing phenol in aqueous samples. The immobilized enzyme exhibits functional activity during long-term (2 months) storage of the MND-oxidase complex at 4 degrees C. The data obtained create the prerequisites for using the created system in environmental monitoring of water pollution with phenol.

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

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

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18.

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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19.

Bioluminescent enzyme inhibition-based assay for the prediction of toxicity of pollutants in urban soils / E. M. Kolosova, O. S. Sutormin, L. V. Stepanova [et al.] // Environ. Technol. Innov. - 2021. - Vol. 24. - Ст. 101842, DOI 10.1016/j.eti.2021.101842 . - ISSN 2352-1864
Кл.слова (ненормированные):
Bioassay -- Bioluminescence -- Industrial contamination -- Soil pollution -- Urbostratozems -- Arsenic -- Chemical analysis -- Enzyme activity -- Enzyme inhibition -- Fluorine compounds -- Soil surveys -- Soil testing -- Soils -- Toxicity -- Arsenic concentration -- Chemical and biologicals -- Comprehensive information -- Contaminated soils -- Environmental assessment methods -- Enzymatic bioassays -- Luminescent bacteria -- Sample preparation -- Soil pollution
Аннотация: There is a need for rapid simple and informative environmental assessment methods. The present investigation is aimed at assessing the possibility of using the combined enzyme system of luminescent bacteria: NAD(P)H:FMN-oxidoreductase + luciferase (Red + Luc) for predicting the potential toxicity of industrial urbostratozems sampled in the city of Krasnoyarsk. Three groups of urbostratozems polluted with fluorine, arsenic and lead, were tested by the methods of chemical analysis and enzymatic bioassay. Only the assessment of the arsenic-contaminated soil samples showed the dependence between the reduced activity of the enzyme system and the arsenic concentration variations. The results reveal that the sensitivity of the Red + Luc enzyme system to the soil pollutants depends on the properties of the studied soil samples. Moreover, the solubility of lead in the soil samples affects the accuracy of the enzymatic bioassays for soil toxicity testing. The results of the enzymatic bioassay of the fluoride-contaminated soil samples are ambiguous. The obtained data show the relevance of the sample preparation during integral bioassays. In addition, soil properties should be taken into account as well. The current study emphasizes the importance of conducting chemical and biological testing as a combined set to obtain comprehensive information about the anthropogenic load. © 2021 Elsevier B.V.

Scopus
Держатели документа:
Department of Biophysics, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Krasnoyarsk Agricultural Research Institute, Federal Research Center ‘Krasnoyarsk Science Center Siberian Branch of the Russian Academy of Sciences’, Krasnoyarsk, 660036, Russian Federation
Department of Aquatic and Terrestrial Ecosystems, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Photobiology Laboratory, Institute of Biophysics, Federal Research Center ‘Krasnoyarsk Science Center Siberian Branch of the Russian Academy of Sciences’, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kolosova, E. M.; Sutormin, O. S.; Stepanova, L. V.; Shpedt, A. A.; Rimatskaya, N. V.; Sukovataya, I. E.; Kratasyuk, V. A.

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20.

Bacterial luciferases from vibrio harveyi and photobacterium leiognathi demonstrate different conformational stability as detected by time-resolved fluorescence spectroscopy / E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 19. - Ст. 10449, DOI 10.3390/ijms221910449 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Conforma-tional stability -- FRET -- Molecular dynamics -- Time-resolved spectroscopy -- Tryptophan fluorescence -- Unfolding pathway -- Urea-induced denaturation
Аннотация: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of ?-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Photobiology Laboratory, Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142290, Russian Federation

Доп.точки доступа:
Nemtseva, E. V.; Gulnov, D. V.; Gerasimova, M. A.; Sukovatyi, L. A.; Burakova, L. P.; Karuzina, N. E.; Melnik, B. S.; Kratasyuk, V. A.

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