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A Glucose-Utilizing Strain, Cupriavidus euthrophus B-10646: Growth Kinetics, Characterization and Synthesis of Multicomponent PHAs [Text] / T. . Volova [et al.] // PLoS One. - 2014. - Vol. 9, Is. 2. - Ст. e87551, DOI 10.1371/journal.pone.0087551. - Cited References: 64. - This study was financially supported by Project "Biotechnologies of novel biomaterials: Innovative Biopolymers and Biomedicine Devices" (Agreement No. 11.G34.31.0013 with Amendment No. 1 of 15 February 2013) in accordance with Resolution No. 220 of the Government of the Russian Federation of April 9, 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning." The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 1932-6203

РУБ Multidisciplinary Sciences
Рубрики:
RALSTONIA-EUTROPHA
   BIODEGRADABLE POLYHYDROXYALKANOATES
   AEROMONAS-HYDROPHILA
   ESCHERICHIA-COLI
   MOLECULAR-WEIGHT
   SURFACE-ENERGY
   NORTH PACIFIC
   TERPOLYESTER
   BIOSYNTHESIS
   POLY(3-HYDROXYBUTYRATE-CO-3-HYDROXYVALERATE-CO-3-HYDROXYHEXANOATE)
Аннотация: This study investigates kinetic and production parameters of a glucose-utilizing bacterial strain, C. eutrophus B-10646, and its ability to synthesize PHA terpolymers. Optimization of a number of parameters of bacterial culture (cell concentration in the inoculum, physiological activity of the inoculum, determined by the initial intracellular polymer content, and glucose concentration in the culture medium during cultivation) provided cell concentrations and PHA yields reaching 110 g/L and 80%, respectively, under two-stage batch culture conditions. Addition of precursor substrates (valerate, hexanoate, propionate, c-butyrolactone) to the culture medium enabled synthesis of PHA terpolymers, P(3HB/3HV/4HB) and P(3HB/3HV/3HHx), with different composition and different molar fractions of 3HB, 3HV, 4HB, and 3HHx. Different types of PHA terpolymers synthesized by C. eutrophus B-10646 were used to prepare films, whose physicochemical and physicalmechanical properties were investigated. The properties of PHA terpolymers were significantly different from those of the P3HB homopolymer: they had much lower degrees of crystallinity and lower melting points and thermal decomposition temperatures, with the difference between these temperatures remaining practically unchanged. Films prepared from all PHA terpolymers had higher mechanical strength and elasticity than P3HB films. In spite of dissimilar surface structures, all films prepared from PHA terpolymers facilitated attachment and proliferation of mouse fibroblast NIH 3T3 cells more effectively than polystyrene and the highly crystalline P3HB.

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Держатели документа:
[Volova, Tatiana
Kiselev, Evgeniy
Nikolaeva, Elena
Sukovatiy, Aleksey
Shishatskaya, Ekaterina] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Volova, Tatiana
Vinogradova, Olga
Shishatskaya, Ekaterina] Siberian Fed Univ, Krasnoyarsk, Russia
[Chistyakov, Anton] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T...; Kiselev, E...; Vinogradova, O...; Nikolaeva, E...; Chistyakov, A...; Sukovatiy, A...; Shishatskaya, E...; Project "Biotechnologies of novel biomaterials: Innovative Biopolymers and Biomedicine Devices" [11.G34.31.0013]

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A glucose-utilizing strain, cupriavidus euthrophus B-10646: Growth kinetics, characterization and synthesis of multicomponent PHAs / T. Volova [et al.] // PLoS ONE. - 2014. - Vol. 9, Is. 2, DOI 10.1371/journal.pone.0087551 . - ISSN 1932-6203
Кл.слова (ненормированные):
3 hydroxybutyrate 3 hydroxyhexanoate 3 hydroxyvalerate copolymer -- 3 hydroxybutyrate 4 hydroxybutyrate 3 hydroxyvalerate copolymer -- copolymer -- gamma butyrolactone -- glucose -- hexanoic acid -- poly(3 hydroxybutyric acid) -- polyhydroxyalkanoic acid -- polystyrene -- propionic acid -- unclassified drug -- valeric acid -- animal cell -- article -- bacterial growth -- bacterium culture -- cell adhesion -- cell proliferation -- crystal structure -- culture optimization -- Cupriavidus -- Cupriavidus euthrophus -- decomposition -- elasticity -- film -- glucose utilization -- kinetics -- mechanics -- melting point -- mouse -- nonhuman -- nucleotide sequence -- physical chemistry -- polymerization -- strength -- synthesis
Аннотация: This study investigates kinetic and production parameters of a glucose-utilizing bacterial strain, C. eutrophus B-10646, and its ability to synthesize PHA terpolymers. Optimization of a number of parameters of bacterial culture (cell concentration in the inoculum, physiological activity of the inoculum, determined by the initial intracellular polymer content, and glucose concentration in the culture medium during cultivation) provided cell concentrations and PHA yields reaching 110 g/L and 80%, respectively, under two-stage batch culture conditions. Addition of precursor substrates (valerate, hexanoate, propionate, ?-butyrolactone) to the culture medium enabled synthesis of PHA terpolymers, P(3HB/3HV/4HB) and P(3HB/ 3HV/3HHx), with different composition and different molar fractions of 3HB, 3HV, 4HB, and 3HHx. Different types of PHA terpolymers synthesized by C. eutrophus B-10646 were used to prepare films, whose physicochemical and physical-mechanical properties were investigated. The properties of PHA terpolymers were significantly different from those of the P3HB homopolymer: they had much lower degrees of crystallinity and lower melting points and thermal decomposition temperatures, with the difference between these temperatures remaining practically unchanged. Films prepared from all PHA terpolymers had higher mechanical strength and elasticity than P3HB films. In spite of dissimilar surface structures, all films prepared from PHA terpolymers facilitated attachment and proliferation of mouse fibroblast NIH 3T3 cells more effectively than polystyrene and the highly crystalline P3HB. Copyright: © 2014 Volova et al.

Scopus
Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Science, Moscow, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.; Kiselev, E.; Vinogradova, O.; Nikolaeva, E.; Chistyakov, A.; Sukovatiy, A.; Shishatskaya, E.

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All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

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Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
Свободных экз. нет
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An elementary multistage discrete model of soil organic matter transformations with a continuous scale of stability / S. I. Bartsev, A. A. Pochekutov // Ecol. Model. - 2019. - Vol. 393. - P61-65, DOI 10.1016/j.ecolmodel.2018.12.012 . - ISSN 0304-3800
Кл.слова (ненормированные):
Kinetics of soil organic matter transformations -- Model of soil organic matter transformations -- Soil organic matter -- Biogeochemistry -- Biological materials -- Decay (organic) -- Organic compounds -- Soils -- Continuous scale -- Discrete modeling -- Elementary model -- Law of mass action -- Multistage process -- Realistic model -- Soil organic matters -- Transformation process -- Mathematical transformations -- biotransformation -- chemical alteration -- decomposition -- numerical model -- reaction kinetics -- soil organic matter
Аннотация: The proposed elementary mathematical model of formation and decomposition of soil organic matter (SOM) is based on using equations of chemical kinetics to describe the multistage process of SOM transformation. The model both describes each step of transformation in accordance with the law of mass action and postulates the trend of increasing stability of the matter towards further transformation, which is common for all steps. Analysis of the model demonstrates that it is extremely difficult to construct a realistic model of SOM dynamics by assembling elementary models of the type presented in this study into the full description of SOM transformation processes. © 2018 Elsevier B.V.

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

Доп.точки доступа:
Bartsev, S. I.; Pochekutov, A. A.

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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. C. Xu, T. J. Wang, G. F. Liu [et al.] // Sens. Actuator B-Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991. - Cited References:66. - We are grateful for financial support from the Taishan Scholars Program of Shandong Province (tsqn201812104), the Qingchuang Science and Technology Plan of Shandong Province (2019KJJ017 and 2020KJC004), the National Natural Science Foundation of China (61671107, 62071085, 11704059, and 31802309), and the Youth Innovation Team Lead-Education Project of Shandong Educational Committee. . - ISSN 0925-4005

РУБ Chemistry, Analytical + Electrochemistry + Instruments & Instrumentation
Рубрики:
LABEL-FREE DETECTION
CHEMICAL-VAPOR-DEPOSITION
DNA HYBRIDIZATION
Кл.слова (ненормированные):
Single-crystal graphene -- FET -- Binding kinetics -- LMW drugs -- Imatinib
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 mu M range. This graphene-based FET biosensor (G-FET) was also applied toquantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs.

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Держатели документа:
Dezhou Univ, Inst Biophys, Shandong Key Lab Biophys, Dezhou 253023, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Shandong Normal Univ, Collaborat Innovat Ctr Light Manipulat & Applicat, Jinan 250358, Peoples R China.

Доп.точки доступа:
Xu, Shicai; Wang, Tiejun; Liu, Guofeng; Cao, Zanxia; Frank, Ludmila A.; Jiang, Shouzhen; Zhang, Chao; Li, Zhenhua; Krasitskaya, Vasilisa V.; Li, Qiang; Sha, Yujie; Zhang, Xiumei; Liu, Huilan; Wang, Jihua; Taishan Scholars Program of Shandong Province [tsqn201812104]; Qingchuang Science and Technology Plan of Shandong Province [2019KJJ017, 2020KJC004]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [61671107, 62071085, 11704059, 31802309]; Youth Innovation Team Lead-Education Project of Shandong Educational Committee

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Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor / S. Xu, T. Wang, G. Liu [et al.] // Sens Actuators, B Chem. - 2021. - Vol. 326. - Ст. 128991, DOI 10.1016/j.snb.2020.128991 . - ISSN 0925-4005
Кл.слова (ненормированные):
Binding kinetics -- FET -- Imatinib -- LMW drugs -- Single-crystal graphene -- Biosensors -- Biosynthesis -- Drug interactions -- Graphene -- Graphene transistors -- Proteins -- Single crystals -- Graphene field-effect transistors -- Graphene sheets -- Interaction kinetics -- Linear response -- Low molecular weight drugs -- Real time -- Small-molecule drugs -- Target proteins -- Field effect transistors
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 ?M range. This graphene-based FET biosensor (G-FET) was also applied to quantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs. © 2020 Elsevier B.V.

Scopus
Держатели документа:
Shandong Key Laboratory of Biophysics, Institute of Biophysics, Dezhou University, Dezhou, 253023, China
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Collaborative Innovation Center of Light Manipulations and Applications, Shandong Normal University, Jinan, 250358, China

Доп.точки доступа:
Xu, S.; Wang, T.; Liu, G.; Cao, Z.; Frank, L. A.; Jiang, S.; Zhang, C.; Li, Z.; Krasitskaya, V. V.; Li, Q.; Sha, Y.; Zhang, X.; Liu, H.; Wang, J.

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Assessment of 241Am accumulation rate by samples of algobacterial community of the Yenisei River. / A. Y. Bolsunovsky, T. A. Zotina, S. V. Kosinenko // Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections / translated from Russian. - 2002. - Vol. 385. - P374-376 . - ISSN 0012-4966
Кл.слова (ненормированные):
americium -- fresh water -- alga -- animal -- article -- bacterium -- kinetics -- metabolism -- nuclear reactor -- phytoplankton -- Russian Federation -- Algae -- Americium -- Animals -- Bacteria -- Fresh Water -- Kinetics -- Nuclear Reactors -- Phytoplankton -- Russia

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

Доп.точки доступа:
Bolsunovsky, A.Y.; Zotina, T.A.; Kosinenko, S.V.

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ATP is a cosubstrate of the luciferase of the earthworm Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar', V. N. Petushkov // Doklady Biochemistry and Biophysics. - 2003. - Vol. 392, Is. 1-6. - P253-255, DOI 10.1023/A:1026134628735 . - ISSN 1607-6729
Кл.слова (ненормированные):
adenosine diphosphate -- adenosine phosphate -- adenosine triphosphate -- luciferase -- luciferin -- magnesium -- animal cell -- article -- controlled study -- earthworm -- hydrolysis -- luminescence -- nonhuman -- Adenosine Diphosphate -- Adenosine Triphosphate -- Animals -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Magnesium -- Oligochaeta -- Substrate Specificity -- Animalia -- Annelida -- Clitellata -- Enchytraeidae -- Pheretima sieboldi

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:
Rodionova, N.S.; Bondar', V.S.; Petushkov, V.N.

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Biochemical changes causes lack of bioluminescence in fruiting bodies of Armillaria / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2017. - Vol. 8, Is. 1. - P9-17, DOI 10.5943/mycosphere/8/1/2 . - ISSN 2077-7000
Кл.слова (ненормированные):
Enzymes and substrate of luminescent reaction -- Kinetics of luminescence -- Luminous mycelia -- Nonluminous fruiting bodies of fungus
Аннотация: Mycelium of Armillaria species exhibit bioluminescence in nature and when cultivated on artificial nutrient media. However, fruiting bodies do not emit visible light. The present study investigates biochemical changes which cause this phenomenon. Light emission was studied in experiments with mixtures of cold and hot extracts of the luminous mycelium of Armillaria borealis IBSO 2328 and nonluminous fruiting bodies of this fungus and an unidentified species of the genus (Armillaria sp.). Hot extracts of fruiting bodies of the nonluminous Pholiota squarrosa were used as the substrate analog of the luminescent reaction, as previously this fungus had been found to contain a high amount of this substance. Control experiments showed that cold extracts of A. borealis IBSO 2328 mycelium contained enzymes for the luminescent reaction, which is initiated after addition hot extracts of P. squarrosa fruiting bodies. Parallel experiments with extracts of the fruiting bodies of Armillaria showed that: (i) - cold extracts did not contain enzymes of the luminescent reaction or contain very small amounts of these enzymes and (ii) - hot extracts did not contain substrate of the luminescent reaction. Thus, the reason why fruiting bodies of Armillaria do not emit light is that they do not contain components required for visible luminescence. The study discusses possible causes why the enzymes and substrate of the luminescent reaction are not synthesized in fruiting bodies of Armillaria. © Guizhou Academy of Agricultural Sciences.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Akademgorodok, Krasnoyarsk, Russian Federation

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

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10.

Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobio1.2017.07.021. - Cited References:54. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 03562016-0712 and 0356-2015-0103) and the RFBR grant 17-04-00764. . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
SEQUENCE-ANALYSIS
   APO-OBELIN
   INTRINSIC FLUORESCENCE
   COELENTERAZINE
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Coelenteramide -- Cysteine -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or p-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coil, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild -type aequorin. In contrast, Cys-free obelin retains only 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a "fast" component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 0.2 and 44.6 0.4 C for aequorin and Cys-free aequorin, and 49.1 0.1 and 28.8 0.3 C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield.

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Держатели документа:
RAS, Photobiol Lab, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,SB, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Academy of Sciences [03562016-0712, 0356-2015-0103]; RFBR [17-04-00764]

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11.

Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobiol.2017.07.021 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenteramide -- Coelenterazine -- Cysteine -- Photoprotein -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or ?-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coli, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. In contrast, Cys-free obelin retains only ~ 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a “fast” component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 ± 0.2 and 44.6 ± 0.4 °C for aequorin and Cys-free aequorin, and 49.1 ± 0.1 and 28.8 ± 0.3 °C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield. © 2017 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Eremeeva, E. V.; Vysotski, E. S.

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12.

Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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13.

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory

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14.

Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

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15.

Biophysical aspects of the biosphere impact on global climate. / D. A. Semenov, R. G. Khlebopros // Doklady. Biochemistry and biophysics. - 2002. - Vol. 387. - P338-339 . - ISSN 1607-6729
Кл.слова (ненормированные):
carbon monoxide -- article -- atmosphere -- biophysics -- chemistry -- climate -- greenhouse effect -- kinetics -- temperature -- theoretical model -- Atmosphere -- Biophysics -- Carbon Monoxide -- Climate -- Greenhouse Effect -- Kinetics -- Models, Theoretical -- Temperature

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

Доп.точки доступа:
Semenov, D.A.; Khlebopros, R.G.

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16.

Ca(2+)-activator of the luminescence system of the earthworms Henlea sp., (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar, V. N. Petushkov // Doklady. Biochemistry and biophysics. - 2002. - Vol. 386. - P260-263 . - ISSN 1607-6729
Кл.слова (ненормированные):
calcium -- divalent cation -- edetic acid -- luciferase -- luciferin -- metal -- animal -- annelid worm -- article -- chemistry -- dose response -- enzymology -- genetics -- kinetics -- luminescence -- metabolism -- Animals -- Calcium -- Cations, Divalent -- Dose-Response Relationship, Drug -- Edetic Acid -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Metals -- Oligochaeta

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

Доп.точки доступа:
Rodionova, N.S.; Bondar, V.S.; Petushkov, V.N.

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17.

Characterization of polymeric microparticles based on resorbable polyesters of oxyalkanoic acids as a platform for deposition and delivery of drugs / A. V. Goreva [et al.] // Polym. Sci. Ser. A. - 2012. - Vol. 54, Is. 2. - P94-105, DOI 10.1134/S0965545X12020022. - Cited References: 33. - This work was supported by the program for Support of Leading Scientific Schools of the Russian Federation (project no. 11.G34.31.0013.2010, Biotechnology of New Biomaterials) and the program of integrated studies of the Presidium of the Siberian Branch, Russian Academy of Sciences (project no. 93). . - 12. - ISSN 0965-545X

РУБ Polymer Science
Рубрики:
IN-VITRO RELEASE
   POLYHYDROXYBUTYRATE MICROSPHERES
   BLENDS
   RIFAMPICIN
   BIOCOMPATIBILITY
   DEGRADATION
   FORMULATION
   COMPOSITE
   CARRIERS
   MODEL
Аннотация: The effect of the preparation technique (chemical composition of a polymer, type and method of emulsion mixing, and molecular mass of a drug) on the yield, structure, and size of microparticles obtained from resorbable polyesters of microbiological origin, polyhydroxyalkanoates, is studied. It is found that the concentration of the polymer solution and the method of emulsion mixing are the most significant factors affecting the diameter of microparticles based on polyhydroxyalkanoates; the surface structure of particles depends to a higher extent on the chemical composition of the polymer. The family of microparticles from 100-200 nm to 50-70 mu m in diameter is synthesized. It is shown that the rate of drug release from microparticles in vitro into the medium is higher in the case of 3-hydroxybutyrate copolymers with 3-hydroxyvalerate than in the case of the homopolymer of 3-hydroxybutyrate. This parameter increases with the content of 3-hydroxyvalerate units in the copolymer and the porosity and mass fraction of the drug in particles with a decrease in their sizes. For in vitro systems containing a phosphate buffer, variation in the preparation parameters makes it possible to obtain microparticles with various characteristics suitable for deposition of drugs. For microparticles obtained from polyhydroxyalkanoates and having different diameters, the mathematical description of the kinetics of drug release from the polymer matrix is provided.

Держатели документа:
[Goreva, A. V.
Shishatskaya, E. I.
Volova, T. G.] Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
[Shishatskaya, E. I.
Volova, T. G.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
[Goreva, A. V.
Sinskey, A. J.] MIT, Cambridge, MA 02139 USA : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Goreva, A.V.; Shishatskaya, E.I.; Volova, T.G.; Sinskey, A.J.

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18.

CHEMILUMINESCENT ANALYSIS OF THE KINETICS OF REACTIVE OXYGEN SPECIES GENERATION BY WHOLE-BLOOD CELLS UNDER COMPENSATIVE EXFUSIONS [Текст] / K. I. PUKHOV [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1991. - Vol. 316, Is. 1. - P. 247-251. - Cited References: 11 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences
Рубрики:
HYDROGEN-PEROXIDE
NEUTROPHIL

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

Доп.точки доступа:
PUKHOV, K.I.; MAKARSKAYA, G.V.; YAKHNINA, Y.I.; PUKHOVA, Y.I.

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19.

Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase [Text] / M. S. Titushin [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 2. - P189-196, DOI 10.1039/b713109g. - Cited References: 41 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
CRYSTAL-STRUCTURE
   LIGHT-EMISSION
   CA2+-REGULATED PHOTOPROTEINS
   BIOLUMINESCENT REPORTER
   RENIFORMIS LUCIFERASE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   ENERGY-TRANSFER
   EXCITED-STATE
   CALCIUM
Аннотация: The Renilla bioluminescent system in vivo is comprised of three proteins-the luciferase, green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called luciferin-binding protein (LBP). This work reports the cloning of the full-size cDNA encoding CBP from soft coral Renilla muelleri, its overexpression and properties of the recombinant protein. The apo-CBP was quantitatively converted to CBP by simple incubation with coelenterazine. The physicochemical properties of this recombinant CBP are determined to be practically the same as those reported for the CBP (LBP) of R. reniformis. CBP is a member of the four-EF-hand Ca2+-binding superfamily of proteins with only three of the EF-hand loops having the Ca2+-binding consensus sequences. There is weak sequence homology with the Ca2+-regulated photoproteins but only as a result of the necessary Ca2+-binding loop structure. In combination with Renilla luciferase, addition of only one Ca2+ is sufficient to release the coelenterazine as a substrate for the luciferase for bioluminescence. This combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone as the substrate for luciferase. This increased quantum yield, a difference of bioluminescence spectra, and markedly different kinetics, implicate that a CBP-luciferase complex might be involved.

Держатели документа:
[Titushin, Maxim S.
Markova, Svetlana V.
Frank, Ludmila A.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Lee, John
Vysotski, Eugene S.] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Markova, S.V.; Frank, L.A.; Malikova, N.P.; Stepanyuk, G.A.; Lee, J...; Vysotski, E.S.

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20.

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.

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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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