Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

в найденном

Найдено в других БД:

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (1)

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=luciferase<.>)

Общее количество найденных документов : 185
Показаны документы с 1 по 20

1-20 21-40 41-60 61-80 81-100 101-120

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PETUSHKOV V.N., KRATASYUK G.A., RODIONOVA N.S., FISH A.M., BELOBROV P.I.
Заглавие : 2-ENZYME NADH-FMN-OXIDOREDUCTASE-LUCIFERASE SYSTEM FROM LUMINESCENT BACTERIA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1984. - Vol. 49, Is. 4. - С. 593-603. - 11. - ISSN 0006-2979
Примечания : Cited References: 24
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V.A., Egorova O.I., Esimbekova E.N., Kudryashova N.S., Orlova N.Y., L'vova L.S.
Заглавие : A biological luciferase test for the bioluminescent assay of wheat grain infection with Fusarium
Колич.характеристики :3 с
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA, 1998. - Vol. 34, Is. 6. - P622-624. - ISSN 0003-6838
Примечания : Cited References: 7
Аннотация: The extent of inhibition of the bioluminescence reaction by wheat grain extracts was studied as a function of the scabby kernel content in wheat. The NADH : flavine mononucleotide oxidoreductase-luciferase bienzyme bioluminescence system was found to be the most sensitive to mycotoxins produced by fungi of the genus Fusarium. A biological luciferase test was developed for monitoring wheat grain infection with Fusarium.
WOS
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : KRATASYUK V.A., ABAKUMOVA V.V., KIM N.B.
Заглавие : A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1994. - Vol. 59, Is. 7. - P761-765. - ISSN 0006-2979
Примечания : Cited References: 11
Предметные рубрики: BIOLUMINESCENT
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--nadh, fmn-oxidoreductase--immobilization
Аннотация: A gel model for the functioning of luciferase in cells has been constructed using bacterial NADH:FMN-oxidoreductase and luciferase immobilized in starch gel disks. The characteristics of the immobilized luciferase depend on the duration of drying, the amount and concentration of the gel, the nature of the support used for drying, and the properties of the initial enzyme preparation. Functionally important enzyme groups remain intact in the immobilized preparation, and luciferase retains its high specificity with respect to aldehydes. The gel microenvironment appears to be optimal for luciferase, judging from its high activity and increased stability. Conditions allowing repeated use of the preparation have been found. The approach permits co-immobilization of luciferase with other enzymes and their substrates. The error in bioluminescence measurements using the disks is 5-10%. A procedure for stabilization of the immobilized luciferase during repeated use has been devised.
WOS
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk, Valentina A., Stepanova, Lyudmila, V, Ranjan, Rajeev, Sutormin, Oleg S., Pande, Shubhra, Zhukova, Galina, V, Miller, Olga M., Maznyak, Natalya, V, Kolenchukova, Oksana A.
Заглавие : A noninvasive and qualitative bioluminescent assay for express diagnostics of athletes' responses to physical exertion
Колич.характеристики :7 с
Коллективы : Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; Krasnoyarsk Regional Foundation of Science [KF-537]
Место публикации : Luminescence: WILEY, 2020. - Article in press. - ISSN 1522-7235, DOI 10.1002/bio.3954. - ISSN 1522-7243(eISSN)
Примечания : Cited References:33. - The Ministry of Science and Higher Education of the Russian Federation, Grant/Award Number: FSRZ-2020-0006; Krasnoyarsk Regional Foundation of Science, Grant/Award Number: KF-537
Предметные рубрики: SALIVARY BIOMARKERS
EXERCISE
Аннотация: Upcoming professional sports authorities seek rapid noninvasive biosensing tools for regular monitoring of athletes' physiological states. The analysis of saliva through luminescence-based biosensors has been perceived as a suitable candidate for such purposes. The present study reports a qualitative bioluminescence assay based on a coupled enzyme system that consists of bacterial luciferase (BLuc) and nicotinamide adenine dinucleotide (NADH):flavin mononucleotide (FMN) oxidoreductase (Red), BLuc-Red, for the express diagnostics of athletes' stress levels before and after physical exertion. The volunteers who participated in the study were grouped as freestyle wrestlers and students who adapted to different levels of physical activities. Under physical exertion modelling conditions, the influence of participant saliva on BLuc-Red catalyzed light emission was investigated. Results showed a significant increase in residual luminescence (I-exp, mean maximum bioluminescence intensity of the experimental measurement (I-exp); I-c, luminescence intensity in control; I-exp/I-c, %) values for participants in the wrestler group while a decrease in the student group (P 0.05). Such contrasting residual luminescence values in both groups were found to be dependent on the catalase activity of saliva. The proposed bioluminescence assay can be utilized as a potential nonspecific biosensing tool for determining the physical state of athletes under high loads.
WOS
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): coelenterazine--2-hydroperoxy-coelenterazine--obelia longissima--renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev A. N., Burakova L. P., Barinova K. A., Frank L. A.
Заглавие : A test system for tick-borne encephalitis virus detection based on bioluminescent immunoassay
Место публикации : J. Sib. Fed. Univ. - Biol.: Siberian Federal University, 2020. - Vol. 13, Is. 3. - С. 310-321. - ISSN 19971389 (ISSN), DOI 10.17516/1997-1389-0296
Аннотация: The tick-borne encephalitis virus (TBEV) is the causative agent of one of the most severe human neuroinfections. The infection transmitted by ixodid ticks is spread throughout the forest and forest-steppe zones of the temperate climatic belt of the Eurasian continent, including the Siberian region of the Russian Federation. Despite the availability of commercial analytical systems for the detection of TBEV, the task of developing approaches to a quick and reliable analysis that can be performed routinely, particularly in environmental studies, remains topical. A solid-phase bioluminescent immunoassay for determining the tick-borne encephalitis virus (TBEV) in ticks was developed. The assay is based on the hybrid protein consisting of a modified thermostable version of Renilla muelleri luciferase and a single-chain mini-antibody to protein E. This unique protein had been obtained and investigated by the authors earlier. The current study describes the expression of the hybrid protein in two different strains of recombinant E. coli cells. The optimal conditions for obtaining a highly purified protein were found. The bioluminescent reaction of the luciferase domain was triggered with the help of the stable natural form of the substrate, a Ca-dependent coelenterazine-binding protein, the recombinant variant of which was obtained by the authors. The conditions for production and storage of the immunoassay components (the hybrid protein, the stable form of the luciferase substrate, and activated microplates) were determined. Using the developed test system, more than 900 tick samples were analyzed for TBEV. In terms of sensitivity (89.5%) and specificity (98.9%), the proposed method is not inferior to colorimetric detection and is much simpler and faster than the latter. © Siberian Federal University. All rights reserved.
Scopus
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko, Kirill A., Belousov, Kirill I., Denisov, Ivan A., Yakimov, Anton S., Esimbekova, Elena N., Bukatin, Anton S., Evstrapov, Anatoly A., Belobrov, Peter I.
Заглавие : Active mixing of immobilised enzymatic system in microfluidic chip
Колич.характеристики :5 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Micro Nano Lett.: INST ENGINEERING TECHNOLOGY-IET, 2017. - Vol. 12, Is. 6. - С. 377-381. - ISSN 1750-0443, DOI 10.1049/mnl.2016.0646
Примечания : Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041).
Предметные рубрики: POLY(METHYL METHACRYLATE)
SURFACE MODIFICATION
POINT
DEVICES
PMMA
Аннотация: Parameters for sample introduction, dried reagents dissolution and mixing with sample for bienzyme system NAD(H):FMN-oxidoreductase and luciferase immobilised in microfluidic chip were successfully determined. Numerical simulations of reaction chamber geometry, flavin mononucleotide (FMN) escape from starch gel and mixing options were conducted to achieve higher sensitivity of bioluminescent reaction. Results of numerical simulations were verified experimentally. The active mixer for dried reagents was made from an electro-mechanical speaker's membrane which was connected to the input of the chip. Such a mixer provided better efficiency than a passive mixing, and it is simple enough for use in point-of-care devices with any systems based on immobilised enzymes in chips.
WOS,
Смотреть статью,
Scopus
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lukyanenko K. A., Denisov I. A., Yakimov A. S., Esimbekova E. N., Belousov K. I., Bukatin A. S., Kukhtevich I. V., Sorokin V. V., Evstrapov A. A., Belobrov P. I.
Заглавие : Analytical Enzymatic Reactions in Microfluidic Chips
Колич.характеристики :6 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2017. - Vol. 53, Is. 7. - С. 775-780. - ISSN 0003-6838, DOI 10.1134/S0003683817070043. - ISSN 1573-8183(eISSN)
Примечания : Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041).
Предметные рубрики: BIOAVAILABLE HEAVY-METALS
DEVICES
POINT
LAB
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--microfluidics--microfluidic chip--enzymatic--bioassay
Аннотация: A number of approaches have been proposed and tested to transfer enzymatic reactions into the functional elements of microfluidic chips on the example of the bienzyme bioluminescent reaction involving NAD(P)H:FMN-oxidoreductase and luciferase. Measurement of the catalytic activity of these enzymes (under the influence of pollutants) is the basis of enzymatic bioassay of various liquids. It was found that all of the components of the reaction must be placed in the same cell of the chip to improve the reproducibility of the measurements. The use of starch gel as a carrier for immobilization and gelatin as a scaffold in the reactor of the chip enables the preservation of enzyme activity in the course of sealing the chip at room temperature. It is shown that the components of the reaction should be vigorously stirred in a microfluidic chip reactor to improve the efficiency of the analysis. As a result of the studies, a prototype of microfluidic chip based on the enzymatic bioluminescent reaction is proposed. It is characterized by a detection limit of copper sulfate of 3 mu M that corresponds to the sensitivity of traditional lux-biosensors based on living cells. The analysis time is reduced to 1 min, and the analysis can be performed by individuals without special laboratory skills.
WOS,
Смотреть статью,
Scopus
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tarasova A.S., Stom D.I., Kudryasheva N.S.
Заглавие : Antioxidant activity of humic substances via bioluminescent monitoring in vitro
Колич.характеристики :8 с
Коллективы : Russian Foundation for Basic Research [15-03-06786a], Russian Academy of Sciences [VI 57.1.1]
Место публикации : Environ. Monit. Assess.: SPRINGER, 2015. - Vol. 187, Is. 3. - Ст.89. - ISSN 0167-6369, DOI 10.1007/s10661-015-4304-1. - ISSN 1573-2959(eISSN)
Примечания : Cited References:51. - This work was supported by the Russian Foundation for Basic Research, Grant No. 15-03-06786a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1.
Предметные рубрики: DETOXIFICATION PROCESSES
TOXICITY
BIOASSAYS
BACTERIA
ASSAY
Ключевые слова (''Своб.индексиров.''): antioxidant activity--oxidative toxicity--general toxicity--humic--substances--bioassay--bioluminescence
Аннотация: This work considers antioxidant properties of natural detoxifying agents-humic substances (HS) in solutions of model inorganic and organic compounds of oxidative nature-complex salt K-3[Fe(CN)(6)] and 1,4-benzoquinone. Bioluminescent system of coupled enzymatic reactions catalyzed by NAD(P) H:FMN-oxidoreductase and bacterial luciferase was used as a bioassay in vitro to monitor toxicity of the oxidizer solutions. Toxicities of general and oxidative types were evaluated using bioluminescent kinetic parameters-bioluminescence intensity and induction period, respectively. Antioxidant activity of HS was attributed to their ability to decrease both general and oxidative toxicities; the HS antioxidant efficiency was characterized with detoxification coefficients D-GT and D-OxT, respectively. Dependencies of D-GT and D-OxT on HS concentration and time of preliminary incubation of the oxidizers with HS were demonstrated. The optimal conditions for detoxification of the oxidizers were 20-min incubation time and 0.5x10(-4) to 2x10(-4) M of HS concentration. The present study promotes application of the enzymatic luminescent bioassay to monitor toxicity of pollutants of oxidative nature in environmental and waste waters in remediation procedures.
WOS
Найти похожие

10.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Frank, Ludmila A., Krasitskaya, Vasilisa V.
Заглавие : Application of Enzyme Bioluminescence for Medical Diagnostics
Колич.характеристики :23 с
Место публикации : Adv. Biochem. Eng. Biotechnol.: SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - С. 175-197. - (Advances in Biochemical Engineering-Biotechnology). - , DOI 10.1007/978-3-662-43385-0_6
Примечания : Cited References:63
Предметные рубрики: RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-regulated photoprotein--diagnostics--immunoassay--luciferase--nucleic acid hybridization assay
Аннотация: Nowadays luciferases are effectively used as analytical instruments in a great variety of research fields. Of special interest are the studies dealing with elaboration of novel analytical systems for the purposes of medical diagnostics. The ever-expanding spectrum of clinically important analytes accounts for the increasing demand for new techniques for their detection. In this chapter we have made an attempt to summarize the results on applications of luciferases as reporters in binding assays including immunoassay, nucleic acid hybridization assay, and so on. The data over the last 15 years have been analyzed and clearly show that luciferase-based assays, due to extremely high sensitivity, low cost, and the lack of need for skilled personnel, hold much promise for clinical diagnostics.
WOS
Найти похожие

11.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Esimbekova, Elena, Kratasyuk, Valentina, Shimomura, Osamu
Заглавие : Application of Enzyme Bioluminescence in Ecology
Колич.характеристики :43 с
Место публикации : Adv. Biochem. Eng. Biotechnol.: SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - С. 67-109. - (Advances in Biochemical Engineering-Biotechnology). - , DOI 10.1007/978-3-662-43385-0_3
Примечания : Cited References:85
Предметные рубрики: BACTERIAL LUCIFERASE
IN-VITRO
PYRETHROID INSECTICIDES
FRESH-WATER
Ключевые слова (''Своб.индексиров.''): bioluminescence--ecological monitoring--enzymatic assay--immobilization--integral water toxicity--luciferase
Аннотация: This review examines the general principles of bioluminescent enzymatic toxicity bioassays and describes the applications of these methods and the implementation in commercial biosensors. Bioluminescent enzyme system technology (BEST) has been proposed in the bacterial coupled enzyme system, wherein NADH: FMN-oxidoreductase-luciferase substitutes for living organisms. BEST was introduced to facilitate and accelerate the development of cost-competitive enzymatic systems for use in biosensors for medical, environmental, and industrial applications. For widespread use of BEST, the multicomponent reagent "Enzymolum'' has been developed, which contains the bacterial luciferase, NADH: FMN-oxidoreductase, and their substrates, co-immobilized in starch or gelatin gel. Enzymolum is the central part of Portable Laboratory for Toxicity Detection (PLTD), which consists of a biodetector module, a sampling module, a sample preparation module, and a reagent module. PLTD instantly signals chemical-biological hazards and allows us to detect a wide range of toxic substances. Enzymolum can be integrated as a biological module into the portable biodetector-biosensor originally constructed for personal use. Based on the example of Enzymolum and the algorithm for creating new enzyme biotests with tailored characteristics, a new approach was demonstrated in biotechnological design and construction. The examples of biotechnological design of various bioluminescent methods for ecological monitoring were provided. Possible applications of enzyme bioassays are seen in the examples for medical diagnostics, assessment of the effect of physical load on sportsmen, analysis of food additives, and in practical courses for higher educational institutions and schools. The advantages of enzymatic assays are their rapidity (the period of time required does not exceed 3-5 min), high sensitivity, simplicity and safety of procedure, and possibility of automation of ecological monitoring; the required luminometer is easily available.
WOS
Найти похожие

12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk, Valentina A., Esimbekova, Elena N.
Заглавие : Applications of Luminous Bacteria Enzymes in Toxicology
Колич.характеристики :8 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Comb. Chem. High Throughput Screen: BENTHAM SCIENCE PUBL LTD, 2015. - Vol. 18, Is. 10. - С. 952-959. - ISSN 1386-2073, DOI 10.2174/1386207318666150917100257. - ISSN 1875-5402(eISSN)
Примечания : Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041.
Предметные рубрики: NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Ключевые слова (''Своб.индексиров.''): bioluminescence--bioluminescent toxicity enzymatic assay--immobilization--of enzymes--luciferase--total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH: FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure.
WOS
Найти похожие

13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V. A., Esimbekova E. N.
Заглавие : Applications of luminous bacteria enzymes in toxicology
Место публикации : Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - С. 952-959. - ISSN 13862073 (ISSN)
Ключевые слова (''Своб.индексиров.''): bioluminescence--bioluminescent toxicity enzymatic assay--immobilization of enzymes--luciferase--total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.
Scopus
Найти похожие

14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondar' V.S., Pozdnyakova I.O., Puzyr' A.P.
Заглавие : Applications of nanodiamonds for separation and purification of proteins
Колич.характеристики :3 с
Место публикации : Phys. Solid State: AMER INST PHYSICS, 2004. - Vol. 46, Is. 4. - С. 758-760. - ISSN 1063-7834, DOI 10.1134/1.1711468
Примечания : Cited References: 11
Предметные рубрики: ESCHERICHIA-COLI
OBELIN
Аннотация: Recombinant apoobelin and recombinant luciferase are separated from bacterial cells of Escherichia coli with the use of detonation nanodiamonds. The application of nanodiamonds has a number of points in its favor, namely, (i) simplifies the procedures for purifying the proteins, (ii) decreases the time of their separation to 30-40 min, (iii) eliminates the necessity of using special chromatographic equipment, and (iv) makes it possible to prepare high-purity apoobelin and luciferase materials with protein yields of 35-45 and 45-60%, respectively. The possible mechanisms of interaction of protein molecules and nanodiamond particles are analyzed. (C) 2004 MAIK "Nauka / Interperiodica".
Найти похожие

15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodionova N.S., Bondar' V.S., Petushkov V.N.
Заглавие : ATP is a cosubstrate of the luciferase of the earthworm Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae)
Место публикации : Doklady Biochemistry and Biophysics. - 2003. - Vol. 392, Is. 1-6. - С. 253-255. - ISSN 16076729 (ISSN) , DOI 10.1023/A:1026134628735
Ключевые слова (''Своб.индексиров.''): 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
Найти похожие

16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva, Elena, V, Gulnov, Dmitry, V, Gerasimova, Marina A., Sukovatyi, Lev A., Burakova, Ludmila P., Karuzina, Natalya E., Melnik, Bogdan S., Kratasyuk, Valentina A.
Заглавие : Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy
Колич.характеристики :17 с
Коллективы : 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)
Место публикации : Int. J. Mol. Sci.: MDPI, 2021. - Vol. 22, Is. 19. - Ст.10449. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms221910449
Примечания : 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).
Предметные рубрики: TRYPTOPHAN FLUORESCENCE
CRYSTAL-STRUCTURE
SUBUNIT
BIOLUMINESCENCE
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./p
WOS
Найти похожие

17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva E. V., Gulnov D. V., Gerasimova M. A., Sukovatyi L. A., Burakova L. P., Karuzina N. E., Melnik B. S., Kratasyuk V. A.
Заглавие : Bacterial luciferases from vibrio harveyi and photobacterium leiognathi demonstrate different conformational stability as detected by time-resolved fluorescence spectroscopy
Место публикации : Int. J. Mol. Sci.: MDPI, 2021. - Vol. 22, Is. 19. - Ст.10449. - ISSN 16616596 (ISSN), DOI 10.3390/ijms221910449
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
Найти похожие

18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryasheva N..., Vetrova E..., Kuznetsov A..., Kratasyuk V..., Stom D...
Заглавие : Bioluminescence assays: Effects of quinones and phenols
Колич.характеристики :5 с
Место публикации : Ecotox. Environ. Safe.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2002. - Vol. 53, Is. 2. - P221-225. - ISSN 0147-6513, DOI 10.1006/eesa.2002.2214
Примечания : Cited References: 18
Ключевые слова (''Своб.индексиров.''): bioluminescence assays--quinones--phenols
Аннотация: The influence of a series of quinones and phenols on bacterial bioluminescence systems was investigated. Three bioluminescence systems used in ecological monitoring were compared: (1) water-soluble; (2) immobilized in starch gel coupled enzyme systems: NADH:FMN-oxidoreductase-luciferase; (3) luminescent bacteria. Bioluminescence inhibition constants of quinones and phenols and bioluminescence induction periods were compared. These kinetic parameters are proportional to quinone concentrations and depend on the quinone redox potential. Different effects of the substances are related to structure and properties of the bioluminescence systems. The set of bioluminescence assays for quinones and phenols monitoring should include two bioluminescence systems: 1 (or 2) and 3. (C) 2002 Elsevier Science (USA).
WOS
Найти похожие

19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kotlobay, Alexey A., Dubinnyi, Maxim A., Purtov, Konstantin V., Guglya, Elena B., Rodionova, Natalja S., Petushkov, Valentin N., Bolt, Yaroslav V., Kublitski, Vadim S., Kaskova, Zinaida M., Ziganshin, Rustam H., Nelyubina, Yulia V., Dorovatovskii, Pavel V., Eliseev, Igor E., Branchini, Bruce R., Bourenkov, Gleb, Ivanov, Igor A., Oba, Yuichi, Yampolsky, Ilia V., Tsarkova, Aleksandra S.
Заглавие : Bioluminescence chemistry of fireworm Odontosyllis
Колич.характеристики :6 с
Коллективы : Russian Science FoundationRussian Science Foundation (RSF) [18-74-10102, 16-14-00052p]; Air Force Office of Scientific ResearchUnited States Department of DefenseAir Force Office of Scientific Research (AFOSR) [FA9550-18-1-0017]
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2019. - Vol. 116, Is. 38. - С. 18911-18916. - ISSN 0027-8424, DOI 10.1073/pnas.1902095116
Примечания : Cited References:16. - We thank the late Dr. Shoji Inoue and Dr. Hisae Kakoi (Meijo University) for providing Odontosyllis materials, Sergey Shakhov for photography, and Drs. Mikhail Baranov and Andrey Mikhaylov for discussions. Some experiments were carried out using equipment provided by the Institute of Bioorganic Chemistry of the Russian Academy of Sciences.ore Facility. Some experiments were supported by Planta LLC. Structural and mechanistic studies were supported by Russian Science Foundation Grant 18-74-10102. Isolation, purification, and biochemical studies were supported by Russian Science Foundation Grant 16-14-00052p. B.R.B. acknowledges support from the Air Force Office of Scientific Research (FA9550-18-1-0017).
Предметные рубрики: MECHANISM
DECARBOXYLATION
OXIDATION
Аннотация: Marine polychaetes Odontosyllis undecimdonta, commonly known as fireworms, emit bright blue-green bioluminescence. Until the recent identification of the Odontosyllis luciferase enzyme, little progress had been made toward characterizing the key components of this bioluminescence system. Here we present the biomolecular mechanisms of enzymatic (leading to light emission) and nonenzymatic (dark) oxidation pathways of newly described O. undecimdonta luciferin. Spectral studies, including 1D and 2D NMR spectroscopy, mass spectrometry, and X-ray diffraction, of isolated substances allowed us to characterize the luciferin as an unusual tricyclic sulfur-containing heterocycle. Odontosyllis luciferin does not share structural similarity with any other known luciferins. The structures of the Odontosyllis bioluminescent system's low molecular weight components have enabled us to propose chemical transformation pathways for the enzymatic and nonspecific oxidation of luciferin.
WOS,
Смотреть статью,
Scopus
Найти похожие

20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : KUDRYASHEVA N.S., KRATASYUK V.A., BELOBROV P.I.
Заглавие : BIOLUMINESCENT ANALYSIS - THE ACTION OF TOXICANTS - PHYSICAL-CHEMICAL REGULARITIES OF THE TOXICANTS EFFECTS
Место публикации : Anal. Lett.: MARCEL DEKKER INC, 1994. - Vol. 27, Is. 15. - С. 2931-2947. - 17. - ISSN 0003-2719
Примечания : Cited References: 13
Ключевые слова (''Своб.индексиров.''): bacterial luciferase biotest--foreign compounds--energy of electron excited states level--redox potential--reducing of bioluminescent intensity--induction period--time of maximum light intensity
Аннотация: The physical-chemical regularities of aromatic compounds' effects in luciferase to toxicity biotesting have been studied, The structures and physical-chemical characteristics of the toxicants and of the bioluminescent emitter were taken into account. The inhibition constants of bioluminescence intensity (I) were calculated and interpreted from the viewpoint of the energy (electron) transfer processes. The induction period (P) and the increase of the rime of the maximum light intensity (t(M)) which take place in the quinones presence, have been shown to deal with hydrogen transfer processes. The values of I, P and t(M) have been shown to be connected with a size of the quinones' aromatic and aliphatic parts, P- and t(M)-dependencies on quinone's redox potential have been demonstrated.
Найти похожие