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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V.A., Esimbekova E.N., Gladyshev M.I., Khromichek E.B., Kuznetsov A.M., Ivanova E.A.
Заглавие : The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems
Место публикации : Chemosphere. - 2001. - Vol. 42, Is. 8. - С. 909-915. - ISSN 00456535 (ISSN) , DOI 10.1016/S0045-6535(00)00177-6
Ключевые слова (''Своб.индексиров.''): alcohol dehydrogenase--bacterial luciferase--bioluminescence--blooming--pollution--trypsin--water toxicity--alcohol dehydrogenase--benzoquinone--luciferase--trypsin--aquatic ecosystem--bioluminescence--water quality--article--bacterium culture--bioluminescence--blue green alga--ecosystem--pond--seasonal variation--water pollution--water quality--benzoquinones--biological assay--cyanobacteria--ecosystem--environmental monitoring--eutrophication--fmn reductase--indicators and reagents--luminescent measurements--nadh, nadph oxidoreductases--water pollutants--russian federation--algae--bacteria (microorganisms)--chlorophyta--cyanobacteria--uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodionova N.S., Petushkov V.N., Belobrov P.I.
Заглавие : Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another
Место публикации : Biophysics. - 1988. - Vol. 33, Is. 3. - С. 424-430. - ISSN 00063509 (ISSN)
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarionov B.A., Protopopova M.V., Karginov V.A., Mertvetsov N.P., Gitelson J.I.
Заглавие : Nucleotide sequence of part of Photobacterium leiognathi lux region
Место публикации : Nucleic Acids Research. - 1988. - Vol. 16, Is. 20. - С. 9855. - ISSN 03051048 (ISSN) , DOI 10.1093/nar/16.20.9855
Ключевые слова (''Своб.индексиров.''): bacterial protein--luciferase--article--bacterial gene--genetics--molecular genetics--nucleotide sequence--photobacterium--bacterial proteins--base sequence--genes, bacterial--luciferase--molecular sequence data--photobacterium
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarrionov B.A., Blinov V.M., Douchenko A.P., Protopopova M.V., Karginov V.A., Mertvetsov N.P., Gitelson J.I.
Заглавие : Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes
Место публикации : Gene. - 1990. - Vol. 86, Is. 1. - С. 89-94. - ISSN 03781119 (ISSN)
Ключевые слова (''Своб.индексиров.''): bioluminescence--expression in e. coli--luciferase--molecular evolution--nucleotide sequence--protein alignment--recombinant dna--luciferase--amino acid sequence--article--bioluminescence--fungus--gene structure--genetic engineering--heredity--nonhuman--nucleotide sequence--priority journal--vibrionaceae--acyltransferases--amino acid sequence--bacterial proteins--base sequence--cloning, molecular--dna, bacterial--genes, structural, bacterial--luciferase--luminescence--molecular sequence data--operon--photobacterium--restriction mapping--escherichia coli--fungi--photobacterium leiognathi--vibrio harveyi--vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.
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Вид документа : Однотомное издание
Шифр издания : А.с. 973614!-349931
Автор(ы) : Высоцкий Е.С., Заворуев В.В., Межевикин В.В.
Заглавие : Питательная среда для культивирования светящихся бактерий .-
Выходные данные : Б.м.,Б.г.
Коллективы : Ин-т биофизики СО АН СССР
Цена : Б.ц.
ГРНТИ : 34.27.51
Предметные рубрики: КУЛЬТИВИРОВАНИЕ КЛЕТОК
СВЕТЯЩИЕСЯ БАКТЕРИИ
ПИТАТЕЛЬНАЯ СРЕДА
ЛЮЦИФЕРАЗА
БИОСИНТЕЗ
ПАТЕНТЫ
BIOTECHNOLOGY
LUCIFERASE PRODUCTION
PATENT
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Бондарь, Владимир Станиславович, Высоцкий, Евгений Степанович, Межевикин В. В., Райбекас А. А.
Заглавие : Исследование природного флавинового субстрата бактериальной люциферазы : научное издание
Место публикации : Докл. АН СССР. - 1987. - Т. 293, N 5. - С. 1253-1255. - ISSN 0002-3264
ГРНТИ : 34.15.21 + 31.27.17
Предметные рубрики: ЛЮЦИФЕРАЗА
СУБСТРАТЫ ПРИРОДНЫЕ
ФЛАВОПРОТЕИН
ПОЛУЧЕНИЕ
СВОЙСТВА
БАКТЕРИИ
LUCIFERASE
А ОР ОТЕ
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Бондарь В.С., Высоцкий Е.С., Заворуев В.В., Межевикин В.В., Райбекас А.А.
Заглавие : Получение препарата бактериальной люциферазы для биолюминесцентного анализа : научное издание
Место публикации : Прикл. биохимия и микробиол. - 1988. - Т. 24, N 6. - С. 745-753. - ISSN 0555-1099
ГРНТИ : 62.13.41
Предметные рубрики: ФЕРМЕНТНЫЕ ПРЕПАРАТЫ
ЛЮЦИФЕРАЗЫ
PHOTOBACTERIUM LEIOGNATHI
БИОЛЮМИНЕСЦЕНТНЫЙ АНАЛИЗ
LUCIFERASE
ВАСТЕ А
Аннотация: Описано получение препарата бактериальной люциферазы из бактерий Photobacterium leiognathi, предназначенной для определения содержания НАД(Ф)Н и активности НАД(Ф)-зависимых дегидрогеназ. Метод основан на использовании доступных и дешевых адсорбентов и включает только две хроматографические стадии. По данным SDS-фореза бактериальная люцифераза из P. leiognathi состоит из двух субъединиц и имеет молекулярную массу около 88 000. Библ. 24. Ин-т биофизики СО АН СССР, Красноярск, СССР
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodicheva E.K., Trubachev I.N., Medvedeva S.E., Egorova O.I. U - Shitova LYu
Заглавие : Growth and luminescence of luminous bacteria promoted by agents of microbial origin.
Место публикации : Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - С. 293-299. - ISSN 08843996 (ISSN)
Ключевые слова (''Своб.индексиров.''): amino acid--carbohydrate--folic acid--luciferase--nitrogen--riboflavin--article--biosynthesis--culture medium--electron microscopy--growth, development and aging--kinetics--luminescence--metabolism--photobacterium--physiology--time--ultrastructure--vibrio--amino acids--carbohydrates--culture media--folic acid--kinetics--luciferase--luminescence--microscopy, electron--nitrogen--photobacterium--riboflavin--time factors--vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V.A., Makurina V.I., Kuznetsov A.M., Kudryasheva N.S., Plotnikova N.B., Medvedeva S.E., Gritsenko I.S., Chernykh V.P.
Заглавие : The effect of succinic acid sulfoderivatives on bacterial luminescence
Место публикации : Prikladnaya Biokhimiya i Mikrobiologiya. - 1991. - Vol. 27, Is. 1. - С. 127-133. - ISSN 05551099 (ISSN)
Ключевые слова (''Своб.индексиров.''): luciferase--n (arylsulfonamido)succinimide--unclassified drug--article--bacterium--bioluminescence--nonhuman--bacteria (microorganisms)
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10.

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.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : RODIONOVA N.S., PETUSHKOV V.N., BELOBROV P.I.
Заглавие : CONFORMATIONAL RELAXATION OF BACTERIAL LUCIFERASE
Место публикации : Biofizika: MEZHDUNARODNAYA KNIGA, 1988. - Vol. 33, Is. 3. - С. 396-400. - 5. - ISSN 0006-3029
Примечания : Cited References: 10
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PETUSHKOV V.N., RODIONOVA N.S., BELOBROV P.I.
Заглавие : EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1985. - Vol. 50, Is. 3. - С. 338-342. - 5. - ISSN 0006-2979
Примечания : Cited References: 13
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13.

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
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PETUSHKOV V.N., KRATASYUK G.A., KRATASYUK V.A., BELOBROV P.I.
Заглавие : THERMAL INACTIVATION OF BACTERIAL LUCIFERASE
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1982. - Vol. 47, Is. 11. - С. 1504-1508. - 5. - ISSN 0006-2979
Примечания : Cited References: 10
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., VYSOTSKII E.S., MEZHEVIKIN V.V., RAIBEKAS A.A.
Заглавие : INVESTIGATION OF NATIVE FLAVIN SUBSTRATE OF BACTERIAL LUCIFERASE
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1987. - Vol. 293, Is. 5. - С. 1253-1255. - 3. - ISSN 0002-3264
Примечания : Cited References: 7
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : MEZHEVIKIN V.V., VYSOTSKII E.S., ZAVORUEV V.V., SALNIKOV M.V.
Заглавие : LOCALIZATION OF LUCIFERASE IN THE LUMINOUS BACTERIA PHOTOBACTERIUM-PHOSPHOREUM
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1981. - Vol. 258, Is. 6. - С. 1470-&. - 0. - ISSN 0002-3264
Примечания : Cited References: 9
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VOROBEVA T.I., VYSOTSKII E.S., ZAVORUEV V.V., MEZHEVIKIN V.V.
Заглавие : REGULATION OF LUCIFERASE SYNTHESIS IN PHOTOBACTERIUM-MANDAPAMENSIS
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1980. - Vol. 49, Is. 4. - С. 452-455. - 4. - ISSN 0026-2617
Примечания : Cited References: 8
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18.

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.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Vysotski E.S.
Заглавие : Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase
Колич.характеристики :4 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2013. - Vol. 450, Is. 1. - С. 147-150. - ISSN 1607-6729, DOI 10.1134/S1607672913030095
Примечания : Cited References: 14. - This work was supported by the Ministry of Education and Science of the Russian Federation (Government Contract no. 16.512.11.2141) and Council of the President of the Russian Federation on Grants and State Support of Leading Scientific Schools (project no. NSh-64987.2010.4).
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
GENE-EXPRESSION
CDNA
CLONING
BIOLUMINESCENCE
RENIFORMIS
Scopus
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin
Колич.характеристики :9 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2013. - Vol. 12, Is. 6. - С. 1016-1024. - ISSN 1474-905X, DOI 10.1039/c3pp00002h
Примечания : Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
CA2+-BINDING PHOTOPROTEIN
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
MNEMIOPSIS-LEIDYI
LIGHT-EMISSION
W92F OBELIN
CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.
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