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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) : Vysotski E.S., Liu Z.J., Rose J..., Wang B.C., Lee J...
Заглавие : Preparation and preliminary study of crystals of the recombinant calcium-regulated photoprotein obelin from the bioluminescent hydroid Obelia longissima
Колич.характеристики :2 с
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: MUNKSGAARD INT PUBL LTD, 1999. - Vol. 55. - С. 1965-1966. - ISSN 0907-4449, DOI 10.1107/S0907444999011828
Примечания : Cited References: 23
Предметные рубрики: AEQUORIN
LUCIFERASE
LIGHT
Аннотация: Crystals of recombinant obelin, the Ca2+-regulated photoprotein from the marine hydroid Obelia longissima, have been grown from sodium citrate solutions. Crystals grow as hexagonal light-yellow rods (0.1 x 0.1 x 1.0 mm) which diffract to beyond 1.8 Angstrom with synchrotron radiation of 1.0 Angstrom wavelength. The crystals have a primitive hexagonal lattice with unit-cell parameters a = 81.55, c = 86.95 Angstrom. The asymmetric unit contains two molecules. This represents the successful preparation of single crystals of a photoprotein obelin which have promising diffraction properties.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Stepanyuk G.A., Vysotski E.S., Lee J..., Markova S.V., Malikova N.P., Wang B.C.
Заглавие : Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state
Колич.характеристики :6 с
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2006. - Vol. 103, Is. 8. - С. 2570-2575. - ISSN 0027-8424, DOI 10.1073/pnas.0511142103
Примечания : Cited References: 51
Предметные рубрики: X-RAY-DIFFRACTION
ANGSTROM RESOLUTION
CA2+-REGULATED PHOTOPROTEINS
AEQUORIN BIOLUMINESCENCE
VIOLET BIOLUMINESCENCE
W92F OBELIN
PROTEIN
LUCIFERASE
LIGHT
PROGRAM
Ключевые слова (''Своб.индексиров.''): coelenterazine--photoprotein--ef hand--luciferase--aequorin
Аннотация: The crystal structure at 1.93-angstrom resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Liu Z.J., Vysotski E.S., Lee J..., Rose J.P., Wang B.C.
Заглавие : Structure based mechanism of the Ca2+ -induced release of coelenterazine from the Renilla binding protein
Колич.характеристики :11 с
Место публикации : Proteins: WILEY-BLACKWELL, 2009. - Vol. 74, Is. 3. - С. 583-593. - ISSN 0887-3585, DOI 10.1002/prot.22173
Примечания : Cited References: 26
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
CRYSTAL-STRUCTURES
RENIFORMIS
LUCIFERASE
BIOLUMINESCENCE
PURIFICATION
ANGSTROM
MUELLERI
Ключевые слова (''Своб.индексиров.''): bioluminescence--ef-hand--coelenteramider--luciferase--ca2+-binding protein
Аннотация: The crystal structure of the Ca2+-loaded coelenterazine binding protein from Renilla muelleri in its apo-state has been determined at resolution 1.8 angstrom. Although calcium binding hardly affects the compact scaffold and overall fold of the structure before calcium addition, there are easily discerned shifts in the residues that were interacting with the coelenterazine and a repositioning of helices, to expose a cavity to the external solvent. Altogether these changes offer a straightforward explanation for how following the addition of Ca2+, the coelenterazine could escape and become available for bioluminescence on Renilla luciferase. A docking computation supports the possibility of a luciferase-binding protein complex.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V.V., Burakova L.P., Pyshnaya I.A., Frank L.A.
Заглавие : Bioluminescent reporters for identification of gene allelic variants
Колич.характеристики :8 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2012. - Vol. 38, Is. 3. - С. 298-305. - ISSN 1068-1620, DOI 10.1134/S1068162012030090
Примечания : Cited References: 13. - The authors thank the staff of Hematology Research Center (Krasnoyarsk Branch of Russian Academy of Medical Sciences) for providing DNA samples. The work was supported by the Integration Interdisciplinary Project of Siberian Branch of the Russian Academy of Sciences No. 76 and the Krasno yarsk Regional Fund for the support of scientific and technological activities.
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
RENILLA-MUELLERI
LUCIFERASE
PURIFICATION
SUBSTRATE
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): snp--pext reaction--obelin--luciferase--bioluminescent microassay
Аннотация: A method for single nucleotide polymorphism identification was developed, which was based on the primer extension reaction (PEXT) followed by bioluminescent solid-phase microassay. Recombinant Ca2+-regulated photoprotein obelin and coelenterazine-dependent Renilla muelleri luciferase were used as reporters. The study was performed as an example of SNP genotyping of the human F5 gene encoding human Factor V Leiden polymorphism 1691 G - A (R506Q). Genomic DNA was amplified by PCR using primers flanking polymorphic site of 140 base pairs. PCR products were used as templates for two PEXT reactions using two primers containing 3'-terminal nucleotides, which were complementary to either normal or mutant alleles. If the template and allele-specific primer were completely complementary, the latter was elongated with DNA polymerase. The resulting extension product contained biotin residue due to the presence of biotinylated deoxyuridine triphosphate (B-dUTP) in the reaction mixture. The products were analyzed using obelin-streptavidin conjugates. The optimal PEXT-reaction conditions were found, which ensured a high reliability of SNP genotyping. A new approach to simultaneously revealing both alleles in one well was developed using two bioluminescent reporters. The efficiency of the proposed approach was shown in the study of clinical DNA samples.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V.V., Korneeva S.I., Kudryavtsev A.N., Markova S.V., Stepanyuk G.A., Frank L.A.
Заглавие : Ca2+-triggered coelenterazine-binding protein from Renilla as an enzyme-dependent label for binding assay
Колич.характеристики :7 с
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2011. - Vol. 401, Is. 8. - С. 2573-2579. - ISSN 1618-2642, DOI 10.1007/s00216-011-5343-2
Примечания : Cited References: 17. - The work was supported by a "Leading Scientific School" (N 64987.2010.4) grant from the President of the Russian Federation and the "Molecular and Cell Biology" Program from the RAS.
Предметные рубрики: BIOLUMINESCENT IMMUNOASSAY
LUCIFERASE
PURIFICATION
RENIFORMIS
MUELLERI
OBELIN
PHOTOPROTEIN
EXPRESSION
SUBSTRATE
CLONING
Ключевые слова (''Своб.индексиров.''): ca2+-triggered coelenterazine-binding protein (cbp)--renilla muelleri luciferase--bioluminescent solid-phase microassay
Аннотация: The recombinant Ca2+-triggered coelenterazine-binding protein (CBP) from Renilla muelleri was investigated as a biospecifically labeled molecule for in vitro assay applications. The protein was shown to be stable in solutions in the frozen state, as well as stable under heating and to chemical modifications. Conjugates with biotin, oligonucleotide, and proteins were obtained and applied as biospecific molecules in a solid-phase microassay. CBP detection was performed with intact (no modifications were made) Renilla luciferase in the presence of calcium, and the detection limit was found to be 75 amol. Model experiments indicate that this approach shows much promise, especially with regard to the development of multianalytical systems.
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Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Tyulkova N.A., Krasnova O.I.
Заглавие : Formation of H2O2 in bacterial bioluminescence reaction with flavinmononucleotide activated with N-methylimidazole on the phosphate group without addition of the exogenous aldehyde
Колич.характеристики :4 с
Место публикации : Bioluminescence & Chemiluminescence: Progress and Perspectives: WORLD SCIENTIFIC PUBL CO PTE LTD, 2005. - 13th International Symposium on Bioluminescence and Chemiluminescence (AUG 02-06, 2004, Yokohama, JAPAN). - P91-94. - ISBN 981-256-118-8, DOI 10.1142/9789812702203_0021
Примечания : Cited References: 10
Предметные рубрики: LUCIFERASE
WOS
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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.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lisitsa A. E., Sukovatyi L. A., Kratasyuk V. A., Nemtseva E. V.
Заглавие : Viscous Media Slow Down the Decay of the Key Intermediate in Bacterial Bioluminescent Reaction
Колич.характеристики :4 с
Коллективы : Ministry of Science and Higher Education of the Russian Federation [6.7734.2017, 01201351504]
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2020. - Vol. 492, Is. 1. - С. 162-165. - ISSN 1607-6729, DOI 10.1134/S1607672920020106. - ISSN 1608-3091(eISSN)
Примечания : Cited References:15. - This work was supported by the Ministry of Science and Higher Education of the Russian Federation (project nos. 6.7734.2017 and 01201351504).
Предметные рубрики: LUCIFERASE
Аннотация: The effects of medium viscosity on the decay rate of the 4a-hydroperoxyflavin intermediate of the bioluminescent reaction was investigated. It was found that at low concentrations of glycerol or sucrose (viscosity 1.1-1.3 cP) the decay rate rises, whereas a further increase in viscosity to 6.2 cP leads to a decrease in the decay rate following a power function with an exponent of 0.82-0.84. Using molecular dynamics methods, it was shown that the presence of glycerol and sucrose molecules causes a change in the mobility of the amino acid residues in the active center of luciferase, particularly those responsible for binding of flavin. The results obtained are indicative of two opposite effects of viscous media with glycerol and sucrose: (1) destabilization of 4a-hydroperoxyflavin due to a change in the structural and dynamic properties of the protein and (2) stabilization of this intermediate by the decrease in the diffusion rate of its decay products.
WOS
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lisitsa, Albert E., Sukovatyi, Lev A., Bartsev, Sergey, I, Deeva, Anna A., Kratasyuk, Valentina A., Nemtseva, Elena, V
Заглавие : Mechanisms of Viscous Media Effects on Elementary Steps of Bacterial Bioluminescent Reaction
Колич.характеристики :19 с
Коллективы : Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science [20-44-243002]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]
Место публикации : Int. J. Mol. Sci.: MDPI, 2021. - Vol. 22, Is. 16. - Ст.8827. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms22168827
Примечания : Cited References:59. - The research was funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (project No. 20-44-243002); by RFBR according to the research project No. 20-34-90118.
Предметные рубрики: FLAVIN INTERMEDIATE
REDUCED FLAVIN
RATE CONSTANTS
LUCIFERASE
Аннотация: Enzymes activity in a cell is determined by many factors, among which viscosity of the microenvironment plays a significant role. Various cosolvents can imitate intracellular conditions in vitro, allowing to reduce a combination of different regulatory effects. The aim of the study was to analyze the media viscosity effects on the rate constants of the separate stages of the bacterial bioluminescent reaction. Non-steady-state reaction kinetics in glycerol and sucrose solutions was measured by stopped-flow technique and analyzed with a mathematical model developed in accordance with the sequence of reaction stages. Molecular dynamics methods were applied to reveal the effects of cosolvents on luciferase structure. We observed both in glycerol and in sucrose media that the stages of luciferase binding with flavin and aldehyde, in contrast to oxygen, are diffusion-limited. Moreover, unlike glycerol, sucrose solutions enhanced the rate of an electronically excited intermediate formation. The MD simulations showed that, in comparison with sucrose, glycerol molecules could penetrate the active-site gorge, but sucrose solutions caused a conformational change of functionally important alpha Glu175 of luciferase. Therefore, both cosolvents induce diffusion limitation of substrates binding. However, in sucrose media, increasing enzyme catalytic constant neutralizes viscosity effects. The activating effect of sucrose can be attributed to its exclusion from the catalytic gorge of luciferase and promotion of the formation of the active site structure favorable for the catalysis.
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