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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tyulkova N.A., Sandalova T.P.
Заглавие : Comparative study of temperature effects on bacterial luciferases
Колич.характеристики :10 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1996. - Vol. 61, Is. 2. - P205-214. - ISSN 0006-2979
Примечания : Cited References: 23
Предметные рубрики: BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): bacterial luciferase--temperature--activation energy
Аннотация: Effects of temperature on bioluminescent patterns of luciferases from luminescent bacteria Vibrio harveyi, Vibrio fischeri, Photobacterium leiognathi, and Photobacterium phosphoreum were studied. The highest luminescence level was observed at 15-25 degrees C for the luciferase from P. phosphoreum, at 20-30 degrees C for the V. fischeri and P. leiognathi enzymes, and at 30-37 degrees C for the enzyme from V. harveyi. All the luciferases were significantly stabilized at increased salt concentrations, at low pH values, or in the presence of dithiothreitol (DTT) and EDTA. The addition of DTT and EDTA affected the reversible stage of enzyme inactivation, while salts reduced the rate of the irreversible stage. A peak corresponding to aggregated protein was detected by gel chromatography of irreversibly inactivated luciferase. Activation energies were calculated for each luciferase in bioluminescent reactions with decanal, dodecanal, tetradecanal, and without aldehydes. The activation energy of the reaction with tetradecanal was much lower than those with the other aldehydes. The temperature dependence of the lifetime of the long-lived reaction intermediate showed that in the 10-30 degrees C interval all the luciferases, except for the enzyme from V. harveyi, have only one active form.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : SANDALOVA T.P., TYULKOVA N.A.
Заглавие : INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE
Колич.характеристики :7 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 6. - P552-558. - ISSN 0006-2979
Примечания : Cited References: 21
Предметные рубрики: AMINO-ACID SEQUENCE
NUCLEOTIDE-SEQUENCE
REACTIVE SULFHYDRYL
PHOTOBACTERIUM-LEIOGNATHI
VIBRIO-HARVEYI
BIOLUMINESCENCE
SUBUNIT
REGION
GENE
Ключевые слова (''Своб.индексиров.''): luciferase--n-ethylmaleimide
Аннотация: The kinetics of inactivation of luciferases from four species of luminescent bacteria by the thiol reagent N-ethylmaleimide were investigated The dependencies of inactivation on ionic strength differed among the enzymes. Increasing the molarity of the buffer increased the rate of inactivation of all luciferases except that of Vibrio harveyi. Modification of Photobacterium phosphoreum luciferase decreased the maximal intensity of bioluminescence, whereas modification of Photobacterium leiognathi and Vibrio fischeri luciferases in high ionic strength buffers decreased the maximal intensity of bioluminescence and changed the luminescence decay rate constant. High ionic strength apparently alters the conformational states of the luciferases.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sukovataya I.E., Tyulkova N.A.
Заглавие : Kinetic analysis of bacterial water-organic media
Колич.характеристики :3 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P271-273. - ISSN 1522-7235, DOI 10.1002/bio.649.abs
Примечания : Cited References: 10
Ключевые слова (''Своб.индексиров.''): bacterial luciferase--organic solvents--michaelis constant
Аннотация: The interaction of luciferases from two types of luminous bacteria, Photobacterium leiognathi and Vibrio harveyi, with their substrates [the photorecovered. FMNH2 and long-chain aldehydes-decanal (C-10), dodecanal (C-12) and tetradecanal (C-14)] in water-organic media was analysed using kinetic graphical methods. Moderate concentrations of organic solvents have been demonstrated to activate the bioluminescence, while higher concentrations inhibit it. The interactions of these effectors with luciferases show different types of kinetics, which depend on concentrations of solvents, kinds of enzymes and substrates. The apparent value of the Michaelis constant, K-m for C-14 of both luciferases and for C-10 of luciferase V. harveyi is enhanced with increasing concentration of the organic solvent, but K-m for C-12 and C-10 of luciferase P. leiognathi decreases. Obviously, at the specific binding of aldehydes with luciferases in the first case, hydrophobic interactions are realized, but in second, the electrostatic interactions are realized. The series of changes in parameters of bioluminescence reaction catalysed by different luciferases is obviously determined by their structural peculiarities. Copyright (C) 2001 John Wiley & Sons, Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petrushkov V.N., Gibson B.G., Visser AJWG, Lee J...
Заглавие : Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria
Колич.характеристики :17 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - P164-180. - ISSN 0076-6879
Примечания : Cited References: 18
Предметные рубрики: YELLOW FLUORESCENT PROTEIN
FISCHERI STRAIN Y-1
AMINO-ACID-SEQUENCE
VIBRIO-FISCHERI
PHOTOBACTERIUM-LEIOGNATHI
RIBOFLAVIN PROTEIN
LUMINOUS BACTERIUM
LUMAZINE PROTEIN
FMN
Y1
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J...
Заглавие : Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1
Колич.характеристики :6 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 25. - С. 8413-8418. - ISSN 0006-2960, DOI 10.1021/bi952691v
Примечания : Cited References: 24
Предметные рубрики: LUMAZINE PROTEIN
LUMINOUS BACTERIUM
STRAIN Y-1
BIOLUMINESCENCE
EMISSION
PURIFICATION
TRANSIENT
LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M..., Gibson B.G., Lee J...
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive
Колич.характеристики :8 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 0006-2960, DOI 10.1021/bi9608931
Примечания : Cited References: 41
Предметные рубрики: BACTERIAL LUCIFERASE
LUMAZINE PROTEIN
FLAVIN INTERMEDIATE
ANGSTROM RESOLUTION
RIBOFLAVIN PROTEIN
PURIFICATION
MECHANISM
EMISSION
ALDEHYDE
INHIBITION
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects call be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, when the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on-off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme, These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found or the protein-protein interaction in the absence of the aliphatic component.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PRIMAKOVA G.A., KUZNETSOV A.M.
Заглавие : LUMINESCENT PLANKTON BACTERIA FROM THE CORAL REEFS AND LITTORAL WATERS OF THE TROPICAL REGIONS OF THE INDIAN-OCEAN AND THE SOUTH CHINA SEA
Колич.характеристики :8 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1990. - Vol. 59, Is. 5. - P630-637. - ISSN 0026-2617
Примечания : Cited References: 19
Предметные рубрики: LUMINOUS BACTERIA
SPECIES COMPOSITION
MEDITERRANEAN SEA
ESTUARY
GULF
ELAT
Аннотация: Luminescent bacteria were regularly encountered on the coral reefs of both the Indian Ocean and the South China Sea. Their counts in these regions amounted to 10(2) to 10(4) colony-forming units (CFU)/liter, and their proportion of the total numbers of saprophytic bacteria was 0.1-6.0%. Up to 85% of the luminescent bacteria occurred in the sea water in the form of aggregates ranging in size from 3-8-mu-m, to below 200-mu-m. The predominant species amongst the luminescent bacteria of these regions was Vibrio harvevi, comprising [4], with only 8.8% represented by Photobacterium leiognathi.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : GUREVICH V.B., SVETLAKOV A.V., POPOVA L.Y., SHENDEROV A.N.
Заглавие : GLUTAMATE SYNTHESIS CONTROL IN VIBRIO-HARVEYI
Колич.характеристики :3 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1986. - Vol. 55, Is. 1. - P66-68. - ISSN 0026-2617
Примечания : Cited References: 10
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., van Stokkum IHM, Gobets B..., van Mourik F..., Lee J..., van Grondelle R..., Visser AJWG
Заглавие : Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
Колич.характеристики :6 с
Место публикации : J. Phys. Chem. B: AMER CHEMICAL SOC, 2003. - Vol. 107, Is. 39. - P10934-10939. - ISSN 1520-6106, DOI 10.1021/jp034266e
Примечания : Cited References: 52
Предметные рубрики: TIME-RESOLVED FLUORESCENCE
VIBRIO-FISCHERI Y1
FEMTOSECOND SOLVATION DYNAMICS
FLAVIN ADENINE-DINUCLEOTIDE
PHOTOBACTERIUM-LEIOGNATHI
BIOLOGICAL WATER
SOLVENT DYNAMICS
DIELECTRIC-RELAXATION
MOLECULAR-DYNAMICS
TRYPTOPHAN
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by similar to7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Govorun A. E., Esimbekova E. N., Kratasyuk V. A.
Заглавие : NAD(P)H:FMN-Oxidoreductase Functioning Under Macromolecular Crowding: In Vitro Modeling
Место публикации : Doklad. Biochem. Biophys.: Pleiades Publishing, 2019. - Vol. 486, Is. 1. - С. 213-215. - ISSN 16076729 (ISSN) , DOI 10.1134/S160767291903013X
Аннотация: The functioning of NAD(P)H:FMN‑oxidoreductase (Red) from Vibrio fischeri under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin) was studied. The dissociation rate constants and the activation energies of dissociation of Red to the subunits were calculated, and the process of denaturation of Red was analyzed. It is shown that the functioning of Red both under conditions of MMC and in diluted solutions is the same. This result refutes the common belief that the native conformation of enzymes in vivo is stabilized due to MMC as compared to the in vitro conditions. © 2019, Pleiades Publishing, Ltd.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gulnov D. V., Nemtseva E. V., Gerasimova M. A., Kratasyuk V. A.
Заглавие : Structural transitions of photobacterium leiognathi luciferase determined by various optical techniques under urea-induced equilibrium denaturation
Место публикации : Tsitologiya: Sankt Peterburg, 2018. - Vol. 60, Is. 10. - С. 847-850. - ISSN 00413771 (ISSN) , DOI 10.7868/S0041377118100181
Ключевые слова (''Своб.индексиров.''): bacterial luciferase--circular dichroism--denaturation--protein fluorescence lifetime--protein intermediate states
Аннотация: The study was aimed to identification of conformational transitions of Photobacterium leiognathi luciferase during equilibrium denaturation with urea using several optical techniques, including circular dichroism, stationary and time-resolved fluorescence. Gravity center and intensity ratio I 325 /I 390 for the fluorescence spectra, molar ellipticity at 222 nm and fluorescence lifetimes of the protein were analyzed. Investigated parameters revealed two possible transitions for P. leiognathi luciferase with the midpoints at 0.5—1.1 and 3.5—4.2 M of urea. Changes in the values of two lifetime components, characterizing the luciferase fluorescence reflect both transitions, while steady-state fluorescence parameters (gravity center of spectrum and I 325 /I 390 ratio) reveal only the second one. Far-UV circular dichroism spectra displayed transitions at 4.2 M of urea for P. leiognathi luciferase. Conformational transitions characteristics of P. leiognathi luciferase and previously studied Vibrio harveyi luciferase (Inlow et al., 2002) were compared. Since, according to the published data for V. harveyi, midpoint of the second conformational transition is at about 2.5 M of urea, the results indicate more stable secondary structure for the P. leiognathi luciferase under study. The possible reasons for observed differences in fluorescent characteristics of two types of luciferases during denaturation can be connected to the microenvironment variation of the tryptophan residues in their tertiary structure, namely in position 131 and 277 in a-subunit. © 2018 Sankt Peterburg. All rights reserved.
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12.

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
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13.

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.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogil'naya O.A., Krivomazova E.S., Kargatova T.V., Lobova T.I., Popova L.Y.
Заглавие : Formation of structured communities by natural and transgenic naphthalene-degrading bacteria
Колич.характеристики :6 с
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA, 2005. - Vol. 41, Is. 1. - P63-68. - ISSN 0003-6838, DOI 10.1007/s10438-005-0012-x
Примечания : Cited References: 18
Предметные рубрики: GENETICALLY-ENGINEERED MICROORGANISM
POLYCYCLIC AROMATIC-HYDROCARBONS
BIOFILM FORMATION
DEGRADATION
Аннотация: This study concerns the formation of structured communities by monocultures and binary associations of Pseudomonas fluorescens transgenic strains and natural heterotrophic bacterial species in naphthalene-containing media with various osmotic pressures. It was shown that cells of P. fluorescens strain 5RL, harboring a recombinant construct in the chromosome, were more resistant to the combined action of the stress factors under study than P. fluorescens 82/pUTK21, harboring a recombinant construct within a plasmid. Natural P. fluorescens 1 strains, particularly Vibrio sp. 14, were more viable at high osmotic pressures and naphthalene concentrations. Experiments with the combined introduction of transgenic and natural bacterial strains at high osmotic pressures demonstrated the stable coexistence of bacterial associations in biofilms, independent of naphthalene concentration. Strains considered for introduction into the environment for bioremediation should be assessed with regard to their susceptibility to the combined effect of anthropogenic and natural stress factors. The design of bacterial associations for the same purpose should take into account the effect of factors important for their survival in polluted areas.
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vetrova E.V., Kudryasheva N.S., Visser AJWG, van Hoek A...
Заглавие : Characteristics of enclogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fischeri NAD(P)H : FMN-oxidoreductase
Колич.характеристики :5 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2005. - Vol. 20: 11th International Symposium on Luminescence Spectrometry - Detection Techniques in Biomedical and Environmental Analysis (MAY 05-08, 2004, Beijing, JAPAN), Is. 3. - P205-209. - ISSN 1522-7235, DOI 10.1002/bio.815
Примечания : Cited References: 22
Предметные рубрики: FLAVODOXIN
ANISOTROPY
REDUCTASE
DYNAMICS
SYSTEM
Ключевые слова (''Своб.индексиров.''): bacterial bioluminescence--flavin fluorescence
Аннотация: The bioluminescent bacterial enzyme system NAD(P)H:FMN-oxidoreductase-luciferase has been used as a test system for ecological monitoring. One of the modes to quench bioluminescence is the interaction of xenobiotics with the enzymes, which inhibit their activity. The use of endogenous flavin fluorescence for investigation of the interactions of non-fluorescent compounds with the bacterial luciferase from Photobacterium leiognathi and NAD(P)H:FMN-oxidoreductase from Vibrio fischeri has been proposed. Fluorescence spectroscopy methods have been used to study characteristics of endogenous flavin fluorescence (fluorophore lifetime, the rotational correlation time). The fluorescence anisotropy behaviour of FMN has been analysed and compared to that of the enzyme-bound flavin. The fluorescence characteristics of endogenous flavin of luciferase and NAD(P)H:FMN-oxidoreductase have been shown to be applicable in studying enzymes' interactions with non-fluorescent compounds. Copyright (c) 2005 John Wiley & Sons, Ltd.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Denisov I., Lukyanenko K., Yakimov A., Kukhtevich I., Esimbekova E., Belobrov P.
Заглавие : Disposable luciferase-based microfluidic chip for rapid assay of water pollution
Место публикации : Lumin. - 2018. - Vol. 33, Is. 6. - С. 1054-1061. - ISSN 15227235 (ISSN) , DOI 10.1002/bio.3508
Ключевые слова (''Своб.индексиров.''): bioassay--lab-on-a-chip--luciferase--microfluidics--solvent bonding
Аннотация: In the present study, we demonstrate the use of a disposable luciferase-based microfluidic bioassay chip for environmental monitoring and methods for fabrication. The designed microfluidic system includes a chamber with immobilized enzymes of bioluminescent bacteria Photobacterium leiognathi and Vibrio fischeri and their substrates, which dissolve after the introduction of the water sample and thus activate bioluminescent reactions. Limits of detection for copper (II) sulfate, 1,3-dihydroxybenzene and 1,4-benzoquinone for the proposed microfluidic biosensor measured 3 ?M, 15 mM, and 2 ?M respectively, and these values are higher or close to the level of conventional environmental biosensors based on lyophilized bacteria. Approaches for entrapment of enzymes on poly(methyl methacrylate) (PMMA) plates using a gelatin scaffold and solvent bonding of PMMA chip plates under room temperature were suggested. The proposed microfluidic system may be used with some available luminometers and future portable luminescence readers. © 2018 John Wiley & Sons, Ltd.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Гительзон И.И., Воробьева Т.И.
Заглавие : Светящиеся бактерии, ассоциированные с бентосными организмами : научное издание
Место публикации : Микробиология. - 1988. - Т. 57, N 5. - С. 847-852
ГРНТИ : 34.27.53
Предметные рубрики: СВЕТЯЩИЕСЯ БАКТЕРИИ
VIBRIO HARVEYI (BACT.)
PHOTOBACTERIUM (BACT.)
ВСТРЕЧАЕМОСТЬ
БЕНТОСНЫЕ ЖИВОТНЫЕ
КИШЕЧНИК ДОННЫХ ЖИВОТНЫХ
ВОДНЫЕ ЭКОСИСТЕМЫ
ИНДИЙСКИЙ ОКЕАН
КОРАЛЛОВЫЕ РИФЫ
Аннотация: Исследована встречаемость светящихся бактерий в ассоциации с бентосными животными, в частности, обитателями коралловых рифов. Обнаружено, что светящиеся бактерии регулярно встречаются на поверхности тела и в кишечнике многих донных животных, но ни с одним из обследованных видов не связаны облигатно. Их ареал простирается от литорали до максимально обследованных глубин 1600 м. Определен состав выделенных бактерий, доминирующим оказался вид Vibrio harveyi, в отличие от морских рыб, кишечник к-рых населен преимущественно видами р. Photobacterium.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M., Gibson B.G., Lee J.
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive
Место публикации : Biochemistry. - 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 00062960 (ISSN) , DOI 10.1021/bi9608931
Ключевые слова (''Своб.индексиров.''): luciferase--anisotropy--antenna--article--bioluminescence--complex formation--energy transfer--enzyme active site--enzyme kinetics--nonhuman--priority journal--protein protein interaction--spectroscopy--vibrionaceae--bacterial proteins--carrier proteins--cloning, molecular--dithionite--flavin mononucleotide--kinetics--luciferases--luminescent measurements--luminescent proteins--models, structural--photobacterium--protein binding--protein conformation--recombinant proteins--spectrophotometry--vibrio--bacteria (microorganisms)--photobacterium--photobacterium leiognathi--vibrio fischeri--vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Medvedeva S.E.
Заглавие : Transfer of xenobiotics through cell membranes of luminous bacteria
Место публикации : Luminescence. - 1999. - Vol. 14, Is. 5. - С. 267-270. - ISSN 15227235 (ISSN)
Ключевые слова (''Своб.индексиров.''): luminous bacteria--toxicant--ultrastructure--bacterial dna--edetic acid--toluene--xenobiotic agent--article--cell membrane--dna damage--drug effect--luminescence--metabolism--photobacterium--sensitivity and specificity--transport at the cellular level--ultrastructure--vibrio--biological transport--cell membrane--dna damage--dna, bacterial--edetic acid--luminescence--photobacterium--sensitivity and specificity--toluene--vibrio--xenobiotics
Аннотация: The influence of some chemical substances on luminous bacteria was studied to elucidate the interrelation between the xenobiotics action on bacterial luminescence and cell ultrastructure. Such substances as quinones, phenols, chlorides of heavy metals (in concentrations of substances inhibiting luminescence by 50%) resulted in damaging effects upon bacteria: a lot of cells had damage of membranes due to changes in their permeability. It was found that the high concentration of EDTA and toluene decreased the luminescence and caused the condensation of DNA-fibrils and the cell damage after long-term and short-term action. The low concentration of EDTA and toluene did not decrease the bacterial luminescence; the noticeable damage of cell membranes did not take place during short-term treatment. However, the long action of these substances changed the membrane permeability resulting in increased sensitivity of bacterial luminescence to some toxic substances. Copyright В© 1999 John Wiley & Sons, Ltd.
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20.

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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