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1.

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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2.

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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3.

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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4.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Visser N.V., van Hoek A..., Skakun V.V., Vysotski E.S., Lee J..., Visser AJWG
Заглавие : Green-Fluorescent Protein from the Bioluminescent Jellyfish Clytia gregaria Is an Obligate Dimer and Does Not Form a Stable Complex with the Ca2+-Discharged Photoprotein Clytin
Колич.характеристики :10 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2011. - Vol. 50, Is. 20. - С. 4232-4241. - ISSN 0006-2960, DOI 10.1021/bi101671p
Примечания : Cited References: 50. - This work was supported by NATO Collaborative Linkage Grant 979229, Grants SB RAS No. 2 and RFBR 08-04-92209, 09-04-12022, and 09-04-00172, the MCB program of the Russian Academy of Sciences, and Bayer AG.
Предметные рубрики: VIBRIO-FISCHERI Y1
ENERGY-TRANSFER
CORRELATION SPECTROSCOPY
BACTERIAL LUCIFERASE
REFRACTIVE-INDEX
PHOTOBACTERIUM-LEIOGNATHI
POLARIZED FLUORESCENCE
EXCITATION TRANSFER
RECOMBINANT OBELIN
LUMAZINE PROTEIN
Аннотация: Green-fluorescent protein (GFP) is the origin of the green bioluminescence color exhibited by several marine hydrozoans and anthozoans. The mechanism is believed to be Forster resonance energy transfer (FRET) within a luciferase GFP or photoprotein-GFP complex. As the effect is found in vitro at micromolar concentrations, for FRET to occur this complex must have an affinity in the micromolar range. We present here a fluorescence dynamics investigation of the recombinant bioluminescence proteins from the jellyfish Clytia gregaria, the photoprotein clytin in its Ca2+-discharged form that is highly fluorescent (lambda(max) = 506 nm) and its GFP (cgreGFP; lambda(max) = 500 nm). Ca2+-discharged clytin shows a predominant fluorescence lifetime of 5.7 ns, which is assigned to the final emitting state of the bioluminescence reaction product, coelenteramide anion, and a fluorescence anisotropy decay or rotational correlation time of 12 ns (20 degrees C), consistent with tight binding and rotation with the whole protein. A 34 ns correlation time combined with a translational diffusion constant and molecular brightness from fluorescence fluctuation spectroscopy all confirm that cgreGFP is an obligate dimer down to nanomolar concentrations. Within the dimer, the two chromophores have a coupled excited-state transition yielding fluorescence depolarization via FRET with a transfer correlation time of 0.5 ns. The 34 ns time of cgreGFP showed no change upon addition of a 1000-fold excess of Ca2+-discharged clytin, indicating no stable complexation below 0.2 mM. It is proposed that any bioluminescence FRET complex with micromolar affinity must be one formed transiently by the cgreGFP dimer with a short-lived (millisecond) intermediate in the clytin reaction pathway.
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5.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryasheva, N. S., Rozhko, T. V.
Заглавие : Effect of low-dose ionizing radiation on luminous marine bacteria: radiation hormesis and toxicity
Колич.характеристики :10 с
Коллективы : Russian Foundation for Basic Research [13-04-01305a]; Program "Molecular and Cellular Biology" of the Russian Academy of Sciences [VI 57.1.1]; Russian Science Foundation [14-14-00076]
Место публикации : J. Environ. Radioact.: ELSEVIER SCI LTD, 2015. - Vol. 142. - С. 68-77. - ISSN 0265-931X, DOI 10.1016/j.jenvrad.2015.01.012. - ISSN 1879-1700(eISSN)
Примечания : Cited References:131. - This work was supported by the Russian Foundation for Basic Research, Grant No.13-04-01305a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. The part of the work (review of effects of americium-241) was supported by the Russian Science Foundation, Grant No. 14-14-00076.
Предметные рубрики: RECOMBINANT LUMINESCENT MICROORGANISMS
PHOTOBACTERIUM-LEIOGNATHI
Ключевые слова (''Своб.индексиров.''): marine bacteria--low-dose effects--radiation hormesis--radiotoxicity--reactive oxygen species
Аннотация: The paper summarizes studies of effects of alpha- and beta-emitting radionuclides (americium-241, uranium-235+238, and tritium) on marine microorganisms under conditions of chronic low-dose irradiation in aqueous media. Luminous marine bacteria were chosen as an example of these microorganisms; bioluminescent intensity was used as a tested physiological parameter. Non-linear dose-effect dependence was demonstrated. Three successive stages in the bioluminescent response to americium-241 and tritium were found: 1 - absence of effects (stress recognition), 2 - activation (adaptive response), and 3 - inhibition (suppression of physiological function, i.e. radiation toxicity). The effects were attributed to radiation hormesis phenomenon. Biological role of reactive oxygen species, secondary products of the radioactive decay, is discussed. The study suggests an approach to evaluation of non-toxic and toxic stages under conditions of chronic radioactive exposure. (C) 2015 Elsevier Ltd. All rights reserved.
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