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1.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Markova S.V., Vysotski E.S., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : Crystal structure of a Ca2+-discharged photoprotein - Implications for mechanisms of the calcium trigger and bioluminescence
Колич.характеристики :6 с
Место публикации : J. Biol. Chem.: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2004. - Vol. 279, Is. 32. - С. 33647-33652. - ISSN 0021-9258, DOI 10.1074/jbc.M402427200
Примечания : Cited References: 31
Предметные рубрики: VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
ELECTRON-DENSITY
W92F OBELIN
AEQUORIN
PROTEINS
LIGHT
SEQUENCE
BINDING
COELENTERAZINE
Аннотация: Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigger and for generation of the different excited states that are the origin of the different colors of bioluminescence. Here we report the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-Angstrom resolution. The results lend support to the proposed mechanisms and provide new structural insight into details of these processes. Global conformational changes caused by Ca2+ association are typical of the class of calcium signal modulators within the EF-hand protein superfamily. Accommodation of the Ca2+ ions into the loops of the EF-hands is seen to propagate into the active site of the protein now occupied by the coelenteramide where there is a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis. Also the H-bonding between His-22 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of coelenteramide, confirming the proposed rapid excited state proton transfer that would lead to the excited state of the phenolate ion pair, which is responsible for the blue emission of bioluminescence.
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2.

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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3.

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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4.

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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5.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sid'ko A.F., Botvich I.Y., Pisman T.I., Shevyrnogov A.P.
Заглавие : Analysis of polarization characteristics of plant canopies using ground-based remote sensing measurements
Колич.характеристики :6 с
Место публикации : J. Quant. Spectrosc. Radiat. Transf.: PERGAMON-ELSEVIER SCIENCE LTD, 2014. - Vol. 144. - С. 117-122. - ISSN 0022-4073, DOI 10.1016/j.jqsrt.2014.03.031. - ISSN 1879-1352
Примечания : Cited References: 26
Предметные рубрики: LINEAR-POLARIZATION
AGRICULTURAL CROPS
WHEAT CANOPIES
LIGHT
REFLECTANCE
VEGETATION
Ключевые слова (''Своб.индексиров.''): spectral brightness coefficients--degree of polarization--polarized component of spectral brightness coefficients--farm crop--coniferous and broadleaf forests
Аннотация: The paper presents results and analysis of a study on polarized characteristics of the reflectance factor of different plant canopies under field conditions, using optical remote sensing techniques. Polarization characteristics were recorded from the elevated work platform at heights of 10-18 m in June and July. Measurements were performed using a double-beam spectrophotometer with a polarized light filter attachment, within the spectral range from 400 to 820 nm. The viewing zenith angle was below 20 degree. Birch (Betila pubescens), pine (Pinus sylvestris L.), wheat (Triticum acstivum) [L.] crops, corn (Zea mays L ssp. mays) crops, and various grass canopies were used in this study. The following polarization characteristics were studied: the reflectance factor of the canopy with the polarizer adjusted to transmit the maximum and minimum amounts of light (R-max and R-min), polarized component of the reflectance factor (R-q), and the degree of polarization (P). Wheat, corn, and grass canopies have higher R-max and R-min values than forest plants. The R-q and P values are higher for the birch than for the pine within the wavelength range between 430 and 740 nm. The study shows that polarization characteristics of plant canopies may be used as an effective means of decoding remote sensing data. (C) 2014 Elsevier Ltd. All rights reserved.
WOS
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6.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PARAMONOV L.E.
Заглавие : MUELLER MATRIX FOR AN ENSEMBLE OF PARTICLES OF ARBITRARY SHAPE WITH AN ARBITRARY SQUARE INTEGRABLE ORIENTATION DISTRIBUTION FUNCTION
Колич.характеристики :10 с
Место публикации : Opt. Spektrosk.: MEZHDUNARODNAYA KNIGA, 1994. - Vol. 77, Is. 6. - P911-920. - ISSN 0030-4034
Примечания : Cited References: 23
Предметные рубрики: SCATTERING
LIGHT
WOS
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7.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PARAMONOV L.E.
Заглавие : A THEORETICAL-ANALYSIS OF OPTICAL-ABSORPTION SPECTRA OF ALGAE
Колич.характеристики :6 с
Место публикации : Okeanologiya: MEZHDUNARODNAYA KNIGA, 1995. - Vol. 35, Is. 5. - P719-724. - ISSN 0030-1574
Примечания : Cited References: 30
Предметные рубрики: NATURAL-WATERS
PHYTOPLANKTON PIGMENTS
LIGHT
ATTENUATION
CELLS
CHLOROPHYLL
SCATTERING
COASTAL
Аннотация: The formula for the absorption cross sections of macroscopically isotropic volume element which consists of ''soft'' particles is proposed. The transformation formula for absorption cross sections on disperse composition is given. The dependence of absorption spectra of green, blue-green and diatom algae on microstructure of suspension is considered. Some inverse problems are discussed.
WOS
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8.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tolomeyev A.P., Zadereev Y.S.
Заглавие : An in situ method for the investigation of vertical distributions of zooplankton in lakes: test of a two-compartment enclosure
Колич.характеристики :8 с
Место публикации : Aquat. Ecol.: SPRINGER, 2005. - Vol. 39, Is. 2. - P181-188. - ISSN 1386-2588, DOI 10.1007/s10452-004-5732-0
Примечания : Cited References: 21
Предметные рубрики: MIGRATION
DAPHNIA
RADIATION
COPEPODS
EXPOSURE
PATTERNS
LIGHT
Ключевые слова (''Своб.индексиров.''): anoxic hypolimnion--solar radiation--stratified lake--vertical migration--zooplankton
Аннотация: Two-section enclosures were designed for the investigation of the effect of various physicochemical and biological factors on vertical distribution of zooplankton in situ. The framework of the enclosure was a cylindrical polyethylene column without any partitions inside, in which the isolation of animals in different sections after in situ exposure was achieved by pinching the flexible central part of the column. Enclosures were tested at the brackish stratified meromictic Lake Shira (Russia, Khakasia). The absence of fish and carnivorous zooplankton in the lake suggests that the vertical distribution of zooplankton is mainly determined by physicochemical gradients in the water column. Experiments and field observations demonstrated that all age and size groups of Arctodiaptomus salinus and Brachionus plicatilis strongly avoided surface layers during the daylight. The escape of zooplankton from the anoxic hypolimnion was less active. Statistically significant avoidance was observed only for copepodites C4-C5 and females of A. salinus. The relatively simple construction of the columns and easy handling during the experiment were the factors that favoured the use of this device to perform in situ basic tests of the effect of different factors on the vertical distribution of zooplankton.
WOS
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