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Microdistribution of 241Am in structures of submerged macrophyte Elodea canadensis growing in the Yenisei River / L. Bondareva [et al.] // Journal of Environmental Radioactivity. - 2010. - Vol. 101, Is. 1. - P16-21, DOI 10.1016/j.jenvrad.2009.08.003 . - ISSN 0265-931X
Кл.слова (ненормированные):
Alpha-track analysis -- Americium -- Elodea canadensis -- Liquid-scintillation spectrometry -- Microdistribution -- Alpha-track analysis -- Elodea canadensis -- Microdistribution -- Scintillation spectrometry -- Track analysis -- Liquids -- Luminescence -- Radioisotopes -- Scintillation -- Spectrometry -- Spectroscopy -- Americium -- americium 241 -- americium -- americium -- bioaccumulation -- experimental study -- leaf -- macrophyte -- mass spectrometry -- morphology -- radionuclide -- spatial distribution -- stem -- submerged vegetation -- tracking -- aquatic flora -- article -- bioaccumulation -- concentration (parameters) -- elodea canadensis -- environmental radioactivity -- isotope analysis -- isotope tracing -- leaf lamina -- leaf surface -- macrophyte -- nonhuman -- plant cell -- plant morphology -- plant stem -- radioisotope distribution -- river -- chemistry -- Hydrocharitaceae -- metabolism -- plant -- plant leaf -- radiation monitoring -- river -- water pollutant -- Eurasia -- Russian Federation -- Yenisei River -- Elodea canadensis -- Americium -- Hydrocharitaceae -- Plant Leaves -- Plant Shoots -- Plant Stems -- Radiation Monitoring -- Rivers -- Water Pollutants, Radioactive
Аннотация: A submerged macrophyte of the Yenisei River, Elodea canadensis, was used to study the microdistribution of the artificial radionuclide 241Am among different components of the plant. The total amount of 241Am added to the experimental system was 1850 В± 31 Bq/L. The total amount of 241Am accumulated by the plants was 182 Bq per sample, or 758,333 В± 385 Bq/kg dry mass. It has been found that the major portion of 241Am accumulated by E. canadensis, up to 85%, was bound to solid components of the cells. It is observed that the microdistribution of 241Am within different components of the submerged plant E. canadensis was not uniform. 241Am distribution vary depending on the age of the leaf blades, the state of the cells and morphological features of the plant stem. В© 2009 Elsevier Ltd. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, 50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Chemistry Department, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondareva, L.; Vlasova, I.; Mogilnaya, O.; Bolsunovsky, A.; Kalmykov, S.

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Physicochemical properties of multicomponent poly(hydroxyalkanoates) / T. G. Volova, P. V. Mironov, A. D. Vasil'ev // Biophysics. - 2007. - Vol. 52, Is. 3. - P293-297, DOI 10.1134/S0006350907030062 . - ISSN 0006-3509
Кл.слова (ненормированные):
Hydroxyhexanoate -- Hydroxyvalerate -- Poly(hydroxybutyrate) -- Bacteria (microorganisms) -- Cupriavidus necator -- Insectivora
Аннотация: The properties of new five-component poly(hydroxyalkanoates) (PHA) formed by short-and medium-chain monomers synthesized by the bacterium Wautersia eutropha B5786 were studied by X-ray diffraction, IR spectroscopy, differential thermal analysis, and viscometry. The degree of crystallinity of PHA decreased from 72 to 57% as the molar fraction of hydroxyhexanoate increased from 2.5 to 18.0 mol%. The melting temperature (T m) and decomposition temperature (T d) of the multicomponent PHA are lower than those for poly(hydroxybutyrate), whose T m and T d are 168-170 and 260-265В°C, respectively. Both parameters of the multicomponent PHA decrease to 156 and 252В°C, respectively, as the hydroxyhexanoate mole fraction is raised. The effect of hydroxyhexanoate on the physicochemical properties of the PHA is similar to that of hydroxyvalerate observed previously. В© 2007 Pleiades Publishing, Inc.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Siberian State Technological University, Krasnoyarsk 660049, Russian Federation
Kirenskii Institute of Physics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Mironov, P.V.; Vasil'ev, A.D.

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Physicochemical properties of two-component polyhydroxyalkanoates, 3-hydroxybutyrate-3-hydroxyvalerate copolymers / T. G. Volova [et al.] // Biophysics. - 2004. - Vol. 49, Is. 6. - P934-942 . - ISSN 0006-3509
Кл.слова (ненормированные):
Hydroxybutyrate-hydroxyvalerate copolymers -- Physicochemical properties -- Polyhydroxyalkanoates -- Structure -- Bacteria (microorganisms) -- Cupriavidus necator
Аннотация: A series of two-component polyhydroxyalkanoates composed of hydroxybutyrate-hydroxyvalerate copolymers with different monomer ratio was obtained with the use of bacteria Ralstonia eutropha B5786. The properties of the polyhydroxyalkanoates in comparison with the homopolymer of hydroxybutyric acid were studied by X-ray diffraction analysis, IR spectroscopy, differential thermal analysis, and viscometry. The ratio of crystalline to amorphous phase in the copolymers tends to unity with increasing hydroxyvalerate content. This is accompanied by a decrease in the degree of crystallinity of the copolymers from 70-80 to 45-50%, the dependence is virtually linear within the range, of hydroxyvalerate mole fraction from several to 25-30 mol%. Thermal characteristics, melting temperature (Tm) and decomposition temperature (Td), of the polyhydroxyalkanoate copolymers are lower than those for polyhydroxybutyrate, whose Tm and Td are 168-170 and 260-265В°C, respectively. Both parameters decrease to 150-160 and 200-220В°C, respectively, when the hydroxyvalerate mole fraction is raised. No distinct correlation between polymer composition and molecular weight has been revealed. Copyright В© 2004 by MAIK "Nauka/Interperiodica".

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian State Technological University, Krasnoyarsk, 660049, Russian Federation
Kirenskii Institute of Physics, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Plotnikov, V.F.; Shishatskaya, E.I.; Mironov, P.V.; Vasil'ev, A.D.

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Distribution and migration of metals in trophic chains of the Yenisei ecosystem near Krasnoyarsk City / O. V. Anishchenko [et al.] // Water Resources. - 2009. - Vol. 36, Is. 5. - P594-603, DOI 10.1134/S0097807809050121 . - ISSN 0097-8078
Кл.слова (ненормированные):
Aquatic organisms -- Atomic absorption -- Bulk concentration -- Cd concentrations -- Cr concentration -- Ecosystem components -- Emission spectral analysis -- Flame photometry -- Fly larvae -- International standards -- Periphytons -- Primary producers -- Waterbodies -- Aquaculture -- Cadmium -- Chromium -- Ecology -- Photometry -- Spectroscopy -- Spectrum analysis -- Spectrum analyzers -- Water absorption -- Water analysis -- Concentration (process) -- aluminum -- aquatic ecosystem -- aquatic organism -- cadmium -- chromium -- concentration (composition) -- copper -- pollutant transport -- river pollution -- trophic environment -- Krasnoyarsk [Russian Federation] -- Russian Federation -- Yenisei River -- Bryophyta -- Decapoda (Crustacea) -- Thymallus arcticus
Аннотация: Methods of atomic absorption, flame photometry, and emission spectral analysis were used to study the concentrations of metals in water and major ecosystem components of the Yenisei River upstream of Krasnoyarsk City (conventionally background area). The mean bulk concentrations of Al and Cu in water exceeded the MAC for water bodies used for fishery. Cu concentration in freshwater shrimp was found to be reliably higher than that in the link of primary producers (periphyton), and Cd concentration in caddis fly larvae was found to exceed that in water moss. The maximal concentrations of metals among the examined aquatic organisms were recorded in periphyton. Cr concentration in the muscles of Arctic grayling was found to exceed some international standards. В© 2009 Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Geophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok 50, Krasnoyarsk 660036, Russian Federation
Siberian Federal University, prosp. Svobodnyi 79, Krasnoyarsk 660046, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Anishchenko, O.V.; Gladyshev, M.I.; Kravchuk, E.S.; Sushchik, N.N.; Gribovskaya, I.V.

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Electron spectroscopy of nanodiamond surface states / P. I. Belobrov [et al.] // Applied Surface Science. - 2003. - Vol. 215, Is. 1-4 SPEC. - P169-177, DOI 10.1016/S0169-4332(03)00287-3 . - ISSN 0169-4332
Кл.слова (ненормированные):
Auger electron spectroscopy -- Nanodiamond -- PEELS -- Surface states -- XPS -- Auger electron spectroscopy -- Diamonds -- Electrons -- Hydrogen -- Nanostructured materials -- Surfaces -- X ray photoelectron spectroscopy -- Nanodiamond (ND) surface states -- Surface phenomena
Аннотация: Electronic states of nanodiamond (ND) were investigated by PEELS, XPS and CKVV Auger spectra. Parallel electron energy loss spectra (PEELS) show that the electrons inside of ND particles are sp3 hybridized but there is a surface layer containing distinct hybridized states. The CKVV Auger spectra imply that the HOMO of the ND surface has a shift of 2.5eV from natural diamond levels of ?p up to the Fermi level. Hydrogen (H) treatment of natural diamond surface produces a chemical state indistinguishable from that of ND surfaces using CKVV. The ND electronic structure forms ?s1?p2?1 surface states without overlapping of ?-levels. Surface electronic states, including surface plasmons, as well as phonon-related electronic states of the ND surface are also interesting and may also be important for field emission mechanisms from the nanostructured diamond surface. В© 2003 Elsevier Science B.V. All rights reserved.

Scopus
Держатели документа:
Molecular Architecture Group, Institute of Biophysics SB RAS, UNESCO Dept. Krasnoyarsk Stt. T.U., Krasnoyarsk 660036, Russian Federation
School of Physics, University of Melbourne, Parkville, Vic. 3010, Australia
RRC Kurchatov Institute, Moscow 123182, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Belobrov, P.I.; Bursill, L.A.; Maslakov, K.I.; Dementjev, A.P.

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Low-field electron emission of diamond/pyrocarbon composites / A. V. Karabutov [et al.] // Journal of Vacuum Science and Technology B: Microelectronics and Nanometer Structures. - 2001. - Vol. 19: 13th International Vaccum Microelectronics Conference (14 August 2000 through 17 August 2000, Guangzhou, Is. 3. - P965-970, DOI 10.1116/1.1368669 . - ISSN 1071-1023
Кл.слова (ненормированные):
Carbon nanotubes -- Chemical bonds -- Chemical vapor deposition -- Composite materials -- Diamond films -- Electric conductivity -- Electron emission -- Electron energy levels -- Hysteresis -- Interfaces (materials) -- Raman scattering -- Semiconducting diamonds -- Semiconductor quantum wells -- Transmission electron microscopy -- X ray diffraction analysis -- X ray photoelectron spectroscopy -- Pyrocarbon composites -- Nanostructured materials
Аннотация: The properties of field electron emission for diamond/pyrocarbon nanocomposites produced from diamond particles surrounded by a pyrocarbon matrix were studied. Low-threshold emissions at fields of ?1 V/?m with no activation or hysterisis in the current versus voltage (I/V) behaviour were observed for the materials. Scanning tunneling-field emission microscopy was used to study the mechanisms of low-field electron emission from the composites, and a model based on quantum well effect at the diamond/graphite interface was proposed and discussed.

Scopus
Держатели документа:
General Physics Institute, Vavilova str. 38, Moscow 117942, Russian Federation
Central Research Institute of Materials, Paradnaya str. 8, St. Petersburg 191014, Russian Federation
Institute of Biophysics, Krasnoyarsk 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Karabutov, A.V.; Frolov, V.D.; Konov, V.I.; Ralchenko, V.G.; Gordeev, S.K.; Belobrov, P.I.

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Preparation of complexes nanodiamond-protein-delta-aluminum oxide. / A. P. Puzyr' [et al.] // Doklady Biochemistry. - 2000. - Vol. 373, Is. 1-6. - P139-141 . - ISSN 0012-4958
Кл.слова (ненормированные):
aluminum oxide -- cytochrome c -- diamond -- article -- chemistry -- electron microscopy -- metabolism -- spectroscopy -- synthesis -- Aluminum Oxide -- Cytochrome c Group -- Diamond -- Microscopy, Electron -- Spectrum Analysis

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk, Russia. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Puzyr', A.P.; Bondar', V.S.; Belobrov, P.I.; Bukaemskii, A.A.

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Surface properties of nanodiamond films deposited by electrophoresis on Si(100) / E. Maillard-Schaller [et al.] // Diamond and Related Materials. - 1999. - Vol. 8, Is. 2-5. - P805-808 . - ISSN 0925-9635
Кл.слова (ненормированные):
Energy band diagram -- Nanodiamond -- Raman spectroscopy -- Surface characterization -- Band structure -- Electrodeposition -- Electrophoresis -- Hydrogen -- Nanostructured materials -- Nitrogen -- Oxidation -- Oxygen -- Phonons -- Plasma applications -- Silicon wafers -- Surface properties -- Dielectrophoresis -- Negative electron affinity (NEA) -- Phonon confinement effect -- Diamond films
Аннотация: The surface properties of diamond nanoparticles (40-50 A in diameter) have been investigated by X-ray photoelectron spectroscopy (XPS), UV photoelectron spectroscopy (UPS) and Raman spectroscopy. The diamond nanoparticles have been deposited on flat Si(100) substrates by electrophoresis/dielectrophoresis. The as-deposited films are strongly oxidized and present a 1-2% nitrogen content. After treatment at 850 В°C in H2 plasma for 60 min, the oxygen is removed, and the position of the C 1s core-level peak indicates a n-type electronic comportment of the diamond nanoparticles. Raman spectroscopy of the as-deposited film shows a sp3 contribution at 1321 cm-1 and a sp2 contribution around 1620 cm-1. The 12 cm-1 shift of the sp3 contribution with respect to the bulk diamond peak at 1333 cm-1 is attributed to a phonon confinement effect due to the size of the diamond particles. The H2 plasma treatment induces a size decrease of the nanocrystallites confirmed by Raman and scanning electron microscopy (SEM) measurements. UPS spectroscopy shows a negative electron affinity of -0.2 eV of the hydrogenated nanodiamond film.

Scopus
Держатели документа:
Solid State Physics Department, University of Fribourg, 1700, Fribourg, Switzerland
Institute of Christallography, 117333, Moscow, Russian Federation
Institute of Biophysics, 660036, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Maillard-Schaller, E.; Kuettel, O.M.; Diederich, L.; Schlapbach, L.; Zhirnov, V.V.; Belobrov, P.I.

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Time course of the spectral brightness of agricultural crops during the vegetation period in Krasnoyarsk krai / A. F. Sid'ko, I. Yu. Pugacheva, A. P. Shevyrnogov // Doklady Biological Sciences. - 2008. - Vol. 419, Is. 1. - P114-117, DOI 10.1134/S0012496608020130 . - ISSN 0012-4966
Кл.слова (ненормированные):
article -- crop -- histology -- light -- metabolism -- plant -- Russian Federation -- season -- spectroscopy -- Crops, Agricultural -- Light -- Plants -- Russia -- Seasons -- Spectrum Analysis

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sid'ko, A.F.; Pugacheva, I.Yu.; Shevyrnogov, A.P.

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10.

A study of spectral-polarization characteristics of plant canopies using land-based remote sensing / A. F. Sid'ko [et al.] // Journal of Quantitative Spectroscopy and Radiative Transfer. - 2013. - Vol. 129. - P109-117, DOI 10.1016/j.jqsrt.2013.06.001 . - ISSN 0022-4073
Кл.слова (ненормированные):
Farm crops -- Forest stands -- Spectral brightness coefficients -- Spectral-polarization characteristics -- Forest stand -- Near-infrared spectral regions -- Plant reflectance -- Polarized components -- Reflectance spectrum -- Reflection properties -- Spectral brightness -- Spectral-polarization characteristics -- Forestry -- Luminance -- Physiological models -- Polarization -- Reflection -- Crops -- brightness temperature -- canopy reflectance -- crop plant -- nadir -- polarization -- remote sensing -- spectral analysis -- Farm Crops -- Forestry -- Forests -- Polarization -- Reflection -- Triticum aestivum -- Zea mays
Аннотация: The study addresses reflection and spectral-polarization characteristics of forest stands and farm crops obtained under field conditions. The study of the reflection properties of farm crops shows that during the summer plant growing season, the major factors influencing the plant canopy reflectance are morpho-physiological parameters, plant architectonics, solar elevation h0, and viewing angle. The crop reflectance minimum was recorded at viewing angles 25-30В° with respect to the nadir. Coniferous and broadleaf forest stands had similar reflectance spectra of polarized light. The polarized component was smaller for all coniferous stands than for broadleaf ones. For broad-leaved farm crops (wheat and corn), the polarized component of the spectral brightness coefficients had a greater influence on the plant reflectance in the red and near-infrared spectral regions, ?>720nm. В© 2013 Elsevier Ltd.

Scopus
Держатели документа:
Institute of Biophysics of the Siberian Branch of RAS, 50-50 Akademgorodok, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sid'ko, A.F.; Botvich, I.; Pisman, T.I.; Shevyrnogov, A.P.

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11.

Spectral composition of light and plant productivity / A. A. Tikhomirov // Advances in Space Research. - 1996. - Vol. 18, Is. 4-5. - P259-263 . - ISSN 0273-1177
Кл.слова (ненормированные):
article -- biology -- cucumber -- growth, development and aging -- illumination -- light -- maize -- photon -- photosynthesis -- plant -- radiation exposure -- spectroscopy -- sunflower -- tomato -- wheat -- Cucumis sativus -- Helianthus -- Light -- Lighting -- Lycopersicon esculentum -- Photobiology -- Photons -- Photosynthesis -- Plants -- Spectrum Analysis -- Triticum -- Zea mays

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Academgorodok, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tikhomirov, A.A.

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12.

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 [Text] / N. P. Malikova [et al.] // Biochemistry. - 2011. - Vol. 50, Is. 20. - P4232-4241, DOI 10.1021/bi101671p. - 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. . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
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.

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Malikova, Natalia P.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
[Visser, Nina V.
van Hoek, Arie] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Nina V.
van Hoek, Arie
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Skakun, Victor V.] Belarusian State Univ, Dept Syst Anal, Minsk 220050, Byelarus
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Visser, N.V.; van Hoek, A...; Skakun, V.V.; Vysotski, E.S.; Lee, J...; Visser, AJWG

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13.

NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex [Text] / M. S. Titushin [et al.] // J. Biol. Chem. - 2010. - Vol. 285, Is. 52. - P40891-40900, DOI 10.1074/jbc.M110.133843. - Cited References: 54. - This work was supported by the National Natural Science Foundation of China, Ministry of Science and Technology of China, CAS Research Grant, CAS Fellowship for Young International Scientists Grant, Russian Foundation for Basic Research (08-09-92209 RFBR-China joint grant), SB RAS Grant 2, "Molecular and Cell Biology" program of RAS, Bayer AG (Germany), and by the University of Georgia Research Foundation and the Georgia Research Alliance. . - ISSN 0021-9258

РУБ Biochemistry & Molecular Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
   STRUCTURAL DETERMINANTS
   RENILLA BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   CRYSTAL-STRUCTURE
   ELECTRON-DENSITY
   SOFTWARE
   PROGRAM
   BINDING
   SYSTEM
Аннотация: Forster resonance energy transfer within a protein-protein complex has previously been invoked to explain emission spectral modulation observed in several bioluminescence systems. Here we present a spatial structure of a complex of the Ca2+ regulated photoprotein clytin with its green-fluorescent protein (cgGFP) from the jellyfish Clytia gregaria, and show that it accounts for the bioluminescence properties of this system in vitro. We adopted an indirect approach of combining x-ray crystallography determined structures of the separate proteins, NMR spectroscopy, computational docking, and mutagenesis. Heteronuclear NMR spectroscopy using variously N-15, C-13, H-2-enriched proteins enabled assignment of backbone resonances of more than 94% of the residues of both proteins. In a mixture of the two proteins at millimolar concentrations, complexation was inferred from perturbations of certain H-1-N-15 HSQC-resonances, which could be mapped to those residues involved at the interaction site. A docking computation using HADDOCK was employed constrained by the sites of interaction, to deduce an overall spatial structure of the complex. Contacts within the clytin-cgGFP complex and electrostatic complementarity of interaction surfaces argued for a weak protein-protein complex. A weak affinity was also observed by isothermal titration calorimetry (K-D = 0.9 mM). Mutation of clytin residues located at the interaction site reduced the degree of protein-protein association concomitant with a loss of effectiveness of cgGFP in color-shifting the bioluminescence. It is suggested that this clytin-cgGFP structure corresponds to the transient complex previously postulated to account for the energy transfer effect of GFP in the bioluminescence of aequorin or Renilla luciferase.

Держатели документа:
[Wang, Jinfeng] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Titushin, Maxim S.
Stepanyuk, Galina A.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Lab Photobiol, Krasnoyarsk 660036, Russia
[Golz, Stefan] Bayer Schering Pharma AG, BSP GDD GTR TD GT, D-42096 Wuppertal, Germany
[Stepanyuk, Galina A.
Wang, Bi-Cheng
Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Feng, Y.G.; Stepanyuk, G.A.; Li, Y...; Markova, S.V.; Golz, S...; Wang, B.C.; Lee, J...; Wang, J.F.; Vysotski, E.S.; Liu, Z.J.

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14.

Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin [Text] / B. . van Oort [et al.] // Biochemistry. - 2009. - Vol. 48, Is. 44. - P10486-10491, DOI 10.1021/bi901436m. - Cited References: 33. - This work was supported by NATO Collaborative Linkage Grant No 979229,Grants of SB RAS and RFBR 09-04-12-022, MCB program of RAS BvO was supported by 'Stichung voor Fundamenteel Onderzock der Materic (FOM)', which is financially supported by the NWO. and by I Rubicon grant of NWO E V E was supported by Wageningen University Sandwich Ph D-Fellowship program S P L was supported by Wageningen University Sandwich Ph D.-Fellowship program, European Community Marie Curie Research Training Network MRTN-CT-2005-019481 (From FLIM to FLIN), and Computational Science Gram 635 000 014 from the netherlands Organization for Scientific Research . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   W92F OBELIN
   COELENTERAZINE
   MECHANISM
   EXPRESSION
   PROTEINS
Аннотация: Addition of calcium tons to the Ca(2+)-regulated photoproteins, such its aequorin and obelin, produces it blue bioluminescence originating from fluorescence transition of the protein-bound product coelenteramide. The kinetics of several transient fluorescent species of the bound coelenteramide is resolved after picosecond-laser excitation and streak camera detection. The Initially formed spectral distributions at picosecond-times are broad, evidently comprised of two contributions, One at higher energy (similar to 25 000 cm(-1)) assigned as from the Ca(2+)-discharged photoprotein-bound coelenteramide in its neutral state. This component decays much more rapidly (t(1/2) similar to 2 ps) in the case of the Ca(2+)-discharged obelin than aequorin (t(1/2) similar to 30 ps). The Second component at lower energy shows several intermediates in the 150-500 ps miles. with it Final species having spectral maxima 19 400 cm(-1), bound to Ca(2+)-discharged obelin. and 2 1300 cm(-1), bound to Ca(2+)-discharged aequorin, and both have it fluorescence decay lifetime of 4 ns It is proposed that the rapid kinetics of these fluorescence transients oil the picosecond time scale, correspond to times For relaxation of the protein Structural environment of the binding cavity

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[van Oort, Bart
Koehorst, Rob B. M.
Laptenok, Sergey P.
van Amerongen, Herbert] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Laptenok, Sergey P.
van Berkel, Willem J. H.
Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Koehorst, Rob B. M.
van Amerongen, Herbert
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
van Oort, B...; Eremeeva, E.V.; Koehorst, RBM; Laptenok, S.P.; van Amerongen, H...; van Berkel, WJH; Malikova, N.P.; Markova, S.V.; Vysotski, E.S.; Visser, AJWG; Lee, J...; NATO Collaborative Linkage [979229]; RFBR [09-04-12-022]; 'Stichung voor Fundamenteel Onderzock der Materic (FOM)'; NWO; Wageningen University; European Community Marie Curie Research Training Network [MRTN-CT-2005-019481]; netherlands Organization [635 000 014]

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15.

LC-MS and microscale NMR analysis of luciferin-related compounds from the bioluminescent earthworm Fridericia heliota / S. M. Marques [et al.] // Journal of Photochemistry and Photobiology B: Biology. - 2011. - Vol. 102, Is. 3. - P218-223, DOI 10.1016/j.jphotobiol.2010.12.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Fridericia heliota -- Luciferin -- Microscale NMR -- RP-HPLC-MS -- alkene -- alkyl group -- benzothiazole -- carboxylic acid -- hydroxyl group -- luciferin -- pterin -- absorption -- article -- bioluminescence -- earthworm -- Fridericia heliota -- isomer -- molecular weight -- nonhuman -- nuclear magnetic resonance -- priority journal -- reversed phase high performance liquid chromatography -- ultraviolet radiation -- Animals -- Chromatography, High Pressure Liquid -- Chromatography, Reverse-Phase -- Firefly Luciferin -- Luminescent Agents -- Magnetic Resonance Spectroscopy -- Mass Spectrometry -- Oligochaeta -- Fridericia heliota
Аннотация: This paper presents the main results of RP-HPLC-MS and microscale NMR analysis performed on Accompanying similar to Luciferin (AsLn(x)), compounds present in extracts of the bioluminescent earthworm Fridericia heliota that display similarities with Fridericia's luciferin, the substrate of the bioluminescent reaction. Three isomers of AsLn were discovered, AsLn(1), AsLn(2) and AsLn(3), all of which present a molecular weight of 529 Da. Their UV-Vis absorption spectra show maxima at 235 nm for AsLn(1), 238 and 295 nm for AsLn(2) and 241 and 295 nm for AsLn(3). MS n fragmentation patterns suggest the existence of carboxylic acid and hydroxyl moieties, and possibly chemical groups found in other luciferins like pterin or benzothiazole. The major isomer, AsLn(2), presents an aromatic ring and alkene and alkyl moieties. These luciferin-like compounds can be used as models that could give further insights into the structure of this newly discovered luciferin. В© 2010 Elsevier Inc. All rights reserved.

Scopus
Держатели документа:
Department of Chemistry and Biochemistry, Faculty of Sciences, Universidade Do Porto, Rua do Campo Alegre 687, 4169-007 Porto, Portugal
Laboratory of Photobiology, Institute of Biophysics, Russian Academy of Sciences, Akademgorodok, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Marques, S.M.; Petushkov, V.N.; Rodionova, N.S.; Esteves Da Silva, J.C.G.

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16.

Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria / V. N. Petushkov [et al.] // Journal of Physical Chemistry B. - 2003. - Vol. 107, Is. 39. - P10934-10939 . - ISSN 1520-6106
Кл.слова (ненормированные):
Bacteria -- Bioluminescence -- Chemical relaxation -- Chromophores -- Dielectric properties -- Proteins -- Solvents -- Bioluminescent bacteria -- Dimethyl ribityl lumazine -- Photobacterium leiognathi -- Riboflavin -- Ultrafast fluorescence relaxation spectroscopy -- Fluorescence
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 ?7% 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.

Scopus
Держатели документа:
MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, Netherlands
Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, Netherlands
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States
Department of Structural Biology, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk 660036, Russian Federation
IPMC, Universite de Lausanne, CH 1015 Lausanne, Switzerland : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Van Stokkum, I.H.M.; Gobets, B.; Van Mourik, F.; Lee, J.; Van Grondelle, R.; Visser, A.J.W.G.

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17.

Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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18.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931 . - ISSN 0006-2960
Кл.слова (ненормированные):
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.

Scopus
Держатели документа:
Department of Biochemistry, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Acad. of Sci. of Russia, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M.; Gibson, B.G.; Lee, J.

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19.

Analysis of polarization characteristics of plant canopies using ground-based remote sensing measurements [Text] / A. F. Sid'ko [et al.] // J. Quant. Spectrosc. Radiat. Transf. - 2014. - Vol. 144. - P117-122, DOI 10.1016/j.jqsrt.2014.03.031. - Cited References: 26 . - ISSN 0022-4073. - ISSN 1879-1352

РУБ Spectroscopy
Рубрики:
LINEAR-POLARIZATION
   AGRICULTURAL CROPS
   WHEAT CANOPIES
   LIGHT
   REFLECTANCE
   VEGETATION
Кл.слова (ненормированные):
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
Держатели документа:
[Sid'ko, A. F.
Botvich, I. Yu.
Pisman, T. I.
Shevyrnogov, A. P.] Siberian Fed Univ, RAS, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sid'ko, A.F.; Botvich, I.Y.; Pisman, T.I.; Shevyrnogov, A.P.

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20.

A Novel Type of Luciferin from the Siberian Luminous Earthworm Fridericia heliota: Structure Elucidation by Spectral Studies and Total Synthesis [Text] / V. N. Petushkov [et al.] // Angew. Chem.-Int. Edit. - 2014. - Vol. 53, Is. 22. - P5566-5568, DOI 10.1002/anie.201400529. - Cited References: 13. - We thank Dr. Alexander O. Chizhov for recording mass spectra and Dr. K. S. Mineev for NMR analysis of synthetic intermediates. We acknowledge support from the Program of the Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11. G34.31.0058), the programs MCB RAS, President of the Russian Federation "Leading science school" (grant 3951.2012.4) and the Russian Foundation for Basic Research (grant 14-03-01015). B. M. S. was supported by a stipend from the Program of the President of the Russian Federation. . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
BIOLUMINESCENT EARTHWORM
Кл.слова (ненормированные):
bioluminescence -- luciferin -- natural products -- NMR spectroscopy -- total synthesis
Аннотация: The structure elucidation and synthesis of the luciferin from the recently discovered luminous earthworm Fridericia heliota is reported. This luciferin is a key component of a novel ATP-dependent bioluminescence system. UV, fluorescence, NMR, and HRMS spectroscopy studies were performed on 0.005 mg of the isolated substance and revealed four isomeric structures that conform to spectral data. These isomers were chemically synthesized and one of them was found to produce light when reacted with a protein extract from F. heliota. The novel luciferin was found to have an unusual extensively modified peptidic nature, thus implying an unprecedented mechanism of action.

WOS
Держатели документа:
[Petushkov, Valentin N.
Rodionova, Natalja S.
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Petushkov, Valentin N.
Rodionova, Natalja S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
[Dubinnyi, Maxim A.
Tsarkova, Aleksandra S.
Baranov, Mikhail S.
Kublitski, Vadim S.
Yampolsky, Ilia V.] Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Dubinnyi, M.A.; Tsarkova, A.S.; Rodionova, N.S.; Baranov, M.S.; Kublitski, V.S.; Shimomura, O...; Yampolsky, I.V.; Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" [11. G34.31.0058]; programs MCB RAS; Russian Federation "Leading science school" [3951.2012.4]; Russian Foundation for Basic Research [14-03-01015]; Russian Federation

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