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Общее количество найденных документов : 5
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1.


   
    Fast kinetics of bioluminescent emitting species / E. V. Eremeeva [et al.] // Luminescence. - 2012. - Vol. 27, Is. 2. - P113-114. - Cited References: 4 . - ISSN 1522-7235
РУБ Biochemistry & Molecular Biology
Рубрики:
EMISSION
   OBELIN


Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Eremeeva, E. V.
Leferink, N. G. H.
Visser, A. J. W. G.
van Berkel, W. J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Leferink, N. G. H.] Univ Manchester, Manchester Interdisciplinary Bioctr, Manchester M1 7DN, Lancs, England
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Leferink, NGH; Visser, AJWG; Markova, S.V.; van Berkel, WJH; Vysotski, E.S.

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2.


   
    Spectral tuning of obelin bioluminescence by mutations of Trp92 [Text] / N. P. Malikova [et al.] // FEBS Lett. - 2003. - Vol. 554, Is. 01.02.2013. - P184-188, DOI 10.1016/S0014-5793(03)01166-9. - Cited References: 13 . - ISSN 0014-5793
РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
VIOLET BIOLUMINESCENCE
   W92F OBELIN

   AEQUORIN

   PURIFICATION

   EXPRESSION

   EMISSION

   CLONING

Кл.слова (ненормированные):
photoprotein -- aequorin -- calcium -- fluorescence
Аннотация: The Ca2+-regulated photoprotein obelin was substituted at Trp92 by His, Lys, Glu, and Arg. All mutants fold into stable conformations and produce bimodal bioluminescence spectra with enhanced contribution from a violet emission. The W92R mutant has an almost monomodal bioluminescence (lambda(max)=390 nm) and monomodal fluorescence (lambda(max)=425 nm) of the product. Results are interpreted by an excited state proton transfer mechanism involving the substituent side group and His22 in the binding cavity. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Stepanyuk, G.A.; Frank, L.A.; Markova, S.V.; Vysotski, E.S.; Lee, J...

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3.


   
    Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive [Text] / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931. - Cited References: 41 . - ISSN 0006-2960
РУБ Biochemistry & Molecular Biology
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.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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4.


   
    Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1 [Text] / V. N. Petushkov, B. G. Gibson, J. . Lee // Biochemistry. - 1996. - Vol. 35, Is. 25. - P8413-8418, DOI 10.1021/bi952691v. - Cited References: 24 . - ISSN 0006-2960
РУБ Biochemistry & Molecular Biology
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.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOLEC BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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5.


   
    Electron spectroscopy of nanodiamond surface states [Text] / P. I. Belobrov [et al.] // Appl. Surf. Sci. - 2003. - Vol. 215: 4th International Vacuum Electron Sources Conference (JUL 15-19, 2002, SARATOV, RUSSIA), Is. 01.04.2013. - P. 169-177, DOI 10.1016/S0169-4332(03)00287-3. - Cited References: 33 . - ISSN 0169-4332
РУБ Chemistry, Physical + Materials Science, Coatings & Films + Physics, Applied + Physics, Condensed Matter
Рубрики:
AUGER LINE-SHAPES
   DIAMOND 111

   GRAPHITE

   EMISSION

Кл.слова (ненормированные):
nanodiamond -- surface states -- PEELS -- XPS -- Auger electron spectroscopy
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 sp(3) 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 2.5 eV from natural diamond levels of sigma(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 sigma(s)(1)sigma(p)(2)pi(1) surface states without overlapping of pi-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. (C) 2003 Elsevier Science B.V. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, SB, Inst Biophys, Mol Architecture Grp, Krasnoyarsk 660036, Russia
Krasnoyarsk State Tech Univ, UNESCO Chair, Krasnoyarsk 660036, Russia
Univ Melbourne, Sch Phys, Parkville, Vic 3010, Australia
IV Kurchatov Atom Energy Inst, RRC, Moscow 123182, Russia
ИБФ СО РАН : 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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