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Общее количество найденных документов : 5
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Leferink NGH, Visser AJWG, Markova S.V., van Berkel WJH, Vysotski E.S.
Заглавие : Fast kinetics of bioluminescent emitting species
Колич.характеристики :2 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2012. - Vol. 27, Is. 2. - С. 113-114. - ISSN 1522-7235
Примечания : Cited References: 4
Предметные рубрики: EMISSION
OBELIN
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Stepanyuk G.A., Frank L.A., Markova S.V., Vysotski E.S., Lee J...
Заглавие : Spectral tuning of obelin bioluminescence by mutations of Trp92
Колич.характеристики :5 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2003. - Vol. 554, Is. 01.02.2013. - С. 184-188. - ISSN 0014-5793, DOI 10.1016/S0014-5793(03)01166-9
Примечания : Cited References: 13
Предметные рубрики: VIOLET BIOLUMINESCENCE
W92F OBELIN
AEQUORIN
PURIFICATION
EXPRESSION
EMISSION
CLONING
Ключевые слова (''Своб.индексиров.''): 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.
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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) : 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) : Belobrov P.I., Bursill L.A., Maslakov K.I., Dementjev A.P.
Заглавие : Electron spectroscopy of nanodiamond surface states
Колич.характеристики :9 с
Место публикации : Appl. Surf. Sci.: ELSEVIER SCIENCE BV, 2003. - Vol. 215: 4th International Vacuum Electron Sources Conference (JUL 15-19, 2002, SARATOV, RUSSIA), Is. 01.04.2013. - P169-177. - ISSN 0169-4332, DOI 10.1016/S0169-4332(03)00287-3
Примечания : Cited References: 33
Предметные рубрики: AUGER LINE-SHAPES
DIAMOND 111
GRAPHITE
EMISSION
Ключевые слова (''Своб.индексиров.''): 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
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