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PHOTON-PHONON INTERACTION INFLUENCE ON THE EXTERNAL VIBRATION SPECTRA OF MOLECULAR CRYSTALS. / A. N. Botvich [et al.] // Physica Status Solidi (B) Basic Research. - 1986. - Vol. 134, Is. 2. - P515-522 . - ISSN 0370-1972
Кл.слова (ненормированные):
BENZENE -- PHONONS -- PHOTONS -- EXTERNAL VIBRATION SPECTRA -- M-CHLORONITROBENZENE -- MOLECULAR CRYSTALS -- PHOTON-PHONON INTERACTION -- CRYSTALS
Аннотация: A method is developed to determine the parameters of electromagnetic and elastic excitations in molecular crystals including the polariton resonance region. The dependence of eigenvectors and eigenfrequencies on the wavevector of elementary excitations is calculated numerically for m-chloronitrobenzene crystals. The conditions are found when the photon-phonon resonance effect becomes observable in the Raman scattering (RS) spectra of this crystal.

Scopus
Держатели документа:
Acad of Sciences of the USSR, Krasnoyarsk, USSR, Acad of Sciences of the USSR, Krasnoyarsk, USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Botvich, A.N.; Shabanov, V.F.; Vtyurin, A.N.; Pozdnyakova, T.A.

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Electrooptic parameters of molecular crystals: Technique of calculations / A. N. Botvich [et al.] // CONFERENCE ON LASERS AND ELECTRO-0PTICS. - 1989. - Summaries of Papers Presented at the Conference on Lasers and Electro-Optics (24 April 1989 through 28 April 1989, Baltimore, MD, USA) Conference code: 12771. - P210
Кл.слова (ненормированные):
Benzene -- Computer Simulation -- Electrooptical Effects -- Digest of Paper -- Intermolecular Distances -- Molecular Polarizability -- Molecular Crystals
Аннотация: Computer simulations of electrooptic interactions in solid molecular systems have been widely used with good effect. In these calculations molecules are usually considered point dipoles (molecule-point approximation), their parameters are taken from free molecules, and summations over the crystal lattice (lattice sums) are done by the Ewald method. Synthesis of effective new systems for electrooptic applications results in large complicated molecules much longer than the intermolecular distances in crystals. To take molecular fragmentation directly into account in this approach requires very long computing time. To simplify this problem, the molecular lattice sums are modified by dividing the molecule into fragments and calculating the lattice sums for each fragment. The results are then averaged over the weight fragment polarizabilities. This weighting coefficient is introduced to take account of the anisotropy of the molecular polarizability distribution over the molecular frame. The rest of the calculations are performed in the usual way. The method has been used to calculate linear and nonlinear optic parameters for some substituted benzene crystals with good results.

Scopus
Держатели документа:
L.V. Kirensky Inst of Phys, Krasnoyarsk, USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Botvich, A.N.; Podoprigora, V.G.; Shabanov, V.F.; Vtyurin, A.N.

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Upper electron-excited states in bioluminescence: experimental indication [Text] / N. S. Kudryasheva [et al.] // Luminescence. - 2001. - Vol. 16, Is. 3. - P. 243-246, DOI 10.1002/bio.613. - Cited References: 22 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bioluminescence -- upper electron-excited states -- energy transfer
Аннотация: The involvement of upper electron-excited states in bacterial bioluminescence process was studied with excitation energy-accepting molecules. The fluorescent aromatic compounds, anthracene and 1.4-bis(5-phenyloxazol-2-yl)benzene, were chosen. Energies of their lowest excited singlet states are higher than the energy of the analogous state of the bioluminescence emitter; their absorption spectra and bioluminescence do not overlap. Hence, the excitation of these molecules by singlet-singlet energy transfer or by light absorption is excluded. Sensitized fluorescence of these compounds in the bioluminescence systems has been recorded, indicating the activity of upper electron-excited states in the bioluminescent process. Copyright (C) 2001 John Wiley & Sons, Ltd.

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Держатели документа:
Russian Acad Sci, Inst Biophys, SB, Krasnoyarsk 660036, Russia
Novosibirsk State Tech Univ, Novosibirsk 630092, Russia
Krasnoyarsk State Univ, Dept Phys, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Nemtseva, E.V.; Meshalkin, Y.P.; Sizykh, A.G.

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Estimation of energy of the upper electron-excited states of the bacterial bioluminescent emitter [Text] / N. S. Kudryasheva [et al.] // J. Photochem. Photobiol. B-Biol. - 2002. - Vol. 68, Is. 02.03.2013. - P. 88-92, DOI 10.1016/S1011-1344(02)00360-3. - Cited References: 25 . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MECHANISM
Кл.слова (ненормированные):
bioluminescence -- electron-excited states -- energy transfer
Аннотация: The hypothesis of activity of the upper electron-excited states of the bacterial bioluminescent emitter was verified using dye molecules as foreign energy acceptors. Six compounds were selected having fluorescent state energies ranging from 25 700 to 32 000 cm(-1) (anthracene, pyrene, 1.4-bis(5-phenyloxasol-2-yl)benzene (POPOP), p-bis(o-methylstyryl)benzene (MSB), 2-methoxy-naphtalene, p-terphenyl), exceeding that of the bioluminescent emitter (22 000 cm(-1)). Their absorption spectra do not overlap with the bioluminescence spectrum; the trivial light absorption and the intermolecular resonance S-S energy transfer were excluded. Bacterial bioluminescent spectra of the coupled enzyme system NADH:FMN-oxidoreductase-luciferase in the presence of MSB were presented as an example. The weak sensitized fluorescence of MSB was registered. The results obtained have confirmed the activity of the energetic precursor in the bacterial bioluminescence. Its energy can be located in the interval of 26 000-27 000 cm(-1). (C) 2002 Published by Elsevier Science B.V.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Akademgorodok 660036, Krasnoyarsk, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660049, Russia
Wageningen Univ, Microspect Ctr, Dept Biomol Sci, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Nemtseva, E.V.; Sizykh, A.G.; Kratasyuk, V.A.; Visser, AJWG

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Volatile metabolites of higher plant crops as a photosynthesizing life support system component under temperature stress at different light intensities / I. I. Gitelson [et al.] // Advances in Space Research. - 2003. - Vol. 31, Is. 7. - P1781-1786, DOI 10.1016/S0273-1177(03)00121-2 . - ISSN 0273-1177
Кл.слова (ненормированные):
Composition -- Crops -- Heat resistance -- Metabolites -- Photosynthesis -- Volatile metabolites -- Space research -- biosphere -- article -- comparative study -- gas -- growth, development and aging -- heat -- indoor air pollution -- light -- metabolism -- microclimate -- photon -- photosynthesis -- physiology -- radiation exposure -- volatilization -- wheat -- Air Pollution, Indoor -- Environment, Controlled -- Gases -- Heat -- Life Support Systems -- Light -- Photons -- Photosynthesis -- Triticum -- Volatilization
Аннотация: The effect of elevated temperatures of 35 and 45В°C (at the intensities of photosynthetically active radiation 322, 690 and 1104 ?mol-m-2-s-1) on the photosynthesis, respiration, and qualitative and quantitative composition of the volatiles emitted by wheat (Triticum aestuvi L., cultivar 232) crops was investigated in growth chambers. Identification and quantification of more than 20 volatile compounds (terpenoids - ?-pinene, ?3 carene, limonene, benzene, ?-and transcaryophyllene, ?- and ?-terpinene, their derivatives, aromatic hydrocarbons, etc.) were conducted by gas chromatograph/mass spectrometry. Under light intensity of 1104 ?mol-m-2-s-1, heat resistance of photosynthesis and respiration increased at 35В°C and decreased at 45В°C. The action of elevated temperatures brought about variations in the rate and direction of the synthesis of volatile metabolites. The emission of volatile compounds was the greatest under a reduced irradiation of 322 ?mol-m-2-s-1 and the smallest under 1104 ?mol-m-2-s-1 at 35В°C. During the repair period, the contents and proportions of volatile compounds were different from their initial values, too. The degree of disruption and the following recovery of the functional state depended on the light intensity during the exposure to elevated temperatures. The investigation of the atmosphere of the growth chamber without plants has revaled the substances that were definitely technogenic in origin: tetramethylurea, dimethylsulfide, dibutylsulfide, dibutylphthalate, and a number of components of furan and silane nature. В© 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

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

Доп.точки доступа:
Gitelson, I.I.; Tikhomirov, A.A.; Parshina, O.V.; Ushakova, S.A.; Kalacheva, G.S.

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Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins / P. V. Natashin [et al.] // FEBS J. - 2014. - Vol. 281, Is. 5. - P1432-1445, DOI 10.1111/febs.12715 . - ISSN 1742-4658
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine, obelin -- 6 (4 hydroxyphenyl) derivative -- aequorin -- benzene derivative -- calcium ion -- hydromedusan -- mutant protein -- obelin -- oxygen -- photoprotein -- unclassified drug -- amino acid substitution -- article -- bioluminescence -- calcium transport -- crystal structure -- fluorescence -- hydrogen bond -- priority journal -- protein conformation -- protein structure -- wild type -- Coelenterata -- aequorin -- bioluminescence -- Ca2+-regulated photoprotein -- coelenterazine, obelin -- Amino Acid Substitution -- Animals -- Conserved Sequence -- Crystallography, X-Ray -- Hydrogen Bonding -- Hydrozoa -- Luminescent Proteins -- Models, Molecular -- Mutagenesis, Site-Directed -- Mutant Proteins -- Protein Conformation -- Spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.

Scopus
Держатели документа:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk 660036, Russian Federation
Laboratory of Bioluminescence Biotechnology, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Russian Federation
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States
IHuman Institute, ShanghaiTech University, Shanghai, China : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Markova, S.V.; Lee, J.; Vysotski, E.S.; Liu, Z.-J.

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Ultraviolet fluorescence of coelenteramide and coelenteramide-containing fluorescent proteins. Experimental and theoretical study / R. R. Alieva [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 162. - P318-323, DOI 10.1016/j.jphotobiol.2016.07.004 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- B3LYP -- Coelenteramide -- Discharged photoproteins -- Excitation energy -- Fluorescence -- Fluorescent protein -- Obelin
Аннотация: Coelenteramide-containing fluorescent proteins are products of bioluminescent reactions of marine coelenterates. They are called ‘discharged photoproteins’. Their light-induced fluorescence spectra are variable, depending considerably on external conditions. Current work studies a dependence of light-induced fluorescence spectra of discharged photoproteins obelin, aequorin, and clytin on excitation energy. It was demonstrated that photoexcitation to the upper electron-excited states (260–300 nm) of the discharged photoproteins initiates a fluorescence peak in the near UV region, in addition to the blue-green emission. To characterize the UV fluorescence, the light-induced fluorescence spectra of coelenteramide (CLM), fluorophore of the discharged photoproteins, were studied in methanol solution. Similar to photoproteins, the CLM spectra depended on photoexcitation energy; the additional peak (330 nm) in the near UV region was observed in CLM fluorescence at higher excitation energy (260–300 nm). Quantum chemical calculations by time depending method with B3LYP/cc-pVDZ showed that the conjugated pyrazine-phenolic fragment and benzene moiety of CLM molecule are responsible for the additional UV fluorescence peak. Quantum yields of CLM fluorescence in methanol were 0.028 ± 0.005 at 270–340 nm photoexcitation. A conclusion was made that the UV emission of CLM might contribute to the UV fluorescence of the discharged photoproteins. The study develops knowledge on internal energy transfer in biological structures – complexes of proteins with low-weight aromatic molecules. © 2016 Elsevier B.V.

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Держатели документа:
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Akademgorodok 50/38, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Alieva, R. R.; Tomilin, F. N.; Kuzubov, A. A.; Ovchinnikov, S. G.; Kudryasheva, N. S.

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