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Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species [Text] / E. S. Vysotski [et al.] // Biochemistry. - 2003. - Vol. 42, Is. 20. - P6013-6024, DOI 10.1021/bi027258h. - Cited References: 45 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CALCIUM
   LUMINESCENCE
   LONGISSIMA
   EVOLUTION
   PROTEINS
   COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA USA
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia
Univ Washington, Friday Harbor Labs, Seattle, WA 98195 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Liu, Z.J.; Markova, S.V.; Blinks, J.R.; Deng, L...; Frank, L.A.; Herko, M...; Malikova, N.P.; Rose, J.P.; Wang, B.C.; Lee, J...

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Variation of Spectral Characteristics of Coelenteramide-Containing Fluorescent Protein from Obelia Longissima Exposed to Dimethyl Sulfoxide / A. S. Petrova [et al.] // Russ. Phys. J. - 2016. - Vol. 59, Is. 4. - P562-567, DOI 10.1007/s11182-016-0806-8. - Cited References:33. - This work was supported in part by the Russian Science Foundation (Contract No. 14-14-00076). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
fluorescent coelenteramide-containing fluorescent proteins -- discharged -- obelin -- proton transfer -- dimethyl sulfoxide
Аннотация: Effect of dimethyl sulfoxide (DMSO), a widespread biomedical agent, on spectral-luminescent characteristics of coelenteramide-containing fluorescent protein - discharged obelin - is investigated. Contributions of violet and blue-green spectral components to fluorescence of discharged obelin are elucidated and characterized at different photoexcitation energies. Dependences of these contributions on the DMSO concentration are presented. Spectral changes are related to the destructive effect of DMSO on fluorescent protein and decreasing efficiency of proton transfer to electronically excited states of fluorophore.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Krasnoyarsk State Agrarian Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Petrova, A. S.; Alieva, R. R.; Belogurova, N. V.; Tirranen, L. S.; Kudryasheva, N. S.; Russian Science Foundation [14-14-00076]

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Variability of fluorescence spectra of coelenteramide-containing proteins as a basis for toxicity monitoring / R. R. Alieva, N. S. Kudryasheva // Talanta. - 2017. - Vol. 170. - P425-431, DOI 10.1016/j.talanta.2017.04.043 . - ISSN 0039-9140
Кл.слова (ненормированные):
Coelenteramide-containing fluorescent protein -- Multicolor fluorescent bioassay -- Obelin -- Primary photochemical process -- Protein destruction -- Proton transfer -- Bioassay -- Biomarkers -- Excited states -- Fluorescence -- Fluorophores -- Ionizing radiation -- Proton transfer -- Toxicity -- Electron-excited state -- Fluorescence spectra -- Fluorescent protein -- Green fluorescent protein -- Obelin -- Photochemical process -- Photochemical properties -- Physicochemical process -- Proteins
Аннотация: Nowadays, physicochemical approach to understanding toxic effects remains underdeveloped. A proper development of such mode would be concerned with simplest bioassay systems. Coelenteramide-Containing Fluorescent Proteins (CLM-CFPs) can serve as proper tools for study primary physicochemical processes in organisms under external exposures. CLM-CFPs are products of bioluminescent reactions of marine coelenterates. As opposed to Green Fluorescent Proteins, the CLM-CFPs are not widely applied in biomedical research, and their potential as colored biomarkers is undervalued now. Coelenteramide, fluorophore of CLM-CFPs, is a photochemically active molecule; it acts as a proton donor in its electron-excited states, generating several forms of different fluorescent state energy and, hence, different fluorescence color, from violet to green. Contributions of the forms to the visible fluorescence depend on the coelenteramide microenvironment in proteins. Hence, CLM-CFPs can serve as fluorescence biomarkers with color differentiation to monitor results of destructive biomolecule exposures. The paper reviews experimental and theoretical studies of spectral-luminescent and photochemical properties of CLM-CFPs, as well as their variation under different exposures – chemicals, temperature, and ionizing radiation. Application of CLM-CFPs as toxicity bioassays of a new type is justified. © 2017

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Alieva, R. R.; Kudryasheva, N. S.

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Using DCMU-fluorescence method for the identification of dominant phytoplankton groups [Text] / N. A. Gaevsky [et al.] // J. Appl. Phycol. - 2005. - Vol. 17, Is. 6. - P. 483-494, DOI 10.1007/s10811-005-2903-x. - Cited References: 28 . - ISSN 0921-8971

РУБ Biotechnology & Applied Microbiology + Marine & Freshwater Biology
Рубрики:
IN-VIVO
   CHLOROPHYLL FLUORESCENCE
   FLUOROMETRIC METHOD
   SITU
   PHOTOSYNTHESIS
   CYANOBACTERIA
   ALGAE
   EVOLUTION
   CULTURES
   LAKES
Кл.слова (ненормированные):
algae -- chlorophyll -- fluorescence -- vizualization
Аннотация: For the identification of ecologically significant dominant groups of phytoplanktonic algae a polychromatic DCMU-induced fluorescence method is recommended. A special fluorometer equipped with a system of replaceable filters is used to differentiate three regions of the spectrum (410 +/- 20, 510 +/- 20 and 540 +/- 10 nm) that can excite the basic light-harvesting pigments. Total and differential (for every algal taxon studied) chlorophyll a calculated from the fluorescence signals is in good agreement with biomass estimates from direct cell counts for several different trophic types of aquatic systems. This is made possible by the vizualization of the ratios of fluorescence signal values in their own coordinates: first, to decide whether it is necessary to correct linear equations in order to eliminate negative solutions; second, to determine the possibility of nulling the negative solution if a point is situated close to a side of the triangle; and third, to reduce the number of linear algebraic equations to two if the points are situated along one of the triangle sides or to one if the points are gathered at the apex. The polychromatic DCMU-induced fluorescence method can be used for monitoring natural phytoplankton populations to detect changes in their taxonomic structure.

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Держатели документа:
Krasnoyarsk State Univ, Dept Biol, Krasnoyarsk, Russia
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gaevsky, N.A.; Kolmakov, V.I.; Anishchenko, O.V.; Gorbaneva, T.B.

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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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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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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.

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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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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria [Text] / V. N. Petushkov [et al.] // J. Phys. Chem. B. - 2003. - Vol. 107, Is. 39. - P. 10934-10939, DOI 10.1021/jp034266e. - Cited References: 52 . - ISSN 1520-6106

РУБ Chemistry, Physical
Рубрики:
TIME-RESOLVED FLUORESCENCE
   VIBRIO-FISCHERI Y1
   FEMTOSECOND SOLVATION DYNAMICS
   FLAVIN ADENINE-DINUCLEOTIDE
   PHOTOBACTERIUM-LEIOGNATHI
   BIOLOGICAL WATER
   SOLVENT DYNAMICS
   DIELECTRIC-RELAXATION
   MOLECULAR-DYNAMICS
   TRYPTOPHAN
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 similar to7% 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.

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Держатели документа:
Univ Wageningen & Res Ctr, Biochem & Biophys Lab, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
Vrije Univ Amsterdam, Fac Sci & Engn, Dept Phys & Astron, NL-1081 HV Amsterdam, Netherlands
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Vrije Univ Amsterdam, Fac Earth & Life Sci, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; van Stokkum, IHM; Gobets, B...; van Mourik, F...; Lee, J...; van Grondelle, R...; Visser, AJWG

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Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa / M. D. Larionova, S. V. Markova, E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P503-510, DOI 10.1111/php.12694. - Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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10.

Traces of the Tunguska Event (1908) in Sediments of Zapovednoe Lake Based on SR–XRF Data / A. V. Darin, D. Y. Rogozin, A. V. Meydus [et al.] // Dokl. Earth Sci. - 2020. - Vol. 492, Is. 2. - P442-445, DOI 10.1134/S1028334X20060045 . - ISSN 1028-334X
Кл.слова (ненормированные):
lake sediments -- microelements -- synchrotron radiation (SR) -- Tunguska event 1908 -- X-ray fluorescent analysis (XRF) -- Catchments -- Chemical elements -- Fluorescence spectroscopy -- Lakes -- Synchrotron radiation -- Bottom sediments -- Extraterrestrial origin -- Micro-particles -- Sediment core -- Synchrotron radiation X-ray fluorescence -- Tunguska -- Water catchment -- Sediments -- chemical element -- explosion -- lacustrine deposit -- radionuclide -- sediment core -- terrigenous deposit -- wildfire -- Russian Federation -- Tunguska
Аннотация: Abstract: An anomalous layer enriched with chemical elements indicating the presence of terrigenous matter was discovered in the sediment core of Zapovednoe Lake located 60 km from the epicenter of the Tunguska event (1908) using synchrotron radiation X-ray fluorescence spectroscopy (SR–XRF). Radioisotope measurements indicate that the age of the layer is consistent with the date of the catastrophe. Apparently, the anomalous layer was formed as a result of an intense terrigenous matter inflow from the water catchment area due to massive forest falls and subsequent wildfires caused by the Tunguska event. Thus, it is established that targeted searches for microparticles of extraterrestrial origin can be carried out in the discovered and dated anomalous bottom sediment layer. © 2020, Pleiades Publishing, Ltd.

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Держатели документа:
Sobolev Institute of Geology and Mineralogy, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Tungusskii State Nature Reserve, Krasnoyarsk, 648490, Russian Federation
Budker Institute of Nuclear Physics, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation
Kurchatov Institute National Research Center, Moscow, 123182, Russian Federation

Доп.точки доступа:
Darin, A. V.; Rogozin, D. Y.; Meydus, A. V.; Babich, V. V.; Kalugin, I. A.; Markovich, T. I.; Rakshun, Y. V.; Darin, F. A.; Sorokoletov, D. S.; Gogin, A. A.; Senin, R. A.; Degermendzhi, A. G.

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11.

Traces of the Tunguska Event (1908) in Sediments of Zapovednoe Lake Based on SR-XRF Data / A. V. Darin, D. Y. Rogozin, A. V. Meydus [et al.] // Dokl. Earth Sci. - 2020. - Vol. 492, Is. 2. - P442-445, DOI 10.1134/S1028334X20060045. - Cited References:10. - This study was performed as a part of a State Assignment of the Institute of Geology and Mineralogy, Siberian Branch, Russian Academy of Sciences, and supported by the Russian Foundation for Basic Research, project nos. 19-04-00320 and 19-05-50046. This study was per-formed in the Shared Research Center "Siberian Synchrotron and Terahertz Radiation Center" on the basis of the VEPP-4-VEPP-2000 Electron-Positron Collider Complex of the Institute of Nuclear Physics, Siberian Branch, Russian Academy of Sciences, using equipment supported by project no. RFMEFI62119X0022. . - ISSN 1028-334X. - ISSN 1531-8354

РУБ Geosciences, Multidisciplinary

Кл.слова (ненормированные):
Tunguska event 1908 -- lake sediments -- X-ray fluorescent analysis (XRF) -- synchrotron radiation (SR) -- microelements
Аннотация: An anomalous layer enriched with chemical elements indicating the presence of terrigenous matter was discovered in the sediment core of Zapovednoe Lake located 60 km from the epicenter of the Tunguska event (1908) using synchrotron radiation X-ray fluorescence spectroscopy (SR-XRF). Radioisotope measurements indicate that the age of the layer is consistent with the date of the catastrophe. Apparently, the anomalous layer was formed as a result of an intense terrigenous matter inflow from the water catchment area due to massive forest falls and subsequent wildfires caused by the Tunguska event. Thus, it is established that targeted searches for microparticles of extraterrestrial origin can be carried out in the discovered and dated anomalous bottom sediment layer.

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Держатели документа:
Russian Acad Sci, Sobolev Inst Geol & Mineral, Siberian Branch, Novosibirsk 630090, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Tungusskii State Nat Reserve, Krasnoyarsk 648490, Russia.
Russian Acad Sci, Budker Inst Nucl Phys, Siberian Branch, Novosibirsk 630090, Russia.
Kurchatov Inst Natl Res Ctr, Moscow 123182, Russia.

Доп.точки доступа:
Darin, A., V; Rogozin, D. Yu; Meydus, A., V; Babich, V. V.; Kalugin, I. A.; Markovich, T., I; Rakshun, Ya, V; Darin, F. A.; Sorokoletov, D. S.; Gogin, A. A.; Senin, R. A.; Degermendzhi, A. G.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-04-00320, 19-05-50046]; Institute of Nuclear Physics, Siberian Branch, Russian Academy of SciencesRussian Academy of Sciences [RFMEFI62119X0022]

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12.

Tolerance of wheat and lettuce plants grown on human mineralized waste to high temperature stress / S. A. Ushakova [et al.] // Advances in Space Research. - 2013. - Vol. 51, Is. 11. - P2075-2083, DOI 10.1016/j.asr.2013.01.017 . - ISSN 0273-1177
Кл.слова (ненормированные):
Air temperature step -- BLSS -- Heat resistance -- Human waste recycling -- Lettuce -- Wheat -- Air temperature -- BLSS -- Human waste -- Lettuce -- Wheat -- Atmospheric temperature -- Electromagnetic field effects -- Electromagnetic fields -- Gas plants -- Heat resistance -- Oxygen supply -- Plants (botany) -- Productivity -- Specific heat -- Thermal stress -- Waste utilization -- Plant shutdowns
Аннотация: The main objective of a life support system for space missions is to supply a crew with food, water and oxygen, and to eliminate their wastes. The ultimate goal is to achieve the highest degree of closure of the system using controlled processes offering a high level of reliability and flexibility. Enhancement of closure of a biological life support system (BLSS) that includes plants relies on increased regeneration of plant waste, and utilization of solid and liquid human wastes. Clearly, the robustness of a BLSS subjected to stress will be substantially determined by the robustness of the plant components of the phototrophic unit. The aim of the present work was to estimate the heat resistance of two plants (wheat and lettuce) grown on human wastes. Human exometabolites mineralized by hydrogen peroxide in an electromagnetic field were used to make a nutrient solution for the plants. We looked for a possible increase in the heat tolerance of the wheat plants using changes in photosynthetically active radiation (PAR) intensity during heat stress. At age 15 days, plants were subjected to a rise in air temperature (from 23 В± 1 В°C to 44 В± 1 В°) under different PAR intensities for 4 h. The status of the photosynthetic apparatus of the plants was assessed by external 2 gas exchange and fluorescence measurements. The increased irradiance of the plants during the high temperature period demonstrated its protective action for both the photosynthetic apparatus of the leaves and subsequent plant growth and development. The productivity of the plants subjected to temperature changes at 250 W m-2 of PAR did not differ from that of controls, whereas the productivity of the plants subjected to the same heat stress but in darkness was halved. В© 2012 COSPAR. Published by Elsevier Ltd.

Scopus
Держатели документа:
SB RAS Institute of Biophysics, 660036 Akademgorodok, Krasnoyarsk, Russian Federation
Institut Pascal, GEPB, UBP, Clermont Universite, F-63000 Clermont-Ferrand, France
UB RAS, Institute of Biology of Komi Science Center, Syktyvkar, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Ushakova, S.A.; Tikhomirov, A.A.; Shikhov, V.N.; Gros, J.-B.; Golovko, T.K.; Dal'Ke, I.V.; Zakhozhii, I.G.

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13.

Tolerance of plants grown on human mineralized waste to changes in air temperature / A. A. Tikhomirov [et al.] // International Astronautical Federation - 59th International Astronautical Congress 2008, IAC 2008. - 2008. - Vol. 1: 59th International Astronautical Congress 2008, IAC 2008 (29 September 2008 through 3 October 2008, Glasgow) Conference code: 79748. - P311-320
Кл.слова (ненормированные):
Air temperature -- Alternating electromagnetic field -- Biological life support systems -- Closedness -- Controlled process -- Fluorescence measurements -- Gas exchange -- Heat stress -- High temperature -- Human waste -- Nutrient solution -- Old plants -- Photosynthetic apparatus -- Photosynthetically active radiation -- Plant components -- Plant growth -- Plant wastes -- Protective action -- Reproductive organs -- Temperature changes -- Temperature conditions -- Atmospheric temperature -- Electromagnetic field effects -- Electromagnetic fields -- Gas plants -- Heat resistance -- Hydrogen peroxide -- Oxygen supply -- Plant life extension -- Productivity -- Specific heat -- Thermal stress -- Waste utilization -- Plant shutdowns
Аннотация: The main objective of an LSS is to supply a crew with food, water and oxygen, and to eliminate its waste. The ultimate goal is to achieve the highest degree of closure of the system using controlled processes offering a high level of reliability and flexibility. Enhancement of closedness of biological life support systems (BLSS) including plants relies on increased regeneration of gas, water and plant waste, and utilization of solid and liquid human wastes. Clearly, the robustness of an LSS subjected to stress will be substantially determined by the robustness of the plant components of the phototrophic unit. The aim of the present work was to estimate the heat resistance of plants grown on human wastes. Human exometabolites mineralized by hydrogen peroxide in an alternating electromagnetic field were used to make a nutrient solution for the plants. We looked for a possible increase in the heat resistance of the plants using changes in photosynthetically active radiation (PAR) intensity during heat stress. At ages 15 and 25 days, plants were subjected to a rise in air temperature (from 22-24В°C to 44В°C) under different PAR intensities for 4 hours. The status of the photosynthetic apparatus of the plants was assessed by external CO2 gas exchange and fluorescence measurements. The increased irradiance of the plants during the high temperature period demonstrated its protective action for both the photosynthetic apparatus of the leaves and subsequent plant growth and development. The productivity of the plants subjected to temperature changes at 250 W/m2 of PAR did not differ from that of controls, whereas the productivity of the plants subjected to the same heat stress but in darkness was halved. The heat resistance of the reproductive organs of 25-day-old plants was significantly lower than that of 15-day-old plants subjected to similar light and temperature conditions.

Scopus
Держатели документа:
SB RAS Institute of Biophysics, 660036, Akademgorodok, Krasnoyarsk, Russian Federation
LGCB, Universite Blaise Pascal, Clermont-Ferrand, France
Institute of Biology Komi SC of UrB RAS, Syktyvkar, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tikhomirov, A.A.; Ushakova, S.A.; Shikhov, V.N.; Gros, J.-B.; Golovko, T.K.; Dal'Ke, I.V.; Zakhozhii, I.G.

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14.

Thermoinduction of chlorophyll fluorescence and the age-related condition of higher plant leaves / T. V. Nesterenko, V. N. Shikhov, A. A. Tikhomiro // Russian Journal of Plant Physiology. - 2001. - Vol. 48, Is. 2. - P244-251, DOI 10.1023/A:1009016520582 . - ISSN 1021-4437
Кл.слова (ненормированные):
Development -- Leaf -- Thermoinduction of chlorophyll fluorescence -- Cucumis -- Cucumis sativus -- Embryophyta -- Lycopersicon esculentum -- Sativum -- Triticum aestivum
Аннотация: The age-related changes in the temperature dependence curves (TDC) of chlorophyll fluorescence were studied in leaf segments of wheat (Triticum aestivum L.), tomato (Lycopersicum esculentum Mill.), and cucumber (Cucumis sativum L.) plants grown under controlled photoculture conditions. Three major TDC patterns of chlorophyll fluorescence were identified within the temperature range of 25-70В°C, with each of the patterns corresponding to a certain phase of leaf development. The transition from one type of thermogram to another was a gradual and ordered process. The magnitude of the low-temperature TDC peak increased until leaves completely expanded and declined with leaf senescence. In the course of leaf senescence, the thermograms exhibited an additional shoulder, which further changed into a peak at 55-65В°C with increasing magnitude. Our data provide the basis for assessing leaf age from the type of chlorophyll fluorescence thermogram and the changes in the particular indices characteristic of TDC of chlorophyll fluorescence.

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

Доп.точки доступа:
Nesterenko, T.V.; Shikhov, V.N.; Tikhomiro, A.A.

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15.

Thermoinduction of chlorophyll fluorescence and the age-related condition of higher plant leaves [Text] / T. V. Nesterenko, V. N. Shikhov, A. A. Tikhomirov // Russ. J. Plant Physiol. - 2001. - Vol. 48, Is. 2. - P. 244-251, DOI 10.1023/A:1009016520582. - Cited References: 27 . - ISSN 1021-4437

РУБ Plant Sciences

Кл.слова (ненормированные):
thermoinduction of chlorophyll fluorescence -- leaf -- development
Аннотация: The age-related changes in the temperature dependence curves (TDC) of chlorophyll fluorescence were studied in leaf segments of wheat (Triticum aestivum L.), tomato (Lycopersicum esculentum Mill.), and cucumber (Cucumis sativum L.) plants grown under controlled photoculture conditions. Three major TDC patterns of chlorophyll fluorescence were identified within the temperature range of 25-70 degreesC, with each of the patterns corresponding to a certain phase of leaf development. The transition from one type of thermogram to another was a gradual and ordered process. The magnitude of the low-temperature TDC peak increased until leaves completely expanded and declined with leaf senescence. In the course of leaf senescence, the thermograms exhibited an additional shoulder, which further changed into a peak at 55-65 degreesC with increasing magnitude. Our data provide the basis for assessing leaf age from the type of chlorophyll fluorescence thermogram and the changes in the particular indices characteristic of TDC of chlorophyll fluorescence.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Nesterenko, T.V.; Shikhov, V.N.; Tikhomirov, A.A.

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16.

The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - P774-779, DOI 10.1006/bbrc.1995.1880 . - ISSN 0006-291X
Кл.слова (ненормированные):
riboflavin -- article -- bioluminescence -- fluorescence -- nonhuman -- priority journal -- protein analysis -- protein synthesis -- vibrio -- vibrionaceae -- Bacterial Proteins -- Chromatography, Gel -- Chromatography, Thin Layer -- Flavin Mononucleotide -- Flavoproteins -- Luminescence -- Riboflavin -- Spectrometry, Fluorescence -- Support, U.S. Gov't, P.H.S. -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Vibrio -- Vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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17.

THE LOCALIZATION OF LUMINESCENT SYSTEM OF LUMINOUS BACTERIA [Текст] / O. A. KUDRYAVTSEVA [и др.] // Biofizika. - 1993. - Vol. 38, Is. 3. - P. 435-439. - Cited References: 10 . - ISSN 0006-3029

РУБ Biophysics

Аннотация: A method for localization of a light source near the interface of two media is described. The method is based on an optical analog of tunnel effect when the radiation source is at the distance smaller than the wavelength from the interface. Application of the tunnel effect permits to obtain high resolution. The developed method was used to determine the localization of a bacterial luminescent system. It has been found that the sources of bioluminescence are located at thin subsurfase lager with width about 70 nm. This result is in favour of the peripheral (periplasmatic or membrane) localization of the bacterial luminescent system. This method makes it possible to investigate processes pelated to light radiation (luminescence, fluorescence and other optical processes) in a thin surface layer of various biological and physical objects.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
KUDRYAVTSEVA, O.A.; BARTSEV, S.I.; OKHONIN, V.A.; MEZHEVIKIN, V.V.

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18.

The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein / S. V. Markova [et al.] // FEBS J. - 2012. - Vol. 279, Is. 5. - P856-870, DOI 10.1111/j.1742-4658.2012.08476.x. - Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany). . - ISSN 1742-464X

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   C-TERMINAL PROLINE
   SEQUENCE-ANALYSIS
   MNEMIOPSIS-SP
   COELENTERAZINE-BINDING
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURES
   EXCITED-STATE
   CDNA CLONING
Кл.слова (ненормированные):
bioluminescence -- calcium -- coelenterazine -- luciferase -- mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Malikova, Natalia P.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Dept Biophys, Krasnoyarsk, Russia
[Golz, Stefan] Bayer Pharma AG, Global Drug Discovery, Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Golz, S...; Malikova, N.P.; Frank, L.A.; Vysotski, E.S.

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19.

The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding [Text] / E. V. Eremeeva [et al.] // FEBS Lett. - 2009. - Vol. 583, Is. 12. - P1939-1944, DOI 10.1016/j.febslet.2009.04.043. - Cited References: 28. - We thank Prof. John Lee for valuable suggestions and providing constructive criticisms. The work was supported by Wageningen University Sandwich PhD-Fellowship Program, Grants 02.512.12. 2006 and 1211.2008.4 of Ministry of Education and Science of Russian Federation, MCB Program of RAS, and by Grant No. 2 of SB RAS. . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
CRYSTAL-STRUCTURE
   CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   CALCIUM
   REGENERATION
   APOAEQUORIN
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Photoprotein -- Trp fluorescence
Аннотация: The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Westphal, Adrie H.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Westphal, A.H.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.; Wageningen University Sandwich PhD-Fellowship Program [02.512.12. 2006]; Ministry of Education and Science of Russian Federation, MCB Program of RAS [1211.2008.4]; SB RAS

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20.

The fluorescence method for determining of photosynthetic apparatus reactivity in plant leaves / T. V. Nesterenko, V. N. Shikhov, A. A. Tikhomirov // Zhurnal Obshchei Biol. - 2019. - Vol. 80, Is. 3. - С. 187-199, DOI 10.1134/S0044459619030060. - Cited References:31 . - ISSN 0044-4596

РУБ Biology
Рубрики:
ELECTRIC-POTENTIAL DIFFERENCE
FREQUENTLY ASKED QUESTIONS
CHLOROPHYLL
Аннотация: Presently, the most promising way of studying, forecasting, and enhancing of organisms' tolerance to harsh environmental impacts is considered to be the estimation of initial functional state of an organism's regulatory systems. To resolve the problem of photosynthetic apparatus (PSA) tolerance to harsh impacts at the level of such a complicated functional system as a plant leaf, it is necessary to assess integral responses of the leaf's PSA to the impact. At that, simple and versatile traits may have certain advantages. At present, chlorophyll fluorescence seems to be one of the main indices of PSA activity, which can be measured relatively fast and easy. One of the possible approaches to operational integrative assessment of PSA activity may consist in usage of the parameters introduced for the curves of chlorophyll fluorescence induction (CFI) slow phase. Temporal patterns of CFI are of special interest. The simplest index T-0.5 (i.e., half-time of chlorophyll fluorescence intensity decrease during the slow phase of CFI) appears to be an integral characteristic of activation rate with regard to a number of photo-assimilation and photo-protective processes in leaves. On basis of the studies, conducted earlier, and published data, we have analyzed the behavior of T-0.5 parameter with comparison to other CFI traits (namely: qN - non-photochemical quenching coefficient, ETR - electron transport rate, Phi(PSII) - effective quantum yield of PSII photochemistry, F-p/F-T ratio) under different conditions. The influence of leaf senescence, changes in intensity of excitation light, slight dehydration of plants and their recovery from water deficiency have been examined. The pattern of T-0.5 behavior, observed in laboratory experiments, and the results of its comparison with other indices of CFI give occasion to propose the usage of T-0.5 for indirect estimation of PSA activity when operational integrative monitoring of PSA state is required. Further studies are necessary for establishing quantitative relationships between PSA activity and fluorescence parameter T-0.5 under specific stress conditions.

WOS,
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Держатели документа:
RAS, Siberian Branch, Inst Biophys, Acad Gorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Nesterenko, T. V.; Shikhov, V. N.; Tikhomirov, A. A.

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