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INDUCTION OF FLUORESCENCE IN WHEAT LEAVES DURING THEIR ONTOGENESIS [Text] / T. V. NESTERENKO, F. Y. SIDKO // SOVIET PLANT PHYSIOLOGY. - 1980. - Vol. 27, Is. 2. - P. 262-266. - Cited References: 14 . - ISSN 0038-5719

РУБ Plant Sciences

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
NESTERENKO, T.V.; SIDKO, F.Y.

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CHLOROPHYLL INDUCTION FLUORESCENCE AND CERTAIN CHARACTERISTICS OF CUCUMBER LEAVES GROWN UNDER ACTION OF LIGHT OF VARIOUS SPECTRAL CONTENT AND INTENSITIES [Текст] / T. V. NESTERENKO [и др.] // FIZIOLOGIYA I BIOKHIMIYA KULTURNYKH RASTENII. - 1985. - Vol. 17, Is. 1. - P. 11-16. - Cited References: 15 . - ISSN 0256-1425

РУБ Plant Sciences + Horticulture

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
NESTERENKO, T.V.; TIKHOMIROV, A.A.; ZOLOTUKHIN, I.G.; VOLKOVA, E.K.

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AGE-CHANGES OF SLOW FLUORESCENCE INDUCTION IN WHEAT LEAF CHLOROPHYLL [Text] / T. V. NESTERENKO, F. Y. SIDKO // SOVIET PLANT PHYSIOLOGY. - 1985. - Vol. 32, Is. 3. - P. 344-350. - Cited References: 27 . - ISSN 0038-5719

SLOW INDUCTION OF CHLOROPHYLL FLUORESCENCE IN CUCUMBER LEAF ONTOGENY [Text] / T. V. NESTERENKO, F. Y. SIDKO // SOVIET PLANT PHYSIOLOGY. - 1986. - Vol. 33, Is. 4. - P. 514-522. - Cited References: 17 . - ISSN 0038-5719

PREDICTIONS OF NATURAL PHYTOPLANKTON STATE USING THE FLUORESCENCE METHOD [Текст] / A. J. BOLSUNOVSKII [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1987. - Vol. 297, Is. 6. - С. 1509-1511. - Cited References: 6 . - 3. - ISSN 0002-3264

РУБ Multidisciplinary Sciences

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BOLSUNOVSKII, A.J.; TERSKOV, I.A.; SIDKO, F.J.; SHUR, L.A.; APONASENKO, A.D.

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PREDICTIONS OF NATURAL PHYTOPLANKTON STATE USING THE FLUORESCENCE METHOD [Текст] / A. J. BOLSUNOVSKII [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1987. - Vol. 297, Is. 6. - P. 1509-1511. - Cited References: 6 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BOLSUNOVSKII, A.J.; TERSKOV, I.A.; SIDKO, F.J.; SHUR, L.A.; APONASENKO, A.D.

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PHYTOPLANKTON CHLOROPHYLL FLUORESCENCE WITH RESPECT TO ILLUMINANCE CONDITIONS [Текст] / F. Y. SIDKO, A. D. APONASENKO, L. A. BALAKCHINA // Okeanologiya. - 1989. - Vol. 29, Is. 1. - P. 127-131. - Cited References: 8 . - ISSN 0030-1574

РУБ Oceanography

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
SIDKO, F.Y.; APONASENKO, A.D.; BALAKCHINA, L.A.

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ESTIMATION OF THE INTENSITY OF PHYTOPLANKTON CHLOROPHYLL FLUORESCENCE EXCITED BY SOLAR-RADIATION [Text] / F. Y. SIDKO [et al.] // SOVIET JOURNAL OF REMOTE SENSING. - 1990. - Vol. 8, Is. 2. - P205-212. - Cited References: 10 . - 8. - ISSN 0275-911X

РУБ Geography + Geology + Remote Sensing + Imaging Science & Photographic Technology
Рубрики:
OCEAN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
SIDKO, F.Y.; APONASENKO, A.D.; SIDKO, A.F.; LOPATIN, V.N.

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Isolation and comparative studies of two fluorescent flavoproteins of luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biofizika. - 1990. - Vol. 35, Is. 2. - С. 368-370 . - ISSN 0006-3029
Кл.слова (ненормированные):
flavoprotein -- fluorescence -- letter -- nonhuman -- Photobacterium leiognathi

Scopus
Держатели документа:
Institute of Biological Physics, Siberian Branch, Academy of Sciences of the USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Raibekas, A.A.; Petushkov, V.N.

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10.

PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA [Text] / V. S. BONDAR, K. P. TROFIMOV, E. S. VYSOTSKII // Biochem.-Moscow. - 1992. - Vol. 57, Is. 10. - P1020-1027. - Cited References: 36 . - 8. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   BEROE-OVATA
   AEQUORIN
   CA-2+
   INDICATORS
   PROTEIN
   BINDING
   PURIFICATION
   EXTRACTION
Кл.слова (ненормированные):
BIOLUMINESCENCE -- CA2+-ACTIVATED PHOTOPROTEIN -- OBELIN -- CHROMATOGRAPHY -- CALCIUM
Аннотация: The photoprotein obelin was isolated and purified to homogeneity (as indicated by sodium dodecyl sulfate polyacrylamide gel electrophoresis) from hydroids of Obelia longissima by gel filtration on Sephadex G-75 fine, ion exchange chromatography on Polysil CA-300 (10 mum), hydrophobic chromatography on Phenyl-Sepharose CL-4B, gel filtration on Sephacryl S-200 superfine, ion exchange chromatography on a Mono Q column at pH 7.0, chromatofocusing on a Mono P column (pH gradient 6.0-4.0), and ion exchange chromatography on a Mono Q column at pH 5.5, 8.8, and 7.0. The molecular weight of the native protein was 30 kD, and that measured in the presence of SDS was 19.8 kD. The specific activity of obelin is 4.9.10(15) quanta/mg protein, pseudo-first-order constant of bioluminescence decay 4 sec-1, and quantum yield 0.16 The range of measurable Ca2+ concentrations is 10(-7) to 10(-5) M. The luminescence spectrum of obelin peaks at 469 nm, and the fluorescence emission maximum of the discharged protein is at 455 nm. The optimum pH for luminescence is between 9.0 and 10.5. The molecular ionization constants are pK1 6.8 and pK2 12.2, and the ionization constants for the active site are pK1 9.1 and pK2 10.2
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; TROFIMOV, K.P.; VYSOTSKII, E.S.

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11.

THE ECOLOGICAL BIOPHYSICS AND ITS PART IN INVESTIGATION OF AQUATIC ECOSYSTEMS [Текст] / I. I. GITELSON [и др.] // Biofizika. - 1993. - Vol. 38, Is. 6. - С. 1069-1078. - Cited References: 11 . - 10. - ISSN 0006-3029

РУБ Biophysics
Рубрики:
SEASONAL DYNAMICS
RESERVOIR
BAY
Аннотация: The notion of ecological biophysics as a scientific discipline investigating physical processes and phenomena caused by functioning of the living super-organism systems is formulated. The three main constituents of the ecological biophysics are defined: elaboration of the monitoring methods of the basis of sensing of the biophysical fields (of bioluminescence and fluorescence), mathematical and physical modeling and investigation of the part of living organisms in the hydrophysical processes of the ecosystem scale. Examples of realization of the ecological biophysical approach in the process of investigations of the World Ocean, Lake Baikal, the reservoirs of Dnieper and Yenisei revers are given.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GITELSON, I.I.; GLADYSHEV, M.I.; DEGERMENDZHY, A.G.; LEVIN, L.A.; SIDKO, F.Y.

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12.

Ecological biophysics and its role in study of aquatic ecosystems / I. I. Gitel'zon [et al.] // Biophysics. - 1993. - Vol. 38, Is. 6. - P1099-1108 . - ISSN 0006-3509
Аннотация: A concept is formulated on ecological and biophysics as a scientific discipline which studies physical processes and phenomena resulting from the functioning of live supra-organism systems. Three main directions of ecological biophysics are defined: creation of methods of monitoring ecosystems on the basis of probing biophysical fields (fields of bioluminescence and fluorescence); mathematical and physical modelling; and study of the role of live organisms in hydrophysical processes on the ecosystem scale. Examples are given of the realization of the ecologo-biophysical approach in research into the ecosystems of the world ocean, Lake Baikal and the Dnieper and Yenisei reservoirs. В© 1994.

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

Доп.точки доступа:
Gitel'zon, I.I.; Gladyshev, M.I.; Degermendzhi, A.G.; Levin, L.A.; Sid'ko, F.Ya.

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13.

QUANTITATIVE DESCRIPTION OF SLOW INDUCTION OF CHLOROPHYLL FLUORESCENCE DURING ONTOGENY OF HIGHER-PLANT LEAVES [Text] / T. V. NESTERENKO, F. Y. SIDKO // RUSSIAN PLANT PHYSIOLOGY. - 1993. - Vol. 40, Is. 1. - P. 5-10. - Cited References: 23 . - ISSN 1070-3292

РУБ Plant Sciences

Кл.слова (ненормированные):
CUCUMIS-SATIVUS -- LEAVES -- ONTOGENY -- CHLOROPHYLL FLUORESCENCE
Аннотация: Additional integral and kinetic parameters of induction curves have been introduced on the basis of analysis of currently employed parameters of slow induction of fluorescence (SIF) for a more complete quantitative description of SIF changes during ontogenesis of higher plant leaves. High sensitivity of the additional parameters to the age state of leaf tissue as compared with previously employed parameters is demonstrated on the example of cucumber leaves (Cucumis sativus L.). Analysis of the relationship between the photosynthetic rate and SIF parameters of separate cucumber leaf disks revealed the presence of a high positive correlation between the photosynthetic rate and the greatest possible average decline in fluorescence intensity during the inductive period for mature regions of the leaf and regions starting to senesce (the correlation coeffcient attained values of 0.95), which indicates the possibility of using the given SIF parameter in further elaboration of methods for estimation of chloroplast photosynthetic activity at the level of the higher plant leaf.

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

Доп.точки доступа:
NESTERENKO, T.V.; SIDKO, F.Y.

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14.

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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15.

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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16.

Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemistry. - 1995. - Vol. 34, Is. 10. - P3300-3309 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- recombinant protein -- article -- ligand binding -- nonhuman -- priority journal -- protein isolation -- protein protein interaction -- protein stability -- vibrionaceae -- Bacterial Proteins -- Binding Sites -- Carrier Proteins -- Circular Dichroism -- Flavin Mononucleotide -- Fluorescence Polarization -- Genes, Bacterial -- Kinetics -- Ligands -- Luciferase -- Luminescence -- Molecular Sequence Data -- Photobacterium -- Recombinant Proteins -- Spectrophotometry -- Support, U.S. Gov't, P.H.S. -- Photobacterium leiognathi -- Vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.

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.

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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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.

Photosynthetic apparatus of cucumber and pea plants grown under red light with discrete or continuous spectra / E. N. Zavorueva [et al.] // Russian Journal of Plant Physiology. - 1996. - Vol. 43, Is. 2. - P191-199 . - ISSN 1021-4437
Кл.слова (ненормированные):
And thermoinduced changes in fluorescence yield -- Cucumis sativum -- Photo -- Photophosphorylation -- Pigments -- Pisum sativum
Аннотация: The effect of light sources with discrete or continuous spectra of red light (50 W/m2, 600-700 nm) on the structural and functional characteristics of chloroplasts were studied in leaves of cucumber (Cucumis sativum L.) plants, which die under strong red light, and pea (Pisum sativum L.) plants, which tolerate red light under the same conditions. Leaf condition was assessed by measuring thermo-and photoinduced changes in the chlorophyll fluorescence yield and the photochemical and photophosphorylating activities of the chloroplasts. Different responses of the pigment apparatus of pea and cucumber plants to red light with continuous or line spectra were revealed. Pea plants responded to discrete-spectrum light by changing P700 content, the ratio of antenna chlorophyll to P700, and the position of the low-temperature peak of the temperature-induced chlorophyll fluorescence yield. In cucumber plants, disturbances in the energy transfer from the short-wavelength pigments to chlorophyll a were observed. In both plants, the effects of line spectrum light on the pigment apparatus were reversible; the ratio of cyclic to noncyclic photophosphorylation, photosynthetic control, and the extent of the coupling of photosynthetic electron transport to photophosphorylation did not change compared to the control light. The need for examining the line spectra of light sources for growing plants under moderate intensities of artificial light (about 50 W/m2 of photosynthetically active radiation) is discussed.

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:
Zavorueva, E.N.; Nesterenko, T.V.; Volkova, E.K.; Tikhomirov, A.A.

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20.

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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