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α-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp. / M. A. Dubinnyi, I. A. Ivanov, N. S. Rodionova [et al.] // ChemistrySelect. - 2020. - Vol. 5, Is. 42. - P13155-13159, DOI 10.1002/slct.202003075 . - ISSN 2365-6549
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Henlea -- Natural products -- NMR spectroscopy
Аннотация: Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as ?-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophan-containing compounds are possible participants of bioluminescence-related metabolism in Henlea sp. © 2020 Wiley-VCH GmbH

Scopus
Держатели документа:
Shemyakin-Ovchinnikov Institute of bioorganic chemistry, Russian academy of Sciences GSP-7, Miklukho-Maklaya str., 16/10, Moscow, 117997, Russian Federation
Institute of Biophysics, Krasnoyarsk Research Center, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Pirogov Russian National Research Medical University, 1 Ostrovityanova st., Moscow, 117997, Russian Federation

Доп.точки доступа:
Dubinnyi, M. A.; Ivanov, I. A.; Rodionova, N. S.; Kovalchuk, S. I.; Kaskova, Z. M.; Petushkov, V. N.

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Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory / F. N. Tomilin, A. V. Rogova, L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2021. - Vol. 20, Is. 4. - P559-570, DOI 10.1007/s43630-021-00039-5 . - ISSN 1474-905X
Кл.слова (ненормированные):
Absorption spectra -- Absorption spectroscopy -- Blue shift -- Dihedral angle -- Substrates -- Absorption maxima -- Covalently bound -- Electronic excitation -- Linear scaling -- Mechanical methods -- Substrate complexes -- Time dependent density functional theory -- Visible absorption spectra -- Density functional theory
Аннотация: Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460–470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein–substrate complex was optimized using a linear scaling quantum–mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60° of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified. © 2021, The Author(s), under exclusive licence to European Photochemistry Association,European Society for Photobiology.

Scopus
Держатели документа:
Kirensky Institute of Physics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/38, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodny 79 pr., Krasnoyarsk, 660041, Russian Federation
National Research Tomsk State University, Lenin Avenue 36, Tomsk, 634050, Russian Federation
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation
Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, South Korea
Research Center for Computational Design of Advanced Functional Materials (CD-FMat), National Institute of Advanced Industrial Science and Technology (AIST), Central 2, Umezono 1-1-1, Tsukuba, 305-8568, Japan

Доп.точки доступа:
Tomilin, F. N.; Rogova, A. V.; Burakova, L. P.; Tchaikovskaya, O. N.; Avramov, P. V.; Fedorov, D. G.; Vysotski, E. 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.

Scopus
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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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.

Scopus
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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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.

WOS
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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Toxicity and antioxidant activity of fullerenol c60,70 with low number of oxygen substituents / E. S. Kovel, A. G. Kicheeva, N. G. Vnukova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 12. - Ст. 6382, DOI 10.3390/ijms22126382 . - ISSN 1661-6596
Кл.слова (ненормированные):
Antioxidant activity -- Bioluminescent assay -- Fullerenol -- Hormesis -- Reactive oxygen species -- Toxicity
Аннотация: Fullerene is a nanosized carbon structure with potential drug delivery applications. We studied the bioeffects of a water-soluble fullerene derivative, fullerenol, with 10-12 oxygen groups (F10-12); its structure was characterized by IR and XPS spectroscopy. A bioluminescent enzyme system was used to study toxic and antioxidant effects of F10-12 at the enzymatic level. Antioxidant characteristics of F10-12 were revealed in model solutions of organic and inorganic oxidizers. Low-concentration activation of bioluminescence was validated statistically in oxidizer solutions. Toxic and antioxidant characteristics of F10-12 were compared to those of homologous fullerenols with a higher number of oxygen groups:F24-28 and F40-42. No simple dependency was found between the toxic/antioxidant characteristics and the number of oxygen groups on the fullerene’s carbon cage. Lower toxicity and higher antioxidant activity of F24-28 were identified and presumptively attributed to its higher solubility. An active role of reactive oxygen species (ROS) in the bioeffects of F10-12 was demonstrated. Correlations between toxic/antioxidant characteristics of F10-12 and ROS content were evaluated. Toxic and antioxidant effects were related to the decrease in ROS content in the enzyme solutions. Our results reveal a complexity of ROS effects in the enzymatic assay system. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Physics SB RAS, FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
FRC KSC SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Kovel, E. S.; Kicheeva, A. G.; Vnukova, N. G.; Churilov, G. N.; Stepin, E. A.; Kudryasheva, N. S.

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Toxicity and Antioxidant Activity of Fullerenol C-60,C-70 with Low Number of Oxygen Substituents / E. S. Kovel, A. G. Kicheeva, N. G. Vnukova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 12. - Ст. 6382, DOI 10.3390/ijms22126382. - Cited References:93. - This research was funded by RFBR, N18-29-19003; RFBR, Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science, N20-44-243001; and partly supported by the Program of the Federal Service for Surveillance on Consumer Rights Protection and HumanWellbeing, Fundamental Study 2020-2025 (Russian Federation). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
HUMIC SUBSTANCES
DETOXIFICATION PROCESSES
BIOLOGICAL-ACTIVITY
Кл.слова (ненормированные):
fullerenol -- toxicity -- antioxidant activity -- reactive oxygen species -- bioluminescent assay -- hormesis
Аннотация: Fullerene is a nanosized carbon structure with potential drug delivery applications. We studied the bioeffects of a water-soluble fullerene derivative, fullerenol, with 10-12 oxygen groups (F10-12); its structure was characterized by IR and XPS spectroscopy. A bioluminescent enzyme system was used to study toxic and antioxidant effects of F10-12 at the enzymatic level. Antioxidant characteristics of F10-12 were revealed in model solutions of organic and inorganic oxidizers. Low-concentration activation of bioluminescence was validated statistically in oxidizer solutions. Toxic and antioxidant characteristics of F10-12 were compared to those of homologous fullerenols with a higher number of oxygen groups:F24-28 and F40-42. No simple dependency was found between the toxic/antioxidant characteristics and the number of oxygen groups on the fullerene's carbon cage. Lower toxicity and higher antioxidant activity of F24-28 were identified and presumptively attributed to its higher solubility. An active role of reactive oxygen species (ROS) in the bioeffects of F10-12 was demonstrated. Correlations between toxic/antioxidant characteristics of F10-12 and ROS content were evaluated. Toxic and antioxidant effects were related to the decrease in ROS content in the enzyme solutions. Our results reveal a complexity of ROS effects in the enzymatic assay system.

WOS
Держатели документа:
FRC KSC SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
FRC KSC SB RAS, Inst Phys SB RAS, Krasnoyarsk 660036, Russia.
FRC KSC SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Kovel, Ekaterina S.; Kicheeva, Arina G.; Vnukova, Natalia G.; Churilov, Grigory N.; Stepin, Evsei A.; Kudryasheva, Nadezhda S.; Kovel, Ekaterina; RFBRRussian Foundation for Basic Research (RFBR) [N18-29-19003]; RFBR, Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science [N20-44-243001]; Program of the Federal Service for Surveillance on Consumer Rights Protection and Human Wellbeing, Fundamental Study 2020-2025 (Russian Federation)

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Time course of the spectral brightness of agricultural crops during the vegetation period in Krasnoyarsk krai / A. F. Sid'ko, I. Yu. Pugacheva, A. P. Shevyrnogov // Doklady Biological Sciences. - 2008. - Vol. 419, Is. 1. - P114-117, DOI 10.1134/S0012496608020130 . - ISSN 0012-4966
Кл.слова (ненормированные):
article -- crop -- histology -- light -- metabolism -- plant -- Russian Federation -- season -- spectroscopy -- Crops, Agricultural -- Light -- Plants -- Russia -- Seasons -- Spectrum Analysis

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

Доп.точки доступа:
Sid'ko, A.F.; Pugacheva, I.Yu.; Shevyrnogov, A.P.

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10.

Thermal, mechanical and biodegradation studies of biofiller based poly-3-hydroxybutyrate biocomposites / S. Thomas [et al.] // Int. J. Biol. Macromol. - 2019, DOI 10.1016/j.ijbiomac.2019.11.112 . - Article in press. - ISSN 0141-8130
Кл.слова (ненормированные):
Biocomposite -- Environmental degradation -- Physical properties -- Poly-3-hydroxybutyrate
Аннотация: Biodegradable poly-3-hydroxybutyrate [P(3HB)] and natural fillers - clay, peat, and birch wood flour – were used to prepare powdered composites to form pellets and granules. Pellets were produced by cold pressing of polymer and filler powder whereas granules were produced from the powders wetted with ethanol. Characterization techniques like IR spectroscopy, differential scanning calorimetry, X-ray analysis, mechanical analysis and electron microscopy were employed to study the properties of the initial P(3HB) and fillers and the composites. Analysis of the IR spectra of the composites showed the absence of chemical bonds between the components, i.e. the composites were physical mixtures. Young's moduli of the pellets prepared from initial materials varied considerably, and the highest value was obtained for P(3HB) pellets (350 MPa). Studies of biodegradation of composite pellets and granules in the soil for 35 days showed that the residual mass of the pellets had decreased to 68% for P(3HB); 56.4% for P(3HB)/peat; 67% for P(3HB)/wood flour, and 64% for P(3HB)/clay; granules exhibited a similar mass loss, residual mass of the granules of P(3HB) was 68.4%, P(3HB)/peat 46.4%; P(3HB)/wood flour 77%, and P(3HB)/clay 74%. This shows the significance of the material as an eco-friendly composite without sacrificing its mechanical properties. © 2018

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Держатели документа:
Siberian Federal University, 79 Svobodnyi Av., Krasnoyarsk, 660041, Russian Federation
International and Interuniversity Centre for Nano Science and Nano technology, Kottayam, Kerala, India
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
L.V. Kirensky Institute of Physics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, 43/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Federal Research Center Krasnoyarsk Scientific Center of the Siberian Branch of Russian, Academy of Sciences, 50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Thomas, S.; Shumilova, A. A.; Kiselev, E. G.; Baranovsky, S. V.; Vasiliev, A. D.; Nemtsev, I. V.; Kuzmin, A. P.; Sukovatyi, A. G.; Avinash, R. P.; Volova, T. G.

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11.

Thermal, mechanical and biodegradation studies of biofiller based poly-3-hydroxybutyrate biocomposites / S. Thomas, A. A. Shumilova, E. G. Kiselev [et al.] // Int. J. Biol. Macromol. - 2020. - Vol. 155. - P1373-1384, DOI 10.1016/j.ijbiomac.2019.11.112. - Cited References:38. - This studywas financially supported by Project "Agropreparations of the new generation: a strategy of construction and realization" (Agreement No 074-02-2018-328) in accordance with Resolution No 220 of the Government of the Russian Federation of April 9, 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning".; The surface of the samples was investigated using a scanning electron microscope Hitachi TM-3000 in the Joint Instrument Use Center at the Krasnoyarsk Scientific Center of Siberian Branch of Russian Academy of Sciences. . - ISSN 0141-8130. - ISSN 1879-0003

РУБ Biochemistry & Molecular Biology + Chemistry, Applied + Polymer Science
Рубрики:
FORMULATIONS
   POLYHYDROXYALKANOATES
   POLYHYDROXYBUTYRATE
   SOIL
Кл.слова (ненормированные):
Poly-3-hydroxybutyrate -- Biocomposite -- Physical properties -- Environmental -- degradation
Аннотация: Biodegradable poly-3-hydroxybutyrate [P(3HB)] and natural fillers - clay, peat, and birch wood flour - were used to prepare powdered composites to form pellets and granules. Pellets were produced by cold pressing of polymer and filler powder whereas granules were produced from the powders wetted with ethanol. Characterization techniques like IR spectroscopy, differential scanning calorimetry, X-ray analysis, mechanical analysis and electron microscopy were employed to study the properties of the initial P(3HB) and fillers and the composites. Analysis of the IR spectra of the composites showed the absence of chemical bonds between the components, i.e. the composites were physical mixtures. Young's moduli of the pellets prepared from initial materials varied considerably, and the highest value was obtained for P(3HB) pellets (350 MPa). Studies of biodegradation of composite pellets and granules in the soil for 35 days showed that the residual mass of the pellets had decreased to 68% for P (3HB); 56.4% for P(3HB)/peat; 67% for P(3HB)/wood flour, and 64% for P(3HB)/clay; granules exhibited a similar mass loss, residual mass of the granules of P(3HB) was 68.4%, P(3HB)/peat 46.4%; P(3HB)/wood flour 77%, and P (3HB)/clay 74%. This shows the significance of the material as an eco-friendly composite without sacrificing its mechanical properties. (C) 2019 Published by Elsevier B.V.

WOS
Держатели документа:
Siberian Fed Univ, 79 Svobodnyi Av, Krasnoyarsk 660041, Russia.
Int & Interuniv Ctr Nano Sci & Nano Technol, Kottayam, Kerala, India.
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Krasnoyarsk Sci Ctr SB RAS, LV Kirensky Inst Phys SB RAS, Fed Res Ctr, 43-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Fed Res Ctr, 50 Akademgorodok, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Thomas, Sabu; Shumilova, A. A.; Kiselev, E. G.; Baranovsky, S., V; Vasiliev, A. D.; Nemtsev, I., V; Kuzmin, Andrei Petrovich; Sukovatyi, A. G.; Avinash, R. Pai; Volova, T. G.; Nemtsev, Ivan; Government of the Russian Federation [220]; Project "Agropreparations of the new generation: a strategy of construction and realization" [074-02-2018-328]

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12.

Synthesis, Mass Spectroscopy Detection, and Density Functional Theory Investigations of the Gd Endohedral Complexes of C-82 Fullerenols / A. A. Shakirova, F. N. Tomilin, V. A. Pomogaev [et al.] // Computation. - 2021. - Vol. 9, Is. 5. - Ст. 58, DOI 10.3390/computation9050058. - Cited References:41. - The experimental results were funded by RFBR project No. 18-29-19003 MK. The quantum chemical study was funded by project 0721-2020-0033 of the Russian Ministry of Science and Education. The collaboration and coordination of Russian and Korean teams was supported by Collaborative NRF-RFBR grant (Korean ID: NRF-2019K2A9A1A06100125; Russian ID: Project No. 19-53-51005 NIFa RFFI-Korea) and NRF 2021R1A2C1010455 grant. . - ISSN 2079-3197

РУБ Mathematics, Interdisciplinary Applications
Рубрики:
ZETA VALENCE QUALITY
   BIOLOGICAL-ACTIVITY
   BASIS-SETS
   TOXICITY
Кл.слова (ненормированные):
endohedral fullerenes -- density functional theory -- antioxidant activity -- reactive oxygen species -- magnetic resonance imaging
Аннотация: Gd endohedral complexes of C-82 fullerenols were synthesized and mass spectrometry analysis of their composition was carried out. It was established that the synthesis yields a series of fullerenols Gd@C82Ox(OH)(y) (x = 0, 3; y = 8, 16, 24, 36, 44). The atomic and electronic structure and properties of the synthesized fullerenols were investigated using the density functional theory calculations. It was shown that the presence of endohedral gadolinium increases the reactivity of fullerenols. It is proposed that the high-spin endohedral fullerenols are promising candidates for application in magnetic resonance imaging.

WOS
Держатели документа:
Siberian Fed Univ, Dept Biophys, Sch Engn Phys & Radio Elect, Sch Petr & Gas Engn, Pr Svobodny 79, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Kirensky Inst Phys, Krasnoyarsk Sci Ctr, Akad Gorodok 50, Krasnoyarsk 660036, Russia.
Natl Res Tomsk State Univ, Dept Phys, Lenina Ave 36, Toms 634050, Russia.
Kyungpook Natl Univ, Dept Chem, 80 Daehak Ro, Daegu 41566, South Korea.
Kyungpook Natl Univ, Green Nano Mat Res Ctr, 80 Daehak Ro, Daegu 41566, South Korea.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk Sci Ctr, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Shakirova, Anastasia A.; Tomilin, Felix N.; Pomogaev, Vladimir A.; Vnukova, Natalia G.; Churilov, Grigory N.; Kudryasheva, Nadezhda S.; Tchaikovskaya, Olga N.; Ovchinnikov, Sergey G.; Avramov, Pavel V.; Tomilin, Felix; RFBRRussian Foundation for Basic Research (RFBR) [18-29-19003 MK]; Russian Ministry of Science and EducationMinistry of Education and Science, Russian Federation [0721-2020-0033]; Collaborative NRF-RFBR grant (Korean) [NRF-2019K2A9A1A06100125]; Collaborative NRF-RFBR grant (Russian) [19-53-51005 NIFa RFFI-Korea]; NRF [2021R1A2C1010455]

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13.

Surface properties of nanodiamond films deposited by electrophoresis on Si(100) / E. Maillard-Schaller [et al.] // Diamond and Related Materials. - 1999. - Vol. 8, Is. 2-5. - P805-808 . - ISSN 0925-9635
Кл.слова (ненормированные):
Energy band diagram -- Nanodiamond -- Raman spectroscopy -- Surface characterization -- Band structure -- Electrodeposition -- Electrophoresis -- Hydrogen -- Nanostructured materials -- Nitrogen -- Oxidation -- Oxygen -- Phonons -- Plasma applications -- Silicon wafers -- Surface properties -- Dielectrophoresis -- Negative electron affinity (NEA) -- Phonon confinement effect -- Diamond films
Аннотация: The surface properties of diamond nanoparticles (40-50 A in diameter) have been investigated by X-ray photoelectron spectroscopy (XPS), UV photoelectron spectroscopy (UPS) and Raman spectroscopy. The diamond nanoparticles have been deposited on flat Si(100) substrates by electrophoresis/dielectrophoresis. The as-deposited films are strongly oxidized and present a 1-2% nitrogen content. After treatment at 850 В°C in H2 plasma for 60 min, the oxygen is removed, and the position of the C 1s core-level peak indicates a n-type electronic comportment of the diamond nanoparticles. Raman spectroscopy of the as-deposited film shows a sp3 contribution at 1321 cm-1 and a sp2 contribution around 1620 cm-1. The 12 cm-1 shift of the sp3 contribution with respect to the bulk diamond peak at 1333 cm-1 is attributed to a phonon confinement effect due to the size of the diamond particles. The H2 plasma treatment induces a size decrease of the nanocrystallites confirmed by Raman and scanning electron microscopy (SEM) measurements. UPS spectroscopy shows a negative electron affinity of -0.2 eV of the hydrogenated nanodiamond film.

Scopus
Держатели документа:
Solid State Physics Department, University of Fribourg, 1700, Fribourg, Switzerland
Institute of Christallography, 117333, Moscow, Russian Federation
Institute of Biophysics, 660036, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Maillard-Schaller, E.; Kuettel, O.M.; Diederich, L.; Schlapbach, L.; Zhirnov, V.V.; Belobrov, P.I.

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14.

Surface bonding states of nano-crystalline diamond balls [Text] / J. L. Peng [et al.] // Int. J. Mod. Phys. B. - 2001. - Vol. 15, Is. 31. - P. 4071-4085, DOI 10.1142/S0217979201007865. - Cited References: 20 . - ISSN 0217-9792

РУБ Physics, Applied + Physics, Condensed Matter + Physics, Mathematical
Рубрики:
PLASMON RESPONSE
   POWDER
   SPECTROSCOPY
   MICROSCOPY
   SILICON
   SI(111)
Аннотация: The rough surface of nano-crystalline diamond spheres induces surface electronic states which appear as a broadened pre-peak over approx. 15 eV at the C K-edge energy threshold for carbon in the parallel electron energy loss spectrum (PEELS). This appears to be at least partially due to 1s-pi* transitions, although typically the latter occupy a range of only 4 eV for the sp(2) edge of highly-oriented pyrollytic graphite (HOPG). No pi* electrons appear in the conduction band inside the diamond particles, where all electrons are sp(3) hybridized. PEELS data were also obtained from a chemical vapour deposited diamond film (CVDF) and gem-quality diamond for comparison with the spectra of nano-diamonds. The density of sp(2) and sp(3) states on the surface of diamond nano-crystals is calculated for simple structural models of the diamond balls, including some conjecture about surface structures. The results are used to interpret the sp(2)/sp(3) ratios measured from the PEELS spectra recorded as scans across the particles. Surface roughness at the atomic scale was also examined using high-resolution transmission electron microscopy (HRTEM) and electron nano-diffraction patterns were used to confirm the crystal structures.

WOS
Держатели документа:
RMIT Univ, Dept Appl Phys, Melbourne, Vic 3051, Australia
Univ Sydney, Electron Microscope Unit, Sydney, NSW 2006, Australia
Russian Acad Sci, Siberian Branch, LV Kirensky Phys Inst, Mol Architecture Grp, Krasnoyarsk 660036, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Melbourne, Sch Phys, Parkville, Vic 3052, Australia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Peng, J.L.; Bulcock, S...; Belobrov, P.I.; Bursill, L.A.

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15.

Spectral composition of light and plant productivity / A. A. Tikhomirov // Advances in Space Research. - 1996. - Vol. 18, Is. 4-5. - P259-263 . - ISSN 0273-1177
Кл.слова (ненормированные):
article -- biology -- cucumber -- growth, development and aging -- illumination -- light -- maize -- photon -- photosynthesis -- plant -- radiation exposure -- spectroscopy -- sunflower -- tomato -- wheat -- Cucumis sativus -- Helianthus -- Light -- Lighting -- Lycopersicon esculentum -- Photobiology -- Photons -- Photosynthesis -- Plants -- Spectrum Analysis -- Triticum -- Zea mays

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

Доп.точки доступа:
Tikhomirov, A.A.

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16.

Recombinant Ca2+-regulated photoproteins of ctenophores: current knowledge and application prospects / L. P. Burakova, E. S. Vysotski // Appl. Microbiol. Biotechnol. - 2019. - Vol. 103, Is. 15. - P5929-5946, DOI 10.1007/s00253-019-09939-0 . - ISSN 0175-7598
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Intracellular calcium -- Photoinactivation -- Absorption spectroscopy -- Alkalinity -- Animals -- Binding sites -- Cloning -- Encoding (symbols) -- Phosphorescence -- Physicochemical properties -- Signal encoding -- Amino acid sequence -- Application prospect -- Biotechnology applications -- Coelenterazine -- Intracellular calcium -- Marine animals -- Photoinactivation -- Structural feature -- Bioluminescence -- Animalia -- Cnidaria -- Ctenophora (coelenterates)
Аннотация: Bright bioluminescence of ctenophores is conditioned by Ca2+-regulated photoproteins. Although they share many properties characteristic of hydromedusan Ca2+-regulated photoproteins responsible for light emission of marine animals belonging to phylum Cnidaria, a substantial distinction still exists. The ctenophore photoproteins appeared to be extremely sensitive to light—they lose the ability for bioluminescence on exposure to light over the entire absorption spectrum. Inactivation is irreversible because keeping the inactivated photoprotein in the dark does not recover its activity. The capability to emit light can be restored only by incubation of inactivated photoprotein with coelenterazine in the dark at alkaline pH in the presence of oxygen. Although these photoproteins were discovered many years ago, only the cloning of cDNAs encoding these unique bioluminescent proteins in the early 2000s has provided a new impetus for their studies. To date, cDNAs encoding Ca2+-regulated photoproteins from four different species of luminous ctenophores have been cloned. The amino acid sequences of ctenophore photoproteins turned out to completely differ from those of hydromedusan photoproteins (identity less than 29%) though also similar to them having three EF-hand Ca2+-binding sites. At the same time, these photoproteins reveal the same two-domain scaffold characteristic of hydromedusan photoproteins. This review is an attempt to systemize and critically evaluate the data scattered through various articles regarding the structural features of recombinant light-sensitive Ca2+-regulated photoproteins of ctenophores and their bioluminescent and physicochemical properties as well as to compare them with those of hydromedusan photoproteins. In addition, we also discuss the prospects of their biotechnology applications. © 2019, Springer-Verlag GmbH Germany, part of Springer Nature.

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Смотреть статью,
WOS
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Vysotski, E. S.

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17.

Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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18.

Preparation of complexes nanodiamond-protein-delta-aluminum oxide. / A. P. Puzyr' [et al.] // Doklady Biochemistry. - 2000. - Vol. 373, Is. 1-6. - P139-141 . - ISSN 0012-4958
Кл.слова (ненормированные):
aluminum oxide -- cytochrome c -- diamond -- article -- chemistry -- electron microscopy -- metabolism -- spectroscopy -- synthesis -- Aluminum Oxide -- Cytochrome c Group -- Diamond -- Microscopy, Electron -- Spectrum Analysis

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

Доп.точки доступа:
Puzyr', A.P.; Bondar', V.S.; Belobrov, P.I.; Bukaemskii, A.A.

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19.

Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin [Text] / B. . van Oort [et al.] // Biochemistry. - 2009. - Vol. 48, Is. 44. - P10486-10491, DOI 10.1021/bi901436m. - Cited References: 33. - This work was supported by NATO Collaborative Linkage Grant No 979229,Grants of SB RAS and RFBR 09-04-12-022, MCB program of RAS BvO was supported by 'Stichung voor Fundamenteel Onderzock der Materic (FOM)', which is financially supported by the NWO. and by I Rubicon grant of NWO E V E was supported by Wageningen University Sandwich Ph D-Fellowship program S P L was supported by Wageningen University Sandwich Ph D.-Fellowship program, European Community Marie Curie Research Training Network MRTN-CT-2005-019481 (From FLIM to FLIN), and Computational Science Gram 635 000 014 from the netherlands Organization for Scientific Research . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   W92F OBELIN
   COELENTERAZINE
   MECHANISM
   EXPRESSION
   PROTEINS
Аннотация: Addition of calcium tons to the Ca(2+)-regulated photoproteins, such its aequorin and obelin, produces it blue bioluminescence originating from fluorescence transition of the protein-bound product coelenteramide. The kinetics of several transient fluorescent species of the bound coelenteramide is resolved after picosecond-laser excitation and streak camera detection. The Initially formed spectral distributions at picosecond-times are broad, evidently comprised of two contributions, One at higher energy (similar to 25 000 cm(-1)) assigned as from the Ca(2+)-discharged photoprotein-bound coelenteramide in its neutral state. This component decays much more rapidly (t(1/2) similar to 2 ps) in the case of the Ca(2+)-discharged obelin than aequorin (t(1/2) similar to 30 ps). The Second component at lower energy shows several intermediates in the 150-500 ps miles. with it Final species having spectral maxima 19 400 cm(-1), bound to Ca(2+)-discharged obelin. and 2 1300 cm(-1), bound to Ca(2+)-discharged aequorin, and both have it fluorescence decay lifetime of 4 ns It is proposed that the rapid kinetics of these fluorescence transients oil the picosecond time scale, correspond to times For relaxation of the protein Structural environment of the binding cavity

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[van Oort, Bart
Koehorst, Rob B. M.
Laptenok, Sergey P.
van Amerongen, Herbert] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Laptenok, Sergey P.
van Berkel, Willem J. H.
Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Koehorst, Rob B. M.
van Amerongen, Herbert
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
van Oort, B...; Eremeeva, E.V.; Koehorst, RBM; Laptenok, S.P.; van Amerongen, H...; van Berkel, WJH; Malikova, N.P.; Markova, S.V.; Vysotski, E.S.; Visser, AJWG; Lee, J...; NATO Collaborative Linkage [979229]; RFBR [09-04-12-022]; 'Stichung voor Fundamenteel Onderzock der Materic (FOM)'; NWO; Wageningen University; European Community Marie Curie Research Training Network [MRTN-CT-2005-019481]; netherlands Organization [635 000 014]

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20.

Physicochemical properties of two-component polyhydroxyalkanoates, 3-hydroxybutyrate-3-hydroxyvalerate copolymers / T. G. Volova [et al.] // Biophysics. - 2004. - Vol. 49, Is. 6. - P934-942 . - ISSN 0006-3509
Кл.слова (ненормированные):
Hydroxybutyrate-hydroxyvalerate copolymers -- Physicochemical properties -- Polyhydroxyalkanoates -- Structure -- Bacteria (microorganisms) -- Cupriavidus necator
Аннотация: A series of two-component polyhydroxyalkanoates composed of hydroxybutyrate-hydroxyvalerate copolymers with different monomer ratio was obtained with the use of bacteria Ralstonia eutropha B5786. The properties of the polyhydroxyalkanoates in comparison with the homopolymer of hydroxybutyric acid were studied by X-ray diffraction analysis, IR spectroscopy, differential thermal analysis, and viscometry. The ratio of crystalline to amorphous phase in the copolymers tends to unity with increasing hydroxyvalerate content. This is accompanied by a decrease in the degree of crystallinity of the copolymers from 70-80 to 45-50%, the dependence is virtually linear within the range, of hydroxyvalerate mole fraction from several to 25-30 mol%. Thermal characteristics, melting temperature (Tm) and decomposition temperature (Td), of the polyhydroxyalkanoate copolymers are lower than those for polyhydroxybutyrate, whose Tm and Td are 168-170 and 260-265В°C, respectively. Both parameters decrease to 150-160 and 200-220В°C, respectively, when the hydroxyvalerate mole fraction is raised. No distinct correlation between polymer composition and molecular weight has been revealed. Copyright В© 2004 by MAIK "Nauka/Interperiodica".

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian State Technological University, Krasnoyarsk, 660049, Russian Federation
Kirenskii Institute of Physics, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Plotnikov, V.F.; Shishatskaya, E.I.; Mironov, P.V.; Vasil'ev, A.D.

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