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The Chemical Basis of Fungal Bioluminescence / K. V. Purtov [et al.] // Angew. Chem. Int. Ed. - 2015. - Vol. 54, Is. 28. - P8124-8128, DOI 10.1002/anie.201501779 . - ISSN 1433-7851
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- biosynthesis -- luciferin -- natural products -- Biochemistry -- Bioluminescence -- Biosynthesis -- Metabolites -- Phosphorescence -- Biochemical mechanisms -- Bioorganic chemistry -- luciferin -- Natural products -- Plant secondary metabolites -- Structural similarity -- Fungi
Аннотация: Many species of fungi naturally produce light, a phenomenon known as bioluminescence, however, the fungal substrates used in the chemical reactions that produce light have not been reported. We identified the fungal compound luciferin 3-hydroxyhispidin, which is biosynthesized by oxidation of the precursor hispidin, a known fungal and plant secondary metabolite. The fungal luciferin does not share structural similarity with the other eight known luciferins. Furthermore, it was shown that 3-hydroxyhispidin leads to bioluminescence in extracts from four diverse genera of luminous fungi, thus suggesting a common biochemical mechanism for fungal bioluminescence. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Держатели документа:
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation

Доп.точки доступа:
Purtov, K.V.; Petushkov, V.N.; Baranov, M.S.; Mineev, K.S.; Rodionova, N.S.; Kaskova, Z.M.; Tsarkova, A.S.; Petunin, A.I.; Bondar, V.S.; Rodicheva, E.K.; Medvedeva, S.E.; Oba, Y.; Arseniev, A.S.; Lukyanov, S.; Gitelson, J.I.; Yampolsky, I.V.

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Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin [Text] / N. V. Sablin, M. A. Gerasimova, E. V. Nemtseva // Russ. Phys. J. - 2016. - Vol. 58, Is. 12. - P1797-1803, DOI 10.1007/s11182-016-0719-6. - Cited References:16. - This work was supported in part by the Russian Academy of Sciences (The program "Molecular and Cell Biology", project No. 6.8), the Ministry of Education and Science of the Russian Federation (project No. 1762), and the Federal Agency of scientific organizations of the Russian Federation (project No. VI 57.1.1). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
ROOM-TEMPERATURE
   AQUEOUS-SOLUTION
   PHOSPHORESCENCE
   FLUORESCENCE
   EOSIN
Кл.слова (ненормированные):
erythrosin B -- phosphorescence -- delayed fluorescence -- quantum yield -- phosphorescence lifetime -- bovine serum albumin
Аннотация: Changes in absorption, fluorescence, phosphorescence, and delayed fluorescence spectra of erythrosin B are studied in the presence of bovine serum albumin at room temperature. Spectral and chronoscopic characteristics of the observed photophysical processes are defined. The binding of erythrosin B with the protein followed by spectral changes is demonstrated. Absorption and fluorescence spectra of the dye in the bound state are described, the binding mechanism is analyzed. The binding parameters of the dye-protein complex are estimated.

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

Доп.точки доступа:
Sablin, N. V.; Gerasimova, M. A.; Nemtseva, E. V.; Russian Academy of Sciences [6.8]; Ministry of Education and Science of the Russian Federation [1762]; Federal Agency of scientific organizations of the Russian Federation [VI 57.1.1]

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Is bacterial luminescence response to low-dose radiation associated with mutagenicity? / T. V. Rozhko [et al.] // J. Environ. Radioact. - 2017. - Vol. 177. - P261-265, DOI 10.1016/j.jenvrad.2017.07.010 . - ISSN 0265-931X
Кл.слова (ненормированные):
Bioassay -- DNA -- Low-dose radiation -- Luminous marine bacteria -- Mutations -- Bacteria -- Bioassay -- Bioluminescence -- Chemical activation -- DNA -- DNA sequences -- Genes -- Ionizing radiation -- Kinetics -- Luminescence -- Nucleic acids -- Phosphorescence -- Physiological models -- Radioisotopes -- Bacterial suspensions -- Beta-emitting radionuclides -- Low dose radiation -- Luminescence intensity -- Marine bacterium -- Mutations -- Photobacterium phosphoreum -- Physiological parameters -- Radiation -- Bacteria (microorganisms) -- Photobacterium phosphoreum
Аннотация: Luminous marine bacteria are widely used in bioassays with luminescence intensity being a physiological parameter tested. The purpose of the study was to determine whether bacterial genetic alteration is responsible for bioluminescence kinetics change under low-dose radiation exposure. The alpha-emitting radionuclide 241Am and beta-emitting radionuclide 3H were used as the sources of low-dose ionizing radiation. Changes of bioluminescence kinetics of Photobacterium phosphoreum in solutions of 241Am(NO3)3, 7 kBq/L, and tritiated water, 100 MBq/L, were studied; bioluminescence kinetics stages (absence of effect, activation, and inhibition) were determined. Bacterial suspension was sampled at different stages of the bioluminescent kinetics; the doses accumulated by the samples were close or a little higher than a tentative limit of a low-dose interval: 0.10 and 0.85 Gy for 241Am, or 0.11 and 0.18 Gy for 3H. Sequence analysis of the 16S ribosomal RNA gene did not reveal a mutagenic effect of low-dose alpha and beta radiation in the bacterial samples. Previous results on bacterial DNA exposed to low-dose gamma radiation (0.25 Gy) were analyzed and compared to those for alpha and beta irradiation. It is concluded that bioluminescence activation and/or inhibition under the applied conditions of low-dose alpha, beta and gamma radioactive exposure is not associated with DNA mutations in the gene sequences tested. © 2017 Elsevier Ltd

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Держатели документа:
Krasnoyarsk State Medical Academy, 1 P.Zheleznyaka, Krasnoyarsk, Russian Federation
Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, Russian Federation
SB RAS Genomics Core Facility, Institute of Chemical Biology and Fundamental Medicine SB RAS, 8 Lavrentiev Avenue, Novosibirsk, Russian Federation
Siberian State Technological University, LB, 29 Pobedy, Lesosibirsk, Krasnoyarsk Region, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, 50/50 Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Rozhko, T. V.; Guseynov, O. A.; Guseynova, V. E.; Bondar, A. A.; Devyatlovskaya, A. N.; Kudryasheva, N. S.

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Exposure of luminous marine bacteria to low-dose gamma-radiation / N. S. Kudryasheva [et al.] // J. Environ. Radioact. - 2017. - Vol. 169-170. - P64-69, DOI 10.1016/j.jenvrad.2017.01.002 . - ISSN 0265-931X
Кл.слова (ненормированные):
Bioassay -- Low-dose gamma-radiation -- Luminous marine bacteria -- Mutagenic effect -- Radiotoxicity -- Temperature dependence -- Bacteria -- Bioassay -- Bioluminescence -- Gamma rays -- Ionizing radiation -- Irradiation -- Phosphorescence -- Physiological models -- Radiation effects -- Temperature distribution -- Low dose -- Marine bacterium -- Mutagenic effect -- Radiotoxicity -- Temperature dependence -- Radiation -- Bacteria (microorganisms) -- Photobacterium phosphoreum
Аннотация: The study addresses biological effects of low-dose gamma-radiation. Radioactive 137Cs-containing particles were used as model sources of gamma-radiation. Luminous marine bacterium Photobacterium phosphoreum was used as a bioassay with the bioluminescent intensity as the physiological parameter tested. To investigate the sensitivity of the bacteria to the low-dose gamma-radiation exposure (?250 mGy), the irradiation conditions were varied as follows: bioluminescence intensity was measured at 5, 10, and 20°С for 175, 100, and 47 h, respectively, at different dose rates (up to 4100 ?Gy/h). There was no noticeable effect of gamma-radiation at 5 and 10°С, while the 20°С exposure revealed authentic bioluminescence inhibition. The 20°С results of gamma-radiation exposure were compared to those for low-dose alpha- and beta-radiation exposures studied previously under comparable experimental conditions. In contrast to ionizing radiation of alpha and beta types, gamma-emission did not initiate bacterial bioluminescence activation (adaptive response). As with alpha- and beta-radiation, gamma-emission did not demonstrate monotonic dose-effect dependencies; the bioluminescence inhibition efficiency was found to be related to the exposure time, while no dose rate dependence was found. The sequence analysis of 16S ribosomal RNA gene did not reveal a mutagenic effect of low-dose gamma radiation. The exposure time that caused 50% bioluminescence inhibition was suggested as a test parameter for radiotoxicity evaluation under conditions of chronic low-dose gamma irradiation. © 2017 Elsevier Ltd

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, 50/50 Akademgorodok, Krasnoyarsk, Russian Federation
Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agrarian University, 90 Mira Prospect, Krasnoyarsk, Russian Federation
SB RAS Genomics Core Facility, Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibirsk, Russian Federation

Доп.точки доступа:
Kudryasheva, N. S.; Petrova, A. S.; Dementyev, D. V.; Bondar, A. A.

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Reactive Oxygen Species and low-dose effects of tritium on bacterial cells / T. V. Rozhko [et al.] // J. Environ. Radioact. - 2019. - Vol. 208-209. - Ст. 106035, DOI 10.1016/j.jenvrad.2019.106035 . - ISSN 0265-931X
Кл.слова (ненормированные):
Bystander effect -- Low-dose effect -- Luminous marine bacterium -- Radiation hormesis -- Reactive oxygen species -- Signaling molecules -- Tritium -- Bioluminescence -- Cell signaling -- Cells -- Cytology -- Irradiation -- Oxygen -- Phosphorescence -- Physiological models -- Tritium -- Bystander effects -- Low dose effects -- Marine bacterium -- Radiation hormesis -- Reactive oxygen species -- Signaling molecules -- Bacteria -- Bacteria (microorganisms)
Аннотация: The paper continues study of exposures of luminous marine bacteria to low-dose radiation of tritium; tritiated water (HTO) was applied as a source of the irradiation. Hypothesis on involvement of Reactive Oxygen Species (ROS) to signaling mechanism of bacterial cells under exposure to low-intensity tritium radiation was verified. Bacterial bioluminescence intensity was considered as a tested physiological parameter; it was compared to the ROS production in the bacterial environment of different activity concentrations: 0.03, 4.0, and 500 MBq/L. Exposure of the bacteria to chronic low-dose tritium irradiation (<0.08 Gy) increased bioluminescence intensity and ROS production considerably (up to 300%). Spearman rank correlation coefficients were calculated and confirmed relations between the bioluminescence intensity and ROS production. Additional peculiarities of HTO effect were: independence of the bioluminescence intensity and ROS content on HTO activity concentration; low ROS content in bacteria-free aquatic environment. Effects of HTO on bacterial bioluminescence were attributed to: (1) trigger function of tritium decay products in the bacterial metabolic oxygen-dependent processes, with bioluminescence involved; (2) signaling role of ROS as intercellular messengers in “bystander effect”; (3) fixed amount of bacterial cells (3•107 cells/mL) provided the upper limits of the bioluminescence intensity and ROS content. As an outlook, in spite of low energy of tritium decay, its influence on aquatic biota via ROS production by microorganisms should be taken into consideration. © 2019 Elsevier Ltd

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Держатели документа:
Krasnoyarsk State Medical University, P.Zheleznyaka 1, Krasnoyarsk, 660022, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Moscow State University, Department of Chemistry, Moscow119991, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Rozhko, T. V.; Nogovitsyna, E. I.; Badun, G. A.; Lukyanchuk, A. N.; Kudryasheva, N. S.

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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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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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The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin / L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - P313-323, DOI 10.1039/c9pp00436j . - ISSN 1474-905X
Кл.слова (ненормированные):
Amino acids -- Bioluminescence -- Conformations -- Phosphorescence -- Amino acid residues -- Amino acid sequence -- Hydrogen bond networks -- Hydromedusan -- Internal cavities -- Phenyl rings -- Photoproteins -- Pi interactions -- Hydrogen bonds
Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal ?-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first ?-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the ?-? interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins. This journal is © The Royal Society of Chemistry and Owner Societies.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation

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

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H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. -F. Chen, E. S. Vysotski, Y. -J. Liu // J Phys Chem B. - 2021, DOI 10.1021/acs.jpcb.1c03985 . - Article in press. - ISSN 1520-6106
Кл.слова (ненормированные):
Amino acids -- Excited states -- Hydrogen bonds -- Molecular dynamics -- Molecular modeling -- Molecules -- Phosphorescence -- Proton transfer -- Quantum theory -- Fast protons -- Marine organisms -- Photoproteins -- Primary products -- Proton transfer process -- Quantum mechanics/molecular mechanics -- Reaction substrates -- Singlet excited state -- Theoretical calculations -- Transfer channel -- Bioluminescence
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S1) is the emitter of CaRP. The S1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs. © 2021 American Chemical Society.

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Держатели документа:
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, 201418, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Center for Advanced Materials Research, Advanced Institute of Natural Sciences, Beijing Normal University at Zhuhai, Zhuhai, 519087, China
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, 100875, China

Доп.точки доступа:
Chen, S. -F.; Vysotski, E. S.; Liu, Y. -J.

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Detecting bioluminescence conditions in fruit bodies of two species of Armillaria basidiomycetes / A. P. Puzyr, A. E. Burov, V. S. Bondar // IOP Conference Series: Earth and Environmental Science : IOP Publishing Ltd, 2021. - Vol. 677: 4th International Scientific Conference on Agribusiness, Environmental Engineering and Biotechnologies, AGRITECH-IV 2020 (18 November 2020 through 20 November 2020, ) Conference code: 167873, Is. 5. - Ст. 052081, DOI 10.1088/1755-1315/677/5/052081
Кл.слова (ненормированные):
Bioluminescence -- Biotechnology -- Fungi -- Phosphorescence -- Armillaria -- Armillaria species -- Fruit body -- Possible mechanisms -- Fruits
Аннотация: Mycelia of various Armillaria fungi are bioluminescent while the fruit bodies do not emit light. The presence in fruit bodies of Armillaria species of enzymes involved in the fungal bioluminescence was investigated by treating them with an exogenous analogue of the substrate for the light-emitting reaction. For this, hot extracts from nonluminous fungus Pholiota squarrosa were used. Upon spraying the pristine and transversely cut fruit bodies with the extracts, light emitting regions of different intensity were revealed. This suggests that the fruit bodies of the studied species are nonluminous due to lack of the substrate for light luminescent reaction. The prolonged incubation of the fruit bodies in water elevated the bioluminescence level. A possible mechanism which can explain this phenomenon is discussed. © 2021 Institute of Physics Publishing. All rights reserved.

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Federal Research Center for Information and Computational Technologies, Krasnoyarsk, 660049, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Burov, A. E.; Bondar, V. S.

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