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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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Experimental approach to study the effect of mutations on the protein folding pathway / E. V. Nemtseva [et al.] // PLoS One. - 2019. - Vol. 14, Is. 1. - Ст. e0210361, DOI 10.1371/journal.pone.0210361. - Cited References:38. - The study of time-resolved protein fluorescence was supported by the Ministry of Science and Education of the Russian Federation (Projects 6.7734.2017). The investigation of protein fluorescence and genetic engineering studies of bovine carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.; The study of time-resolved protein fluorescence was supported by the Ministry of Science and Education of the Russian Federation (Project 6.7734.2017). The investigation of protein fluorescence and genetic engineering studies of bovine carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. . - ISSN 1932-6203

РУБ Multidisciplinary Sciences
Рубрики:
FLUORESCENCE LIFETIMES ORIGIN
   TRANSITION-STATE
   EXCHANGE
   TRYPTOPHAN
Аннотация: Is it possible to compare the physicochemical properties of a wild-type protein and its mutant form under the same conditions? Provided the mutation has destabilized the protein, it may be more correct to compare the mutant protein under native conditions to the wild-type protein destabilized with a small amount of the denaturant. In general, is it appropriate to compare the properties of proteins destabilized by different treatments: mutations, pH, temperature, and denaturants like urea? These issues have compelled us to search for methods and ways of presentation of experimental results that would allow a comparison of mutant forms of proteins under different conditions and lead to conclusions on the effect of mutations on the protein folding/unfolding pathway. We have studied equilibrium unfolding of wild-type bovine carbonic anhydrase II (BCA II) and its six mutant forms using different urea concentrations. BCA II has been already studied in detail and is a good model object for validating new techniques. In this case, time-resolved fluorescence spectroscopy was chosen as the basic research method. The main features of this experimental method allowed us to compare different stages of unfolding of studied proteins and prove experimentally that a single substitution of the amino acid in three mutant forms of BCA II affected the native state of the protein but did not change its unfolding pathway. On the contrary, the inserted disulfide bridge in three other mutant forms of BCA II affected the protein unfolding pathway. An important result of this research is that we have validated the new approach allowing investigation of the effect of mutations on the folding of globular proteins, because in this way it is possible to compare proteins in the same structural states rather than under identical conditions.

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Scopus
Держатели документа:
Siberian Fed Univ, Krasnoyarsk, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino, Moscow Region, Russia.

Доп.точки доступа:
Nemtseva, Elena V.; Gerasimova, Marina A.; Melnik, Tatiana N.; Melnik, Bogdan S.; Gerasimova, Marina; Nemtseva, Elena; Ministry of Science and Education of the Russian Federation [6.7734.2017]; Russian Science Foundation [N14-24-00157]

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alpha-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. - Cited References:49. - This work was supported by the State Assignment for Basic Research of the Russian Academy of Sciences (project no. 0356-2019-0019) and the Russian Foundation for Basic Research (project no. 19-04-00348-a). . - ISSN 2365-6549

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
   MANNOSYLATION
   TRYPTOPHAN
   PROTEIN
   COMPLEMENT
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 alpha-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.

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Держатели документа:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, GSP-7,Miklukho Maklaya Str 16-10, Moscow 117997, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Res Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Pirogov Russian Natl Res Med Univ, 1 Ostrovityanova St, Moscow 117997, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Ivanov, Igor A.; Rodionova, Natalia S.; Kovalchuk, Sergey I.; Kaskova, Zinaida M.; Petushkov, Valentin N.; State Assignment for Basic Research of the Russian Academy of Sciences [0356-2019-0019]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-04-00348-a]

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