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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., van Stokkum IHM, Gobets B..., van Mourik F..., Lee J..., van Grondelle R..., Visser AJWG
Заглавие : Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
Колич.характеристики :6 с
Место публикации : J. Phys. Chem. B: AMER CHEMICAL SOC, 2003. - Vol. 107, Is. 39. - P10934-10939. - ISSN 1520-6106, DOI 10.1021/jp034266e
Примечания : Cited References: 52
Предметные 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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva, Elena V., Gerasimova, Marina A., Melnik, Tatiana N., Melnik, Bogdan S.
Заглавие : Experimental approach to study the effect of mutations on the protein folding pathway
Колич.характеристики :17 с
Коллективы : Ministry of Science and Education of the Russian Federation [6.7734.2017]; Russian Science Foundation [N14-24-00157]
Место публикации : PLoS One: PUBLIC LIBRARY SCIENCE, 2019. - Vol. 14, Is. 1. - Ст.e0210361. - ISSN 1932-6203, DOI 10.1371/journal.pone.0210361
Примечания : 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.
Предметные 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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Dubinnyi, Maxim A., Ivanov, Igor A., Rodionova, Natalia S., Kovalchuk, Sergey I., Kaskova, Zinaida M., Petushkov, Valentin N.
Заглавие : alpha-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp.
Колич.характеристики :5 с
Коллективы : 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]
Место публикации : ChemistrySelect: WILEY-V C H VERLAG GMBH, 2020. - Vol. 5, Is. 42. - С. 13155-13159. - ISSN 2365-6549, DOI 10.1002/slct.202003075
Примечания : 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).
Предметные рубрики: STRUCTURE ELUCIDATION
MANNOSYLATION
TRYPTOPHAN
PROTEIN
COMPLEMENT
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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