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    Structural properties of tryptophan microenvironment in bacterial luciferase [Text] / A. A. Deeva, E. V. Nemtseva, V. A. Kratasyuk // Luminescence. - 2014. - Vol. 29. - P72-73. - Cited References: 4 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
FLUORESCENCE
   RESIDUES

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Держатели документа:
[Deeva, Anna A.
Nemtseva, Elena V.
Kratasyuk, Valentina A.] Siberian Fed Univ, Krasnoyarsk, Russia
[Nemtseva, Elena V.
Kratasyuk, Valentina A.] Inst Biophys SB RAS, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deeva, A.A.; Nemtseva, E.V.; Kratasyuk, V.A.

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Fluorescence lifetime components reveal kinetic intermediate states upon equilibrium denaturation of carbonic anhydrase II / E. V. Nemtseva [et al.] // Methods Appl. Fluoresc. - 2018. - Vol. 6, Is. 1. - Ст. 015006, DOI 10.1088/2050-6120/aa994a. - Cited References:28. - The study of time-resolved protein fluorescence was supported by the Ministry for Science and Education of the Russian Federation (project 6.7734.2017/BCH). Kinetic and genetic engineering studies of carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. . - ISSN 2050-6120

РУБ Chemistry, Analytical + Chemistry, Physical
Рубрики:
PROTEIN FLUORESCENCE
   TRYPTOPHAN PROTEINS
   RESIDUES
   STABILITY
Кл.слова (ненормированные):
time-resolved fluorescence spectroscopy -- carbonic anhydrase II -- protein -- intermediate states -- comparison of kinetic and equilibrium experiments -- protein fluorescence lifetime
Аннотация: In most cases, intermediate states of multistage folding proteins are not 'visible' under equilibrium conditions but are revealed in kinetic experiments. Time-resolved fluorescence spectroscopy was used in equilibrium denaturation studies. The technique allows for detecting changes in the conformation and environment of tryptophan residues in different structural elements of carbonic anhydrase II which in its turn has made it possible to study the intermediate states of carbonic anhydrase II under equilibrium conditions. The results of equilibrium and kinetic experiments using wild-type bovine carbonic anhydrase II and its mutant form with the substitution of leucine for alanine at position 139 (L139A) were compared. The obtained lifetime components of intrinsic tryptophan fluorescence allowed for revealing that, the same as in kinetic experiments, under equilibrium conditions the unfolding of carbonic anhydrase II ensues through formation of intermediate states.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia.

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

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Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation / L. P. Burakova, M. S. Lyakhovich, K. S. Mineev [et al.] // Org. Lett. - 2021. - Vol. 23, Is. 17. - P6846-6849, DOI 10.1021/acs.orglett.1c02410. - Cited References:20. - This work was supported by grant 20-04-00085 of the Russian Foundation for Basic Research, grant 20-44-242003 of the Russian Foundation for Basic Research, Krasnoyarsk Territory, and Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds, grant 17-1401169p of the Russian Science Foundation, and the President of Russian Federation grant for Leading Scientific Schools LS-2605.2020.4 in part of structural elucidation of native products and organic synthesis. We thank Konstantin Antonov (IBCh RAS) and Igor Ivanov (IBCh RAS) for the registration of HRMS spectra. . - ISSN 1523-7060. - ISSN 1523-7052

РУБ Chemistry, Organic
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENCE
   OBELIN
   RESIDUES
   BINDING
Аннотация: Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photo-inactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.

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Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Lyakhovich, Maria S.; Mineev, Konstantin S.; Petushkov, Valentin N.; Zagitova, Renata, I; Tsarkova, Aleksandra S.; Kovalchuk, Sergey, I; Yampolsky, Ilia, V; Vysotski, Eugene S.; Kaskova, Zinaida M.; Mineev, Konstantin; Tsarkova, Aleksandra; Vysotski, Eugene; Kaskova, Zinaida; Burakova, Lyudmila; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085]; Russian Foundation for Basic Research, Krasnoyarsk Territory [20-44-242003]; Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds; Russian Science FoundationRussian Science Foundation (RSF) [17-1401169p]; Russian FederationRussian Federation [LS-2605.2020.4]

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