Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=Flavoprotein<.>)

Общее количество найденных документов : 4
Показаны документы с 1 по 4

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.

Найти похожие

Isolation and comparative studies of two fluorescent flavoproteins of luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biofizika. - 1990. - Vol. 35, Is. 2. - С. 368-370 . - ISSN 0006-3029
Кл.слова (ненормированные):
flavoprotein -- fluorescence -- letter -- nonhuman -- Photobacterium leiognathi

Scopus
Держатели документа:
Institute of Biological Physics, Siberian Branch, Academy of Sciences of the USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Raibekas, A.A.; Petushkov, V.N.

Найти похожие

Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

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

Доп.точки доступа:
Raibekas, A.A.

Найти похожие

Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications / O. Mogilnaya, N. Ronzhin, E. Posokhina, V. Bondar // Protein J. - 2021, DOI 10.1007/s10930-021-10010-z. - Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, Project No. 0356-2019-0022. . - Article in press. - ISSN 1572-3887. - ISSN 1573-4943

РУБ Biochemistry & Molecular Biology
Рубрики:
ARYL-ALCOHOL OXIDASE
   GLUCOSE-OXIDASE
   PEROXIDASES
   MECHANISM
Кл.слова (ненормированные):
Extracellular oxidase -- Flavoprotein -- Fungi -- Phenol
Аннотация: The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with beta-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H2O2, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55-70 degrees C and pH 5.0. Kinetic parameters K-m and V-max of the oxidase for phenol were 0.21 mM and 0.40 mu M min(-1). We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Posokhina, Ekaterina; Bondar, Vladimir; [0356-2019-0022]

Найти похожие

Тематический навигатор

Другие библиотеки

Библиотека института физики

Центральная научная библиотека КНЦ СО РАН

Библиотека института химии и химический технологии

Библиотека института вычислительного моделирования

Библиотека института леса

Библиотека СФУ

Краевая научная библиотека

© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)