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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Lee J.
Заглавие : Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1
Место публикации : European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - С. 790-796. - ISSN 00142956 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T.G., Guseinov O.A., Kalacheva G.S., Medvedeva S.E., Puzyr A.A.
Заглавие : Effect of carbon monoxide on metabolism and ultrastructure of carboxydobacteria
Место публикации : World Journal of Microbiology and Biotechnology. - 1993. - Vol. 9, Is. 2. - С. 160-163. - ISSN 09593993 (ISSN) , DOI 10.1007/BF00327827
Ключевые слова (''Своб.индексиров.''): carbon monoxide--carboxydobacteria--cytochromes--hydrogenase--seliberia carboxydohydrogena
Аннотация: Growth of Seliberia carboxydohydrogena was inhibited by CO at 10 to 40% (v/v), resulting in increased substrate utilization and enhanced synthesis of cytochromes and cyclopropane and saturated fatty acids. The bacteria showed increased formation of new membrane structures, with pronounced folding of their cell walls. В© 1993 Rapid Communications of Oxford Ltd.
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