Тип публикации: статья из журнала
Год издания: 2009
Идентификатор DOI: 10.1016/j.bpc.2008.12.012
Ключевые слова: Time-resolved fluorescence decay, Bioluminescence enzyme, Enzyme/xenobiotic interactions, Rotational dynamics of enzyme substrate, Bioluminescence enzyme, Enzyme/xenobiotic interactions, Rotational dynamics of enzyme substrate, Time-resolved fluorescence decay, 1,4 benzoquinone, 1,4 naphthoquinone, alkanal monooxygenase (FMN linked), flavine mononucleotide, quinone derivative, xenobiotic agent, anisotropy, article, bioluminescence, controlled study, drug mechanism, drug structure, enzyme active site, enzyme binding, enzyme inhibition, enzyme mechanism, enzyme substrate, fluorescence analysis, hydrophobicity, microenvironment, molecular interaction, nonhuman, Photobacterium leiognathi, photochemical quenching, priority journal, sequence homology, structure activity relation, Benzoquinones, Flavins, Fluorescence, Fluorescence Polarization, Hydrophobicity, Luciferases, Bacterial, Time Factors, Bacteria (microorganisms), Photobacterium leiognathi
Аннотация: The interaction of quinone with luciferase from Photobacterium leiognathi was studied based on the fluorescence decay measurements of the endogenous flavin bound to the enzyme. Homologous 1,4-quinones, 1,4-benzoquinone, methyl-1,4-benzoquinone, 2-methyl-5-isopropyl-1,4-benzoquine and 1,4-naphthoquinone, were investigated. In the absence of quinone, the fluorescence intensity and anisotropy decays of the endogenous flavin exhibited two intensity decay lifetimes (similar to 1 and 5 ns) and two anisotropy decay lifetimes (similar to 0.2 and 20 ns), suggesting a heterogeneous quenching and a rotational mobility microenvironment of the active site of the luciferase, respectively. In the presence of quinone, the intensity decay heterogeneity was largely maintained, whereas the fraction of the short anisotropy decay component and the averaged rotational rate of FMN increased with the increasing hydrophobicity of the quinone. We hypothesize that the hydrophobicity of the quinone plays a role in the non-specific inhibition mechanism of xenobiotic molecules in the bacterial bioluminescence system via altering the rotational mobility of the endogenous flavin in the luciferase. (C) 2008 Elsevier B.V. All rights reserved.
Журнал: BIOPHYSICAL CHEMISTRY
Выпуск журнала: Vol. 141, Is. 1
Номера страниц: 59-65
ISSN журнала: 03014622
Место издания: AMSTERDAM
Издатель: ELSEVIER SCIENCE BV
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