Effect of quinone on the fluorescence decay dynamics of endogenous flavin bound to bacterial luciferase

Описание

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, 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, Luciferases, Bacterial, Time Factors, Bacteria (microorganisms)

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 abПоказать полностьюsence 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.

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Издание

Журнал: BIOPHYSICAL CHEMISTRY

Выпуск журнала: Vol. 141, Is. 1

Номера страниц: 59-65

ISSN журнала: 03014622

Место издания: AMSTERDAM

Издатель: ELSEVIER SCIENCE BV

Авторы

  • Vetrova E.V. (Department of Physics,Texas Tech University)
  • Cheng K.H. (Department of Physics,Texas Tech University)
  • Kudryasheva N.S. (Siberian Federal University)

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