Discharged photoprotein obelin: Fluorescence peculiarities

Тип публикации: статья из журнала

Год издания: 2010

Идентификатор DOI: 10.1016/j.jphotobiol.2010.07.001

Ключевые слова: Fluorescent protein, Discharged photoprotein, Obelin, Spectral components, Calcium, Conformational transition, 2 hydroperoxycoelenterazine, calcium ion, photoprotein, polypeptide, unclassified drug, article, bioluminescence, chromatophore, coelenterate, emission tomography, enzyme substrate complex, fluorescence, nonhuman, Obelia longissima, priority journal, Animals, Benzeneacetamides, Catalytic Domain, Hydrozoa, Luminescent Proteins, Protein Binding, Pyrazines, Recombinant Proteins, Spectrometry, Fluorescence, Hydroida

Аннотация: Photoprotein obelin, the enzyme-substrate complex of polypeptide with 2-hydroperoxycoelenterazine, is responsible for bioluminescence of marine hydroid Obelia longissima. Addition of Ca(2+) to the photoprotein triggers the bioluminescent reaction with light emission. The product of the bioluminescent reaction - enzyme-bound coelenteramide - is a fluorescent protein called 'discharged' obelin. It is stable and highly fluorescent. The paper considers dependence of its light-induced fluorescence on Ca2+ concentration. Increase of Ca(2+) concentration enhanced the fluorescence intensity of discharged obelin; the dependence was found as linear in double logarithmic coordinates at Ca(2+) concentration range 10(-7)-10(-6) M, both in excitation and emission spectra. The spectra were divided into components; contributions of the components to experimental excitation and emission spectra depended on Ca(2+) concentration. The data suggest enzymatic conformational transition in discharged obelin at similar to 5 x 10(-7) M of Ca(2+) concentration. Spectra variations were attributed to acidity changes of discharged obelin chromophore (coelenteramide) in its fluorescent state S. (C) 2010 Elsevier B.V. All rights reserved.

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Издание

Журнал: JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY

Выпуск журнала: Vol. 101, Is. 1

Номера страниц: 103-108

ISSN журнала: 10111344

Место издания: LAUSANNE

Издатель: ELSEVIER SCIENCE SA

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