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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/27416
Title: Ultrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylase
Authors: Haik Chosrowjan
Seiji Taniguchi
Noboru Mataga
Thanawat Phongsak
Jeerus Sucharitakul
Pimchai Chaiyen
Fumio Tanaka
Institute for Laser Technology
Mahidol University
Chulalongkorn University
Mahasarakham University
Keywords: Chemistry;Materials Science
Issue Date: 25-Jun-2009
Citation: Journal of Physical Chemistry B. Vol.113, No.25 (2009), 8439-8442
Abstract: The reductase unit of p-hydroxyphenylacetate hydroxylase contains flavin mononucleotide (FMN) as a cofactor. Fluorescence decay curves measured by fluorescence up-conversion method were remarkably dependent on monitored emission wavelength. The fluorescence lifetime was shorter at the shorter emission wavelengths and longer at the longer wavelengths. Spectral shift correlation function of p-coumaric acid in water and FMN in C1 protein in buffer solution were expressed by two-exponential functions. Correlation times, φ1 and φ2, of p-coumaric acid were 0.053 and 0.650 ps, respectively, which was similar to previous works. φ1 and φ2 of C1were 0.455 and 250 ps, respectively. The Stokes shift from t = 0 to t = ∞ was 2200 cm-1o;, while it is 500 cm-1in the static Stokes shift obtained by the solvent effect of the fluorescence spectrum under static excitation. This suggests that the isoalloxazine ring of FMN in C1 is exposed in hydrophilic environment. Such large Stokes shift was unusual among flavoproteins. The biphasic decay of the spectral correlation function in C1 was discussed and compared to the biphasic decay of tryptophan in proteins. © 2009 American Chemical Society.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=67649214510&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/27416
ISSN: 15206106
Appears in Collections:Scopus 2006-2010

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