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dc.contributor.authorHaik Chosrowjanen_US
dc.contributor.authorSeiji Taniguchien_US
dc.contributor.authorNoboru Matagaen_US
dc.contributor.authorThanawat Phongsaken_US
dc.contributor.authorJeerus Sucharitakulen_US
dc.contributor.authorPimchai Chaiyenen_US
dc.contributor.authorFumio Tanakaen_US
dc.contributor.otherInstitute for Laser Technologyen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherChulalongkorn Universityen_US
dc.contributor.otherMahasarakham Universityen_US
dc.identifier.citationJournal of Physical Chemistry B. Vol.113, No.25 (2009), 8439-8442en_US
dc.description.abstractThe 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.en_US
dc.rightsMahidol Universityen_US
dc.subjectMaterials Scienceen_US
dc.titleUltrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylaseen_US
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