The Solvent Effect on Fluorescence Spectrum, Change of Solute-Solvent Interaction during the Lifetime of Excited Solute Molecule

Mataga, Noboru; Kaifu, Yôzo; Koizumi, Masao

doi:10.1246/bcsj.28.690

Cited by 569 publications

(251 citation statements)

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“…The tryptophan residues, which belong to various classes, have different spectral and structural properties and, as a result, the different combinations of universal (dipole-dipole relaxation [16][17][18][19][20][21][22][23] and specific (exciplex formation 24-28 ) interactions could occur in the excited state of tryptophan fluorophores.…”

Section: Discussionmentioning

confidence: 99%

The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data

et al. 2008

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Protein fluorescence is a powerful tool for studying protein structure and dynamics if we have a means to interpret the spectral data in terms of protein structural properties. Our previous research successfully provided this support through the development of individual software modules implementing the algorithms for fluorescence and structural analyses. Now we have integrated the developed software modules, introduced a new program for the assignment of tryptophan residues to spectral‐structural classes, and created a web‐based toolkit PFAST: protein fluorescence and structural toolkit: http://pfast.phys.uri.edu/. PFAST contains three modules: (1) FCAT is a fluorescence‐correlation analysis tool, which decomposes protein fluorescence spectra to reveal the spectral components of individual tryptophan residues or groups of tryptophan residues located close to each other, and assigns spectral components to one of five previously established spectral‐structural classes. (2) SCAT is a structural‐correlation analysis tool for the calculation of the structural parameters of the environment of tryptophan residues from the atomic structures of the proteins from the Protein Data Bank (PDB), and for the assignment of tryptophan residues to one of five spectral‐structural classes. (3) The last module is a PFAST database that contains protein fluorescence and structural data obtained from results of the FCAT and SCAT analyses. Proteins 2008. © 2008 Wiley‐Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data

et al. 2008

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“…A quantitative estimate of the effect of the solvent polarity on the position of the fluorescence spectrum can be obtained from the Lippert-Mataga equation [36][37][38]. In the Lippert-Mataga model the frequency of the emission band maximum varies linearly with the solvent polarity parameter A f:…”

Section: Steady State Spectramentioning

confidence: 99%

Picosecond time-dependent Stokes shift studies of fluoroprobe in liquid solution

et al. 1995

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We report on a picosecond spectroscopic study of the dynamical Stokes shift of fluoroprobe in the lowest excited state in the solvents diethylether and ethylacetate. Time-resolved emission spectra with a time-resolution of approximately 10 ps are presented. The spectra reflect dynamical Stokes shifts of a few thousand wave numbers within 10-100 ps after the pulsed laser excitation. The time-dependent shifts are representative of the solvation dynamics of fluoroprobe in diethylether and ethylacetate.

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“…The magnitude of the difference between the absorption energy and fluorescence energy, that is, the Stokes shift, is related to the ⌬ of the fluorescent molecule according to the Lippert-Mataga equation. 17,18 This method has been successfully applied to many molecules so far in solution to estimate ͉⌬ ͉. In this method, however, emission measurements are necessary, and the information about the molecular polarizability cannot be obtained.…”

Section: Introductionmentioning

confidence: 99%

Comparative study of electroabsorption spectra of polar and nonpolar organic molecules in solution and in a polymer film

Tayama

Iimori

Ohta

2009

The Journal of Chemical Physics

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Electroabsorption ͑EA͒ spectra of polar and nonpolar molecules of coumarin 153 ͑C153͒ and pyrene in solution and in a polymer film of polymethylmethacrylate ͑PMMA͒ have been measured in the UV-visible region at room temperature. The shape of the EA spectra of C153 in benzene, 1,4-dioxane, or monochlorobenzene remarkably depends on the angle between the polarization direction of the absorption light and the applied electric field, whereas the EA spectra of C153 doped in PMMA show only the Stark shift and the field-induced change in spectral shape is negligible. These results demonstrate that C153 is reoriented by application of electric fields in solution, but the molecules are immobilized in a PMMA film. Based on the EA spectra, electric dipole moments both in the ground state and in the excited state have been evaluated for C153 in different solvents. In the EA spectra of pyrene, only the Stark shift is observed both in solution and in PMMA, indicating that the field-induced molecular reorientation does not occur both in solution and in PMMA. The change in dipole moment of C153 as well as the change in molecular polarizability of pyrene following absorption is much larger in solution than that in PMMA.

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The Solvent Effect on Fluorescence Spectrum, Change of Solute-Solvent Interaction during the Lifetime of Excited Solute Molecule

Cited by 569 publications

References 4 publications

The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data

The protein fluorescence and structural toolkit: Database and programs for the analysis of protein fluorescence and structural data

Picosecond time-dependent Stokes shift studies of fluoroprobe in liquid solution

Comparative study of electroabsorption spectra of polar and nonpolar organic molecules in solution and in a polymer film

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