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Proceedings Paper

The Application Of Picosecond-Resolved Fluorescence Spectroscopy In The Study Of Flavins And Flavoproteins
Author(s): Antonie J.W.G Visser; Arie van Hoek
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Paper Abstract

Picosecond relaxation processes of flavins and flavoproteins were investigated with mode-locked and synchronously pumped lasers as source of excitation and time-correlated single photon counting in detection. Free flavin rotational correlation times of 80-150 ps (values depending on the flavin derivative used) could be precisely determined. Picosecond-resolved fluorescence of the flavin bound in the electron-carrier protein flavodoxin from Desulfovibrio vulgaris yields a fluorescence lifetime component of 30 ps in the fluorescence decay. Time-resolved tryptophan fluorescence in flavodoxin exhibits a short lifetime component, which is attributed in part to energy transfer from tryptophan to flavin. Three-dimensional fluorescence spectroscopy and fluorescence anisotropy decay analysis of the two tryptophan residues in flavodoxin provide new evidence for specific flavin-tryptophan interaction. Finally, picosecond-resolved spectroscopy enables the direct measurement of energy transfer between two different chromophores in a protein, from which topographical details can be inferred.

Paper Details

Date Published: 24 June 1988
PDF: 9 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945369
Show Author Affiliations
Antonie J.W.G Visser, Agricultural University (The Netherlands)
Arie van Hoek, Agricultural University (The Netherlands)


Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)

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