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Femtosecond and picosecond fluorescence of native bacteriorhodopsin and a nonisomerizing analog
Author(s) -
Haacke S.,
Schenkl S.,
Vinzani S.,
Chergui M.
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10092
Subject(s) - bacteriorhodopsin , chemistry , picosecond , excited state , intermolecular force , intramolecular force , fluorescence , femtosecond , photochemistry , relaxation (psychology) , fluorescence spectroscopy , ultrafast laser spectroscopy , vibrational energy relaxation , spectroscopy , molecule , chemical physics , atomic physics , stereochemistry , laser , optics , organic chemistry , psychology , social psychology , biochemistry , physics , quantum mechanics , membrane
The spectrally and temporally resolved fluorescence properties of native bacteriorhodopsin (bR) and bR reconstituted with a nonisomerizing analog of the retinal Schiff base (bR5.12) are examined. The first attempt to experimentally monitor the excited state relaxation processes in both type of pigments using ultrafast fluorescence spectroscopy is reported. The fluorescence is emitted from retinal molecules in an all‐trans configuration. Substantial energy relaxation involves very fast intramolecular and intermolecular vibrational modes and these are shown to occur on a time scale faster than isomerization. The possible contribution of dielectric interaction between the retinal Schiff base and the protein environment for the excited state energy relaxation is discussed. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 306–309, 2002