On the excitation wavelength dependence of the fluorescence of bacteriorhodopsin

We present a systematic study of the time-integrated fluorescence of native bacteriorhodopsin, as a function of excitation wavelength across the visible absorption band. While the fluorescence max. is unaffected, the spectrum broadens on the high-energy side, with decreasing excitation wavelengths. In addn., there is no mirror image relation between emission and absorption, even for the longest excitation wavelengths. By comparison with the retinal cation in soln., we attribute these observations to vibrationally hot emission, and to the topol. of the excited state surface on the way to isomerization.


Published in:
Chemical Physics Letters, 441, 4-6, 322-326
Year:
2007
Keywords:
Note:
CAN 147:229109
6-3
General Biochemistry
Laboratoire de Spectroscopie Ultrarapide, BSP, ISIC,Ecole Polytechnique Federale de Lausanne,Lausanne,Switz.
Journal
0009-2614
written in English.
Other identifiers:
Laboratories:




 Record created 2006-02-27, last modified 2018-03-17


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)