Abstract
The all-trans to 13-cis photoisomerization of the retinal chromophore in bacteriorhodopsin (bR) acts as a strong steric and electronic perturbation for the protein environment, thereby driving the proton pump mechanism. Photoexcitation and torsional movement are expected to be paralleled by various intra- and intermolecular relaxation processes. According to femtosecond (fs) time-resolved optical absorption spectroscopy the electronic ground state is reached after about 500 fs (J) [1-4], which then relaxes on a 3 ps time-scale to the K-state with the chromophore in 13-cis configuration.
© 2002 Optical Society of America
PDF ArticleMore Like This
Feng Gai, Kenton C. Hasson, and Philip A. Anfinrud
FC.5 International Conference on Ultrafast Phenomena (UP) 1996
T. Kobayashi, T. Saito, and H. Ohtani
WC3 International Conference on Ultrafast Phenomena (UP) 2002
M. Liebel and P. Kukura
JSIV_2_5 International Quantum Electronics Conference (IQEC) 2013