Abstract:
Retinal proteins are small transmembrane proteins working as photosensors - the
visual protein rhodopsin is the most prominent example - or as photo-activated
ion pumps in bacteria. According to textbooks the primary photo-reaction in
retinal proteins is isomerization of retinal.
But the most recent results from different groups show that faster intra- and
inter-molecular processes are also operative. In particular, it is of general
importance to understand how the protein controls the bond selectivity and the
speed of isomerization. We will report on femtosecond experiments, which reveal
new physics regarding the protonated retinal Schiff base in solvents and in the
protein matrix.