Abstract
In photosensory or photoactive proteins with chromophores absorbing in the visible region, such as rhodopsin (Rh) for vision, bacteriorhodopsin (bR), photoactive yellow protein (PYP) etc., light absorption leads to ultrafast and highly efficient reactions. Interestingly, despite quite different chromophores of these proteins, their behavior concerning the photoinduced primary processes in the protein nanospace in the course of the relaxation and twisting, including coherent processes seems to be similar. For instance, the fluorescence dynamics in all three proteins is nonexponential, no dynamic Stokes shift but a slight narrowing of the fluorescence spectra within first few picoseconds of the reaction were observed [1-3]. The spectral narrowing effect is most probably due to damping of coherently coupled intrachromophore high frequency modes and/or low frequency vibrations of environmental protein interacting with chromophore along the twisting coordinate. If this is the case, oscillatory behavior in fluorescence dynamics of photosensory proteins should be observed. To our knowledge, no such observation has been reported yet.
© 2002 Optical Society of America
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