Abstract
We have studied primary processes of ultrafast photoisomerization reactions of photoactive yellow protein (PYP) and visual rhodopsin (Rh) as well as ultrafast photoinduced electron transfer reactions of flavoproteins (FP) by means of the fs fluorescence up-conversion method. On the basis of these studies, we have examined the effects of the protein nanospace (PNS), where the chromophore is held, on the dynamics and mechanisms of the ultrafast and highly efficient photoinduced reactions of these proteins. In this article, we discuss mainly results of our comparative fluorescence dynamics studies on wild type (w. -t.) PYP, it’s site-directed mutants, analogues with replaced chromophore and FP, including the coherent vibrations in the ultrafast fluorescence decays of w. -t. PYP and mutants in the course of the photoisomerization, ultrafast dynamic Stokes shift of fluorescence of PYP analogues, and ultrafast electron transfer of FP.
