Flavins are the chromophores in several blue-light-sensitive photoreceptor proteins and act as redox cofactors in many enzymes that are relevant for biological processes. Despite their biological relevance and numerous detailed optical investigations of their photophysical properties, the ultrafast nonequilibrium dynamics of their elementary optical excitations are not yet fully known. Here, we use ultrafast coherent vibrational spectroscopy with a 10-fs time resolution in the 450-nm spectral range to study their excited state coherent vibrational dynamics. We observe that coherent wavepacket motion along high-frequency C–C stretching modes with a ∼20-fs period is rapidly damped on a 20-fs time scale. In contrast, coherent motion along several low-frequency modes persists for much longer. We attribute this to a mode-selective intramolecular vibrational energy redistribution driven by nonadiabatic couplings between the optical bright state and a close-lying dark electronic state, in accordance with model calculations. Our results may be of relevance for the formation of long-lived radical pair states in magnetic-field sensitive proteins.
Timmer et al. (Sat,) studied this question.