Abstract
A thorough characterization of the early time sub-100 fs relaxation dynamics of biologically relevant chromophores is of crucial importance for a complete understanding of the mechanisms regulating the ultrafast dynamics of the relaxation processes in more complex multichromophoric light-harvesting systems. While chlorophyll a has already been the object of several investigations, little has been reported on chlorophyll b, despite its pivotal role in many functionalities of photosynthetic proteins. Here the relaxation dynamics of chlorophyll b in the ultrafast regime have been characterized using 2D electronic spectroscopy. The comparison of experimental measurements performed at room temperature and 77 K allows the mechanisms and the dynamics of the sub-100 fs relaxation dynamics to be characterized, including spectral diffusion and fast internal conversion assisted by a specific set of vibrational modes.