Abstract The applications of Raman and absorption spectroscopy to understand the photophysics and the dynamics of hemoglobin and myoglobin are discussed. The extension of these techniques to the picosecond and the femtosecond domains is described. Study of hemeprotein reactivity on this ultrafast time scale is advantageous because it simplifies the experimental observation to those times before the ligand has diffused out of the heme pocket. The fate of transient heme species produced by ligand photodissociation and the vibrational cooling of the heme and the subsequent delocalization of strain energy in hemoglobin are discussed. These subjects are considered in the context of other experimental and theoretical results.