Studies of the kinetics of photoinduced ligand dissociation in the heme-proteins have been largely confined to excitation in the visible region of the absorption spectrum. We propose to vary the wavelength of excitation using a parametric amplifier which we have set up and is now operational. One key issue will be the effect on the cage dynamics since the kinetic energy of the exiting ligand can vary with the excitation wavelength, i.e., the energy deposited in the molecule. In addition we plan to determine if the electronic absorption band in the near infrared, which has been ignored in discussion of the kinetics of dissociation, is the dissociative state to which all excitations relax by a direct picosecond excitation experiment. In our experiments on the role of hydrogen bonding on the dynamics of structural changes in the dimers of 7-azaindole we plan to investigate the kinetics of the ground state structural change from tautomer back to dimer. Transient absorption, laser induced fluorescence and temperature dependent measurements will be used to gain information barrier height and the cooperative simultaneous or sequential nature of the double proton transfer process. In our studies of energy relaxation we plan to gain information on the competitive effects of intramolecular and intermolecular hydrogen bonding on the energy decay process. Using transient absorption and fluorescence measurements on ortho-hydroxy benzophenone in a variety of solvents differing in structure and hydrogen bonding strength we aim to gain insight into possible ground state equilibria between different structures and the effects on excited state decay channels.