Time-resolved multiphoton ionization mass spectrometry coupled with Rydberg Fingerprint Spectroscopy (RFS) has been used to analyze the structural and electronic dynamics of N,N-dimethylphenethylamine (PENNA) and N,N-dimethylcyclohexethylamine (CENNA). In PENNA, the molecule converts from 3p to 3s on a time scale of 149 is, a process that is reflected in the mass spectrum as the onset of fragmentation. Once in 3s, the overall signal intensity of the PENNA 3s signal shows biexponential decay kinetics, which is attributed to the electronic curve crossing from the Rydberg state to a dissociative antibonding orbital of the ethylenic bridge. This curve crossing exemplifies a possible fragmentation pathway observed in electron capture dissociation of proteins. The initially fast reaction (1.3 ps) is greatly slowed down as a result of an apparent relaxation process with a 5.6 ps time constant. The electron binding energy of the 3s Rydberg state of PENNA is observed to shift with a time constant of 4.8 ps, which is correlated to a cation-pi interaction driven conformeric rearrangement.