The temporally overlapping, ultrafast electronic and vibrational dynamics of a model five-coordinate, highspin heme in a nominally isotropic solvent environment has been studied for the first time with three complementary ultrafast techniques: transient absorption, time-resolved resonance Raman Stokes, and time-resolved resonance Raman anti-Stokes spectroscopies. Vibrational dynamics associated with an evolving ground-state species dominate the observations. Excitation into the blue side of the Soret band led to very rapid S-2 -> S-1 decay (sub-100 fs), followed by somewhat slower (800 fs) S-1 -> S-0* nonradiative decay. The initial vibrationally excited, non-Boltzmann S-0* state was modeled as shifted to lower energy by 300 cm(-1) and broadened by 20%. On a similar to 10 ps time scale, the S-0* state evolved into its room-temperature, thermal distribution S-0 profile largely through VER. Anti-Stokes signals disappear very rapidly, indicating that the vibrational energy redistributes internally in about 1-3 ps from the initial accepting modes associated with S-1 -> S-0 internal conversion to the rest of the macrocycle. Comparisons of anti-Stokes mode intensities and lifetimes from TRARRS studies in which the initial excited state was prepared by ligand photolysis [Mizutani, T.; Kitagawa, T. Science 1997, 278, 443, and Chem. Rec. 2001, 1, 258] suggest that, while transient absorption studies appear to be relatively insensitive to initial preparation of the electronic excited state, the subsequent vibrational dynamics are not. Direct, time-resolved evaluation of vibrational lifetimes provides insight into fast internal conversion in hemes and the pathways of subsequent vibrational energy flow in the ground state. The overall similarity of the model heme electronic dynamics to those of biological systems may be a sign that the protein's influence upon the dynamics of the heme active site is rather subtle.