Our understanding of metalloporphyrin resonance Raman spectra has advanced to the point where it is possible to obtain detailed information about the structure of the heme group in situ in heme proteins. The porphyrin skeletal mode frequencies can be analyzed in terms of the ligation and spin state of the heme and may provide information about protein-induced stresses. The high-frequency region of the spectrum also contains bands due to vibrations of the porphyrin peripheral substituents, which are potentially monitors of the protein contacts. In the low-frequency region, it is possible to locate bands, at least in some states of the heme protein, which are associated with vibrations of the axial ligands. They give direct information about the nature of the bonding to exogenous ligands or to the proximal protein residue. Thus, a variety of evidence is potentially available in the resonance Raman spectra from which a fairly complete picture of the heme site can be assembled for a particular protein in its various functional states. Detailed studies have been pursued for paradigmatic heme proteins, including myoglobin, hemoglobin, cytochrome c, horseradish peroxidase, and cytochrome oxidase. These studies provide a substantial data base from which the exploration of lesser known systems can be launched. Another extension of current knowledge to new frontiers is in the time domain, since pulsed lasers now make it feasible to carry out time-resolved resonance Raman studies on heme protein reactions. Time-resolved resonance Raman spectroscopy is capable of elucidating the temporal evolution of heme structure and provides a link between heme chemistry and protein dynamics. This link is being elucidated for hemoglobin and cytochrome c, where specific heme intermediates have been identified following ligand photodissociation or electron transfer.