In this review article, we discuss surface-enhanced resonance Raman scattering (SERRS) studies of hemeproteins such as myoglobin, hemoglobin, and cytochrome on various metal substrates; for example, colloidal silver nanoparticles coated with and without self-assembled monolayers (SAM), a roughened silver electrode protected with and without SAM, a sharp silver tip, and colloidal gold nanoparticles coated with and without SAM. Moreover, we classify the studies in terms of an excitation wavelength; namely, excitation at the B- (Soret) band, Q- (α and β) band, and in the near infrared (NIR) range. In the SERRS studies with B band excitation, it has been shown that the hemeprotein on a silver surface takes a non-native form through detachment from the heme pocket in the protein. With Q band excitation, on the other hand, the change in SERRS has been explained by the orientation of the hemeprotein on the surface. Even by excitation in the NIR range, the peak positions are consistent with the assignment of the major vibrational modes of heme despite there being no resonance Raman effect. Thus, the SERRS of hemeproteins is influenced by a resonance Raman effect, LSPR, and interactions with the metal surface such as structural changes, orientation, and selective adsorption. Moreover, we discuss how SERRS has been applied to complicated biological systems such as living cells containing hemeprotein. For mitochondria, a change of the oxidation-state was observed by the electron transport chain in the cell and at different positions. As an example of a biomedical application of SERRS, the sensitive detection of malaria is presented.