Resonance Raman spectra are reported on ferric, ferrous, and cyanide-bound cytochrome cbb(3) oxidase, and compared with other heme b and heme c containing enzymes. These spectra are used to assess the spin and ligation states of the hemes via the porphyrin marker band frequencies, and for the deoxy form of heme b(3), the status of the Fe-histidine bond via its stretching frequency. The cytochrome cbb(3) complex in its resting form contains six-coordinated low-spin hemes, c, a six-coordinated low-spin heme b, and a six-coordinated high-spin heme b(3). In the reduced form of the enzyme, heme b(3) is five-coordinated and high-spin, while hemes c and heme b remain six-coordinated and low-spin. The cyanide-bound spectrum is consistent with low-spin six-coordinated heme b(3). Our results indicate that the 235 cm(-1) mode observed in the reduced spectrum of cbb(3) can be assigned to the Fe2+-His of heme b(3). The upsilon(Fe2+-His) frequency is the highest among those reported to date for the heme-copper respiratory oxidases. Possible explanations for the atypical Fe-His bonding are discussed.