Accessibility of the Cytochrome a heme in Cytochrome c Oxidase to Exchangeable Protons.

The comparison of the resonance Raman spectrum of cytochrome a(2+) from cytochrome oxidase in deuterated buffers to that in protonated buffers reveals many lines that have different frequency or intensity. Some of the frequency differences are very large, e.g., on the order of 10 cm(-1). From these differences in the Raman spectra we infer that the heme pocket is readily accessible to protons and that labile groups are either on the heme or interact strongly with it. These data suggest the possibility of direct participation in proton translocation and/or oxygen protonation by the heme of cytochrome a.