Abstract
We report the resonance Raman spectra of cytochrome c oxidase, both solubilized and in electron transport particles using laser excitation near the Soret band. As in the spectra of other hemoproteins, such as cytochrome c , the shape and intensity of a number of bands change when the oxidation state is varied. However, one of the hemes of solubilized cytochrome c oxidase shows redox behavior which is anomalous. Spectra of electron transport particles are dominated by cytochrome c oxidase. There are, however, definite differences between spectra of solubilized cytochrome c oxidase and electron transport particles in the oxidized states.
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