Abstract
Summary Resonance enhancement of high and low frequency vibrational modes of oxidized cytochrome a 3 in several cytochrome oxidase species have been observed when flowing samples and excitation frequencies of 413.1 nm and 406.7 nm were used. The data are interpreted by excitation profile arguments which incorporate optical parameters from the spectra of cytochromes a and a 3 deduced by Vanneste ( Biochemistry 5 , 838–848 (1966)). The carbonyl of oxidized cytochrome a 3 is conjugated with the heme a π-electron system independent of both its iron spin state and the redox state of cytochrome a . This contrasts with the behavior of cytochrome a and of reduced cytochrome a 3 . Mechanistic implications of these conformational differences are briefly considered.
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