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  • Title: Circular-dichroic properties and secondary structure of Pseudomonas aeruginosa soluble cytochrome c oxidase.
    Author: Tordi MG, Silvestrini MC, Colosimo A, Provencher S, Brunori M.
    Journal: Biochem J; 1984 Mar 15; 218(3):907-12. PubMed ID: 6326749.
    Abstract:
    The c.d. spectra of Pseudomonas aeruginosa cytochrome c oxidase in the oxidized state and the reduced state are reported in the visible- and u.v. absorption regions. In the visible region the comparison between the spectra of reduced cytochrome c oxidase and ferrocytochrome c-551 allows the identification of the c.d. bands mainly due to the d1 haem chromophore in cytochrome c oxidase. In the near-u.v. region the assignment of some of the observed peaks to the haem groups and to the aromatic amino acid residues is proposed. A careful analysis of the data in the far-u.v. region leads to the determination of the relative amounts of alpha-helix and beta-sheet in the enzyme, giving for the first time a picture of its secondary structure. A significant difference in this respect between the reduced and the oxidized species is observed and discussed in the light of similar conclusions reported by other workers.
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