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Biochemical and biophysical studies on cytochromecoxidase. XVIII. Potentiometric titrations of cytochromecoxidase followed by circular dichroism

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Bioenergetics
0005-2728
Publisher
Elsevier
Publication Date
Volume
357
Issue
1
Identifiers
DOI: 10.1016/0005-2728(74)90108-x

Abstract

Abstract 1. Potentiometric circular dichroism titrations of cytochrome c oxidase, carried out in the absence of cytochrome c, confirm the potentiometric equivalence of the two heme a groups of cytochrome c oxidase. In the presence of cytochrome c, two different midpoint potentials are found for the two heme a groups of cytochrome c oxidase. 2. Circular dichroism difference spectra (reduced minus oxidized) of the two heme a components of cytochrome c oxidase have been obtained by means of this potentiometric titration. On reduction of the first heme a group a circular dichroism difference spectrum is obtained with peaks at 425, 442 and 602.5 nm; the second heme a group shows difference peaks at 434, 447 and 608 nm. Whereas both heme a groups contribute about equally to the absorbance difference spectrum, the second heme a group reduced contributes about twice as much to the circular dichroism difference spectrum as does the first heme a group. 3. From these spectral and circular dichroism differences it is concluded that, on reduction of or ligand binding to cytochrome c oxidase, conformational changes occur which affect the symmetry of the environments of the heme a groups.

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