Abstract
The relationship between cardiolipin and cytochrome c oxidase in maintaining electron transfer activity in mitochondrial membranes has recently been put into question (Powell and Abramovitch, 1985). The rate of electron transfer is determined by the electrostatic interactions that exist between the specific binding domains on the oxidase and the positively charged residues on ferrocytochrome c (Sinjorgo et al., 1987). The role that negatively charged acidic phospholipids play in influencing electron flow in this reaction has not been conclusively documented. It has been reported that the interaction between cytochrome c oxidase and cardiolipin not only modulates enzyme activity but induces polymorphic phase changes in the lipid structure in the membrane environment in which the enzyme is located (Rietveld et al., 1987).
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© 1988 Springer Science+Business Media New York
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Trivedi, A., Wearring, A.V., Kohlwein, S.D., Paltauf, F., Tustanoff, E.R. (1988). Functional Importance of Mitochondrial Cardiolipin in Yeast Cytochrome c Oxidase Activity. In: Lemasters, J.J., Hackenbrock, C.R., Thurman, R.G., Westerhoff, H.V. (eds) Integration of Mitochondrial Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2551-0_9
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DOI: https://doi.org/10.1007/978-1-4899-2551-0_9
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