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Updated: Aug 16, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
Is a third proton-conducting pathway operative in bacterial cytochrome c oxidase?
J Salje1, B Ludwig, O-M H Richter
1Molecular Genetics Group, Institute for Biochemistry, Johann Wolfgang Goethe Universität, Biozentrum, Marie-Curie-Strasse 9, D-60439 Frankfurt/M, Germany.
Abstract:
Despite the existence of several three-dimensional structures of cytochrome c oxidases, a detailed understanding of pathways involved in proton movements through the complex remains largely elusive. Next to the two well-established pathways (termed D and K), an additional proton-conducting network ('H-channel') has been proposed for the beef heart enzyme. Yet, our recent mutational studies on corresponding residues of the Paracoccus denitrificans cytochrome c oxidase provide no clues that such a pathway operates in the prokaryotic enzyme.
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