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The electron distribution in the activated state of cytochrome c oxidase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 32018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, article id 7502Article in journal (Refereed) Published
Abstract [en]

Cytochrome c oxidase catalyzes reduction of O-2 to H2O at a catalytic site that is composed of a copper ion and heme group. The reaction is linked to translocation of four protons across the membrane for each O-2 reduced to water. The free energy associated with electron transfer to the catalytic site is unequal for the four electron-transfer events. Most notably, the free energy associated with reduction of the catalytic site in the oxidized cytochrome c oxidase (state O) is not sufficient for proton pumping across the energized membrane. Yet, this electron transfer is mechanistically linked to proton pumping. To resolve this apparent discrepancy, a high-energy oxidized state (denoted O-H) was postulated and suggested to be populated only during catalytic turnover. The difference between states O and O-H was suggested to be manifested in an elevated midpoint potential of Cu-B in the latter. This proposal predicts that one-electron reduction of cytochrome c oxidase after its oxidation would yield re-reduction of essentially only Cu-B. Here, we investigated this process and found similar to 5% and similar to 6% reduction of heme a(3) and Cu-B, respectively, i.e. the apparent redox potentials for heme a(3) and CuB are lower than that of heme a.

Place, publisher, year, edition, pages
2018. Vol. 8, article id 7502
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-157778DOI: 10.1038/s41598-018-25779-wISI: 000431955100007PubMedID: 29760451OAI: oai:DiVA.org:su-157778DiVA, id: diva2:1235752
Available from: 2018-07-27 Created: 2018-07-27 Last updated: 2018-07-27Bibliographically approved

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