BIROn - Birkbeck Institutional Research Online

    A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria

    Marechal, Amandine and Xu, J.-Y. and Genko, N. and Hartley, Andrew and Haraux, F. and Meunier, B. and Rich, P. (2020) A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria. Proceedings of the National Academy of Sciences of the United States of America , ISSN 0027-8424. (In Press)

    [img] Text
    Marechal-et-al_H-e_Stoichiometry_2020.pdf - Author's Accepted Manuscript
    Restricted to Repository staff only

    Download (875kB)
    [img]
    Preview
    Text
    31559a.pdf - Published Version of Record
    Available under License Creative Commons Attribution Non-commercial No Derivatives.

    Download (1MB) | Preview

    Abstract

    Mitochondria metabolise almost all of the oxygen that we consume, reducing it to water by cytochrome c oxidase (CcO). CcO maximises energy capture into the protonmotive force by pumping protons across the mitochondrial inner membrane. Forty years after the H+/e- stoichiometry was established, a consensus has yet to be reached on the route taken by pumped protons to traverse CcO’s hydrophobic core and on whether bacterial and mitochondrial CcOs operate via the same coupling mechanism. To resolve this, we exploited the unique amenability to mitochondrial DNA mutagenesis of the yeast S. cerevisiae to introduce single point mutations in the hydrophilic pathways of CcO to test function. From ADP/O ratio measurements on preparations of intact mitochondria, we definitely established that the D-channel, and not the H-channel, is the proton pump of the yeast mitochondrial enzyme, supporting an identical coupling mechanism in all forms of the enzyme.

    Metadata

    Item Type: Article
    School: School of Science > Biological Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Amandine Marechal
    Date Deposited: 16 Apr 2020 13:36
    Last Modified: 01 Dec 2020 08:48
    URI: https://eprints.bbk.ac.uk/id/eprint/31559

    Statistics

    Downloads
    Activity Overview
    64Downloads
    30Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item