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Phosphorylation disrupts long-distance electron transport in cytochrome c

Author

Listed:
  • Alexandre M. J. Gomila

    (The Barcelona Institute for Science and Technology (BIST)
    CIBER-BBN, ISCIII)

  • Gonzalo Pérez-Mejías

    (Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC))

  • Alba Nin-Hill

    (University of Barcelona, Department of Inorganic and Organic Chemistry, Institute of Theoretical Chemistry (IQTCUB))

  • Alejandra Guerra-Castellano

    (Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC))

  • Laura Casas-Ferrer

    (The Barcelona Institute for Science and Technology (BIST)
    UMR 5221 CNRS-Université de Montpellier)

  • Sthefany Ortiz-Tescari

    (The Barcelona Institute for Science and Technology (BIST))

  • Antonio Díaz-Quintana

    (Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC))

  • Josep Samitier

    (The Barcelona Institute for Science and Technology (BIST)
    CIBER-BBN, ISCIII
    University of Barcelona (UB), Faculty of Physics)

  • Carme Rovira

    (University of Barcelona, Department of Inorganic and Organic Chemistry, Institute of Theoretical Chemistry (IQTCUB)
    Catalan Institution for Research and Advanced Studies (ICREA))

  • Miguel A. Rosa

    (Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC))

  • Irene Díaz-Moreno

    (Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC))

  • Pau Gorostiza

    (The Barcelona Institute for Science and Technology (BIST)
    CIBER-BBN, ISCIII
    Catalan Institution for Research and Advanced Studies (ICREA))

  • Marina I. Giannotti

    (The Barcelona Institute for Science and Technology (BIST)
    CIBER-BBN, ISCIII
    University of Barcelona (UB), Faculty of Chemistry)

  • Anna Lagunas

    (The Barcelona Institute for Science and Technology (BIST)
    CIBER-BBN, ISCIII)

Abstract

It has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c1 subunit of the cytochrome bc1 can proceed at long-distance through the aqueous solution. Cytochrome c is thought to adjust its activity by changing the affinity for its partners via Tyr48 phosphorylation, but it is unknown how it impacts the nanoscopic environment, interaction forces, and long-range electron transfer. Here, we constrain the orientation and separation between cytochrome c1 and cytochrome c or the phosphomimetic Y48pCMF cytochrome c, and deploy an array of single-molecule, bulk, and computational methods to investigate the molecular mechanism of electron transfer regulation by cytochrome c phosphorylation. We demonstrate that phosphorylation impairs long-range electron transfer, shortens the long-distance charge conduit between the partners, strengthens their interaction, and departs it from equilibrium. These results unveil a nanoscopic view of the interaction between redox protein partners in electron transport chains and its mechanisms of regulation.

Suggested Citation

  • Alexandre M. J. Gomila & Gonzalo Pérez-Mejías & Alba Nin-Hill & Alejandra Guerra-Castellano & Laura Casas-Ferrer & Sthefany Ortiz-Tescari & Antonio Díaz-Quintana & Josep Samitier & Carme Rovira & Migu, 2022. "Phosphorylation disrupts long-distance electron transport in cytochrome c," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34809-1
    DOI: 10.1038/s41467-022-34809-1
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    References listed on IDEAS

    as
    1. R. Merkel & P. Nassoy & A. Leung & K. Ritchie & E. Evans, 1999. "Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy," Nature, Nature, vol. 397(6714), pages 50-53, January.
    2. Anna Lagunas & Alejandra Guerra-Castellano & Alba Nin-Hill & Irene Díaz-Moreno & Miguel A. De la Rosa & Josep Samitier & Carme Rovira & Pau Gorostiza, 2018. "Long distance electron transfer through the aqueous solution between redox partner proteins," Nature Communications, Nature, vol. 9(1), pages 1-7, December.
    Full references (including those not matched with items on IDEAS)

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