Phosphorylation disrupts long-distance electron transport in cytochrome c

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 (), Miguel A. Rosa, Irene Díaz-Moreno (), Pau Gorostiza (), Marina I. Giannotti () and Anna Lagunas ()
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Alexandre M. J. Gomila: The Barcelona Institute for Science and Technology (BIST)
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)
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)
Carme Rovira: University of Barcelona, Department of Inorganic and Organic Chemistry, Institute of Theoretical Chemistry (IQTCUB)
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)
Marina I. Giannotti: The Barcelona Institute for Science and Technology (BIST)
Anna Lagunas: The Barcelona Institute for Science and Technology (BIST)

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-34809-1

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