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Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/192910
Phosphorylation disrupts long-distance electron transport in cytochrome c
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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.
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GOMILA, Alexandre m. j., PÉREZ-MEJÍAS, Gonzalo, NIN-HILL, Alba, GUERRA-CASTELLANO, Alejandra, CASAS-FERRER, Laura, ORTIZ TESCARI, Sthefany, DÍAZ QUINTANA, Antonio, SAMITIER I MARTÍ, Josep, ROVIRA I VIRGILI, Carme, DE LA ROSA, Miguel a., DÍAZ MORENO, Irene, GOROSTIZA, Pau, GIANNOTTI, Marina inés, LAGUNAS, Anna. Phosphorylation disrupts long-distance electron transport in cytochrome c. _Nature Communications_. 2022. Vol. 13, núm. 7100. [consulta: 25 de febrer de 2026]. ISSN: 2041-1723. [Disponible a: https://hdl.handle.net/2445/192910]