Phosphorylation disrupts long-distance electron transport in cytochrome c

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 phosp...

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Detalles Bibliográficos
Autores: 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 Langa, Pablo Ignacio, Giannotti, Marina Inés, Lagunas, Anna
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/192910
Acceso en línea:https://hdl.handle.net/2445/192910
Access Level:acceso abierto
Palabra clave:Química bioinorgànica
Proteïnes
Bioinorganic chemistry
Proteins
Descripción
Sumario: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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