by Keyword: cardiolipin
Gomila, AMJ, Pérez-Mejías, G, Nin-Hill, A, Guerra-Castellano, A, Casas-Ferrer, L, Ortiz-Tescari, S, Díaz-Quintana, A, Samitier, J, Rovira, C, De la Rosa, MA, Díaz-Moreno, I, Gorostiza, P, Giannotti, MI, Lagunas, A, (2022). Phosphorylation disrupts long-distance electron transport in cytochrome c Nature Communications 13, 7100 
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.© 2022. The Author(s).
JTD Keywords: apoptosis, binding, cardiolipin, complex, dynamics, force, respiration, structural basis, tyrosine phosphorylation, Histone chaperone activity
