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 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.

Design of vesicle prototissues as a model for cellular tissues.

Synthesizing biomimetic prototissues with predictable physical properties is a promising tool for the study of cellular tissues, as they would enable to test systematically the role of individual physical mechanisms on complex biological processes. The aim of this study is to design a biomimetic cohesive tissue with tunable mechanical properties by the controlled assembly of giant unillamelar vesicles (GUV). GUV-GUV specific adhesion is mediated by the inclusion of the streptavidin-biotin pair, or DNA complementary strands. Using a simple assembly protocol, we are capable of synthesizing vesicle prototissues of spheroidal or sheet-like morphologies, with predictable cell-cell adhesion strengths, typical sizes, and degree of compaction.