Phosphorylation disrupts long-distance electron transport in cytochrome c.

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 phosphoryla

SUBMITTER: Gomila AMJ 

PROVIDER: S-EPMC9675734 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature