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Phosphorylation disrupts long-distance electron transport in cytochrome c
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Journal Article
Phosphorylation disrupts long-distance electron transport in cytochrome c
2022
Overview
It has been recently shown that electron transfer between mitochondrial cytochrome
c
and the cytochrome
c
1
subunit of the cytochrome
bc
1
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
c
1
and cytochrome
c
or the phosphomimetic Y48
p
CMF 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.
Electron transfer between mitochondrial cytochrome
c
and subunit of cytochrome
bc
1
can proceed at long distance. Here the authors investigate further the mechanism and show phosphorylation regulation of the interactions between the protein partners in the electron transport chain.
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