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Phosphorylation disrupts long-distance electron transport in cytochrome c. | LitMetric

AI Article Synopsis

  • New research indicates that electron transfer between mitochondrial cytochrome c and cytochrome bc can happen over long distances in aqueous solutions.
  • Cytochrome c's activity is believed to be regulated by Tyr48 phosphorylation, which affects its interaction with partners, though the exact impact on electron transfer remains unclear.
  • The study reveals that phosphorylation hinders long-range electron transfer, alters the interaction distance between partner proteins, increases their binding strength, and disrupts equilibrium, providing insights into electron transport chain regulation.

Article Abstract

It has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c subunit of the cytochrome bc 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 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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9675734PMC
http://dx.doi.org/10.1038/s41467-022-34809-1DOI Listing

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