Phosphorylation disrupts long-distance electron transport in cytochrome c-Reference-Cited by-同舟云学术

Phosphorylation disrupts long-distance electron transport in cytochrome c

Published:2022-10-12 Issue: Volume: Page:
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Author:

Gomila Alexandre¹,Pérez-Mejías Gonzalo²^ORCID,Hill Alba Nin³^ORCID,Guerra Alejandra⁴,Casas-Ferrer Laura¹,Ortiz-Tescari Sthefany¹,Díaz-Quintana Antonio⁵^ORCID,Samitier Josep⁶,Rovira Carme⁷^ORCID,Rosa Miguel A. De la⁸^ORCID,Díaz-Moreno Irene⁹^ORCID,Gorostiza Pau⁶^ORCID,Giannotti Marina¹⁰^ORCID,Lagunas Anna¹¹^ORCID

Affiliation:

1. Institute for Bioengineering of Catalonia (IBEC)

2. Instituto de Investigaciones Químicas-cicCartuja

3. Universitat de Barcelona

4. Institute of Chemical Research (IIQ-CSIC)

5. University of Seville - CSIC

6. Institute for Bioengineering of Catalonia

7. University of Barcelona

8. Universidad de Sevilla & CSIC

9. Instituto de Investigaciones Químicas, Universidad de Sevilla - CSIC

10. Biomedical Research Networking Center in Bioengineering, Biomaterials, and Nanomedicine (CIBER-BBN)

11. Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine

Abstract

Abstract It has been recently shown that electron transfer (ET) between mitochondrial cytochrome c (Cc) and the cytochrome c1 subunit of the cytochrome bc1 (Cc1) and Cc can proceed at long-distance through the aqueous solution. Cc 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 ET. Here, we constrain the orientation and separation between Cc1 and Cc or the phosphomimetic Y48pCMF Cc, and deploy an array of single-molecule, bulk, and computational methods to investigate the molecular mechanism of ET regulation by Cc phosphorylation.. We demonstrate that phosphorylation impairs long-range ET, 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.

Publisher

Research Square Platform LLC

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