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TitleTransient protein structure guides surface diffusion pathways for electron transport in membrane supercomplexes.
Journal, issue, pagesNat Commun, Year 2026
Publish dateFeb 5, 2026
AuthorsChun Kit Chan / Jonathan Nguyen / Corey F Hryc / Chitrak Gupta / Kevin Redding / William Dowhan / Matthew L Baker / Alberto Perez / Eugenia Mileykovskaya / Abhishek Singharoy /
PubMed AbstractThe exact biological role of mitochondrial supercomplexes remains debated, particularly their role in guiding redox proteins across membranes during energy conversion. We integrate multiscale ...The exact biological role of mitochondrial supercomplexes remains debated, particularly their role in guiding redox proteins across membranes during energy conversion. We integrate multiscale modeling and single particle cryo-electron microscopy (cryo-EM) to examine electron transfer in mitochondrial supercomplexes composed of complexes III and IV (CIII and CIV). Using bioinformatic and entropy-based methods, we generated structural ensembles capturing conformations of CIII's disordered QCR6 hinge within the yeast CIII2CIV2 supercomplex. Molecular and Brownian Dynamics simulations reveal that these negatively charged hinge states electrostatically couple with redox proteins, promoting their binding and directional diffusion across the membrane on millisecond timescales. Rather than hindering transfer, disorder lowers the diffusion barrier. Anionic lipids reinforce this recognition by retaining a membrane pool of redox proteins when hinge length is critical. Cryo-EM models of ΔQCR6 show large rearrangements, yet maintain a robust electrostatic environment enabling surface-mediated transfer despite reduced charge. Overall, electron carriers confined on bioenergetic membranes follow a refolding-guided diffusion mechanism that enhances supercomplex energy conversion efficiency by nearly 30%.
External linksNat Commun / PubMed:41644522
MethodsEM (single particle)
Resolution4.21 - 4.3 Å
Structure data

EMDB-71415: Yeast Respiratory SuperComplex - deltaQCR6
Method: EM (single particle) / Resolution: 4.21 Å

EMDB-71416: Yeast Respiratory SuperComplex - non uniform refinement
Method: EM (single particle) / Resolution: 4.3 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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