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Structure paper

TitleA carboxylate switch point controls long-range energy transduction in respiratory Complex I.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateJul 1, 2026
AuthorsAdel Beghiah / Patricia Saura / Terezia Kovalova / Franziska Hoeser / Thorsten Friedrich / Ville R I Kaila /
PubMed AbstractComplex I is a highly intricate membrane-bound protein complex that powers the cellular energy metabolism by a long-range ( > 300 Å) proton-coupled electron transfer (PCET) reaction. Here, we ...Complex I is a highly intricate membrane-bound protein complex that powers the cellular energy metabolism by a long-range ( > 300 Å) proton-coupled electron transfer (PCET) reaction. Here, we investigate the highly debated coupling mechanism of Complex I by probing the charge transfer reaction along its functionally central carboxylate pathway (E-channel). By combining biophysical and site-directed mutagenesis experiments with high-resolution (2.6-2.8 Å) cryo-electron microscopy (cryo-EM) and multiscale simulations, we identify a conserved carboxylate switch point (D79) that mediates proton transfer by establishing a kinetic gate and couples the redox chemistry to proton pumping. We find that mutation of the identified site, as found in patients suffering from severe neurodegenerative disorders, drastically perturbs the charge transfer mechanism, and results in a 20% PCET activity. Our combined findings illustrate mechanistic principles of molecular gates underlying long-range charge transfer reactions, and show how disease mutations perturb the function of conserved switch points in energy transduction.
External linksNat Commun / PubMed:42386739 / PubMed Central
MethodsEM (single particle)
Resolution2.59 - 3.0 Å
Structure data

55748

9taj

EMDB-55748, PDB-9taj:
E. coli Complex I WT purified in LMNG
Method: EM (single particle) / Resolution: 3.0 Å

55749

9tak

EMDB-55749, PDB-9tak:
Local refinement of E. coli Complex I WT membrane domain in LMNG
Method: EM (single particle) / Resolution: 2.8 Å

55750

9tal

EMDB-55750, PDB-9tal:
Local refinement of E. coli Complex I WT hydrophilic domain in LMNG
Method: EM (single particle) / Resolution: 2.66 Å

55751

9tam

EMDB-55751, PDB-9tam:
E. coli Complex I D79N NuoA mutant purified in LMNG
Method: EM (single particle) / Resolution: 2.96 Å

55752

9tan

EMDB-55752, PDB-9tan:
Local refinement of E. coli Complex I D79N NuoA mutant hydrophilic domain in LMNG
Method: EM (single particle) / Resolution: 2.59 Å

55753

9tao

EMDB-55753, PDB-9tao:
Local refinement of E. coli Complex I D79N NuoA mutant membrane domain in LMNG
Method: EM (single particle) / Resolution: 2.61 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-CA:
Unknown entry

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

ChemComp-LFA:
EICOSANE

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-TRD:
TRIDECANE

ChemComp-UQ8:
Ubiquinone-8

ChemComp-HOH:
WATER

ChemComp-7PH:
(1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate

Source
  • escherichia coli bw25113 (bacteria)
  • escherichia coli bl21(de3) (bacteria)
KeywordsPROTON TRANSPORT / bioenergetics / Leigh's syndrome

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