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Structure paper

TitleStructural changes shifting the redox potential of the outlying cluster N1a in respiratory complex I.
Journal, issue, pagesStructure, Vol. 34, Issue 1, Page 175-183.e3, Year 2026
Publish dateJan 8, 2026
AuthorsDaniel Wohlwend / Thilo Seifermann / Emmanuel Gnandt / Marta Vranas / Stefan Gerhardt / Thorsten Friedrich /
PubMed AbstractEnergy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, is central to energy metabolism by coupling NADH oxidation and quinone reduction with proton translocation across the membrane. ...Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, is central to energy metabolism by coupling NADH oxidation and quinone reduction with proton translocation across the membrane. Electrons are transferred from the primary acceptor flavin mononucleotide via a chain of iron-sulfur clusters to quinone. The enigmatic cluster N1a is conserved, but not part of this electron transfer chain. We reported on variants of the complex in which N1a is not detectable by EPR spectroscopy. This was tentatively attributed to the lower redox potential of the variant N1a. However, it remained an open question, whether the variants contain this cluster at all. Here, we determined the structures of these variants by X-ray crystallography and cryogenic-electron microscopy. Cluster N1a is present in all variants and the shift of its redox potential is explained by nearby structural changes. A role of the cluster for the mechanism of the complex is discussed.
External linksStructure / PubMed:41265450
MethodsEM (single particle) / X-ray diffraction
Resolution1.844 - 2.6 Å
Structure data

52895

9q8i

EMDB-52895, PDB-9q8i:
Cryo-EM structure of E. coli complex I variant V96P/N142M (NuoE)
Method: EM (single particle) / Resolution: 2.35 Å

EMDB-52969: Cryo-EM Map of the membrane arm of respiratory complex I V96P/N142M (nuoE) used for the creation of a composite map
Method: EM (single particle) / Resolution: 2.32 Å

EMDB-52970: Cryo-EM consensus map of E. coli complex I V96P/N142M (NuoE)
Method: EM (single particle) / Resolution: 2.35 Å

EMDB-52971: focused map of the peripheral arm of E. coli complex I variant V96P/N142M (NuoE)
Method: EM (single particle) / Resolution: 2.32 Å

EMDB-52973: focused map of the junction between peripheral arm and membrane arm of E. coli respiratory complex I variant V96P/N142M (NuoE)
Method: EM (single particle) / Resolution: 2.32 Å

PDB-9he5:
Crystal structure of the oxidized respiratory complex I subunit NuoEF from Aquifex aeolicus, mutation V90P(NuoE)
Method: X-RAY DIFFRACTION / Resolution: 1.844 Å

PDB-9heg:
Crystal structure of the oxidized respiratory complex I subunit NuoEF from Aquifex aeolicus, mutation V136M(NuoE)
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-9hem:
Crystal structure of the oxidized respiratory complex I subunit NuoEF from Aquifex aeolicus, mutation V136M(NuoE), bound to NAD+
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-9hen:
Crystal structure of the oxidized respiratory complex I subunit NuoEF from Aquifex aeolicus, double mutation V90P and V136M(NuoE), bound to NAD+
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-NA:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-BU3:
(R,R)-2,3-BUTANEDIOL

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

ChemComp-CA:
Unknown entry

Source
  • escherichia coli (E. coli)
  • aquifex aeolicus vf5 (bacteria)
KeywordsOXIDOREDUCTASE / Complex I / NADH oxidoreductase / respiratory chain / iron-sulfur-cluster / flavin / cellular respiration / Fe-S-Cluster / flavoprotein / MEMBRANE PROTEIN / NADH ubiquinone oxidoreductase / electron transport / proton transport

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