ArticleProceedings of the National Academy of Sciences of the United States of America2022
Respiratory complex I with charge symmetry in the membrane arm pumps protons.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 16 citations in OpenAlex.
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
- Selective inhibition of respiratory complex I reveals a bioenergetic vulnerability inbioRxiv : the preprint server for biology · 2026Article
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Directed mutagenesis of large multi-subunit protein complexes by plasmid sub-fragmentation.Scientific reports · 2026Article
- Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.Nature communications · 2026Article
- Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.International journal of molecular sciences · 2026Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Quinone Catalysis Modulates Proton Transfer Reactions in the Membrane Domain of Respiratory Complex I.Journal of the American Chemical Society · 2023Article
- Optimization of hydrogen production in Enterobacter aerogenes by Complex I peripheral fragments destruction and maeA overexpression.Microbial cell factories · 2023Article
- Horizontal proton transfer across the antiporter-like subunits in mitochondrial respiratory complex I.Chemical science · 2023Article
- HScientific reports · 2023Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, is essential for cellular energy metabolism coupling NADH oxidation to proton translocation. The mechanism of proton translocation by complex I is still under debate. Its membrane arm contains an unusual central axis of polar and charged amino acid residues connecting the quinone binding site with the antiporter-type subunits NuoL, NuoM, and NuoN, proposed to catalyze proton translocation. Quinone chemistry probably causes conformational changes and electrostatic interactions that are propagated through these subunits by a conserved pattern of predominantly lysine, histidine, and glutamate residues. These conserved residues are thought to transfer protons along and across the membrane arm. The distinct charge distribution in the membrane arm is a prerequisite for proton translocation. Remarkably, the central subunit NuoM contains a conserved glutamate residue in a position that is taken by a lysine residue in the two other antiporter-type subunits. It was proposed that this charge asymmetry is essential for proton translocation, as it should enable NuoM to operate asynchronously with NuoL and NuoN. Accordingly, we exchanged the conserved glutamate in NuoM for a lysine residue, introducing charge symmetry in the membrane arm. The stably assembled variant pumps protons across the membrane, but with a diminished H
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