ArticleNature2013
Crystal structure of the entire respiratory complex I.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 382 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
382 citing papers in PubMed, 787 citations in OpenAlex.
- Ferric derisomaltose augments intrinsic skeletal muscle electron transport chain activity in heart failure: A FERRIC-HF II molecular substudy.European journal of heart failure · 2025Trial
- H4K12 Lactylation Regulates NDUFS7 to Drive Microglia Reverse Electron Transport in Spinal Cord Injury.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
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- Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026Review
- A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Nature communications · 2026Article
- A Bacillales-specific tubular scaffold essential for NADH dehydrogenase activity.Nature communications · 2026Article
- Mitochondrial complex I deficiency-associated diseases and models.Cellular and molecular life sciences : CMLS · 2026Review
- 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
- Review
- Climate-associated natural selection in the human mitochondrial genome.Molecular biology and evolution · 2026Article
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- Mitochondrial hyperoxidation contributes to warm ischemia-reperfusion injury in rat and pig livers.Communications medicine · 2026Article
- Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.International journal of molecular sciences · 2026Article
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Article
- NRF2 Deficiency Disrupts Mitochondrial Homeostasis via NDUFS7 in Trabecular Meshwork.Research (Washington, D.C.) · 2026Article
- Mitochondrial complex I in focus: mechanisms and therapeutic strategies of urinary system diseases.Frontiers in physiology · 2026Review
322 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Complex I is the first and largest enzyme of the respiratory chain and has a central role in cellular energy production through the coupling of NADH:ubiquinone electron transfer to proton translocation. It is also implicated in many common human neurodegenerative diseases. Here, we report the first crystal structure of the entire, intact complex I (from Thermus thermophilus) at 3.3 Å resolution. The structure of the 536-kDa complex comprises 16 different subunits, with a total of 64 transmembrane helices and 9 iron-sulphur clusters. The core fold of subunit Nqo8 (ND1 in humans) is, unexpectedly, similar to a half-channel of the antiporter-like subunits. Small subunits nearby form a linked second half-channel, which completes the fourth proton-translocation pathway (present in addition to the channels in three antiporter-like subunits). The quinone-binding site is unusually long, narrow and enclosed. The quinone headgroup binds at the deep end of this chamber, near iron-sulphur cluster N2. Notably, the chamber is linked to the fourth channel by a 'funnel' of charged residues. The link continues over the entire membrane domain as a flexible central axis of charged and polar residues, and probably has a leading role in the propagation of conformational changes, aided by coupling elements. The structure suggests that a unique, out-of-the-membrane quinone-reaction chamber enables the redox energy to drive concerted long-range conformational changes in the four antiporter-like domains, resulting in translocation of four protons per cycle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.