ArticleNature communications2019
A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Synergistic bactericidal mechanism of carvacrol and ε-polylysine againstRSC advances · 2026Article
- Mitochondrial complex I deficiency-associated diseases and models.Cellular and molecular life sciences : CMLS · 2026Review
- Comparative Variation and Associations Among Seminal Microbiota, Oxidative Status, and Semen Quality in Different Rooster Types.Animals : an open access journal from MDPI · 2026Article
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Impact of low-intensity 463 nm blue light on proliferation and adaptive mutation of Escherichia coli DH5α cells.Scientific reports · 2025Article
- Limited Diversity of Thermal Adaptation to a Critical Temperature inInternational journal of molecular sciences · 2025Article
- Proton-Translocating NADH-Ubiquinone Oxidoreductase: Interaction with Artificial Electron Acceptors, Inhibitors, and Potential Medicines.International journal of molecular sciences · 2024Review
- Changing the Electron Acceptor Specificity ofInternational journal of molecular sciences · 2023Article
- Production of Reduced Graphene Oxide by Using Three Different Microorganisms and Investigation of Their Cell Interactions.ACS omega · 2023Article
- Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]-Hydrogenase Complex HydABC.Journal of the American Chemical Society · 2023Article
- Seminal Bacterioflora of Two Rooster Lines: Characterization, Antibiotic Resistance Patterns and Possible Impact on Semen Quality.Antibiotics (Basel, Switzerland) · 2023Article
- The role of sphingosine-1-phosphate in the development and progression of Parkinson's disease.Frontiers in cellular neuroscience · 2023Review
- Article
- Genome-Scale Mining of Acetogens of the GenusMicrobiology spectrum · 2022Article
- Structure of respiratory complex I - An emerging blueprint for the mechanism.Current opinion in structural biology · 2022Review
- Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries.Microbiology spectrum · 2022Article
- Characterization of a novel + 70 Da modification in rhGM-CSF expressed in E. coli using chemical assays in combination with mass spectrometry.Amino acids · 2022Article
- Resolving Chemical Dynamics in Biological Energy Conversion: Long-Range Proton-Coupled Electron Transfer in Respiratory Complex I.Accounts of chemical research · 2021Article
- Structural Basis for Inhibition of ROS-Producing Respiratory Complex I by NADH-OH.Angewandte Chemie (International ed. in English) · 2021Article
- Mitochondrial iron-sulfur clusters: Structure, function, and an emerging role in vascular biology.Redox biology · 2021Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by the reduction state of the nearby [Fe-S] cluster N1a. Fixation of the peptide bond by site-directed mutagenesis led to an inactivation of electron transfer and a decreased reactive oxygen species (ROS) production. We suggest the redox-gated peptide flip to represent a previously unrecognized molecular switch synchronizing NADH oxidation in response to the redox state of the complex as part of an intramolecular feed-back mechanism to prevent ROS production.
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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.