ArticleAngewandte Chemie (International ed. in English)2021
Structural Basis for Inhibition of ROS-Producing Respiratory Complex I by NADH-OH.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 17 citations in OpenAlex.
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Hydrogen-bond-assisted meta-nitrogen-doped graphyne enables real-time electrocatalytic NADH tracking in single cells.Chemical science · 2026Article
- The Role of NADAmerican journal of cardiovascular drugs : drugs, devices, and other interventions · 2025Review
- Discovery of a novel polymyxin adjuvant against multidrug-resistant gram-negative bacteria through oxidative stress modulation.Acta pharmaceutica Sinica. B · 2025Article
- Proton-Translocating NADH-Ubiquinone Oxidoreductase: Interaction with Artificial Electron Acceptors, Inhibitors, and Potential Medicines.International journal of molecular sciences · 2024Review
- NIR-enhanced Pt single atom/g-CBioactive materials · 2024Article
- Emerging role of carbonyl-carbonyl interactions in the classification of beta turns.Protein science : a publication of the Protein Society · 2024Article
- Flavonoid-Phenolic Acid Hybrids Are Potent Inhibitors of Ferroptosis via Attenuation of Mitochondrial Impairment.Antioxidants (Basel, Switzerland) · 2023Article
- Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidases.Scientific reports · 2023Article
- Structural Basis for Inhibition of ROS-Producing Respiratory Complex I by NADH-OH.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
14 authors at 4 institutions in 4 countries.
Funding
Abstract
nadhubiquinone oxidoreductase, respiratory complex I, plays a central role in cellular energy metabolism. As a major source of reactive oxygen species (ROS) it affects ageing and mitochondrial dysfunction. The novel inhibitor NADH-OH specifically blocks NADH oxidation and ROS production by complex I in nanomolar concentrations. Attempts to elucidate its structure by NMR spectroscopy have failed. Here, by using X-ray crystallographic analysis, we report the structure of NADH-OH bound in the active site of a soluble fragment of complex I at 2.0 Å resolution. We have identified key amino acid residues that are specific and essential for binding NADH-OH. Furthermore, the structure sheds light on the specificity of NADH-OH towards the unique Rossmann-fold of complex I and indicates a regulatory role in mitochondrial ROS generation. In addition, NADH-OH acts as a lead-structure for the synthesis of a novel class of ROS suppressors.
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