ArticleThe Biochemical journal2005
Inhibitory effect of palmitate on the mitochondrial NADH:ubiquinone oxidoreductase (complex I) as related to the active-de-active enzyme transition.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 80 citations in OpenAlex.
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- Understanding Hypertension: A Metabolomic Perspective.Biology · 2025Review
- Proton-Translocating NADH-Ubiquinone Oxidoreductase: Interaction with Artificial Electron Acceptors, Inhibitors, and Potential Medicines.International journal of molecular sciences · 2024Review
- Investigating potential biomarkers of acute pancreatitis in patients with a BMI>30 using Mendelian randomization and transcriptomic analysis.Lipids in health and disease · 2024Article
- Cellular stress in the pathogenesis of nonalcoholic steatohepatitis and liver fibrosis.Nature reviews. Gastroenterology & hepatology · 2023Review
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- Hypolipidemic effect and molecular mechanism of ginsenosides: a review based on oxidative stress.Frontiers in pharmacology · 2023Review
- Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?Current opinion in structural biology · 2022Review
- Energy substrate metabolism and oxidative stress in metabolic cardiomyopathy.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Mitochondria homeostasis: Biology and involvement in hepatic steatosis to NASH.Acta pharmacologica Sinica · 2022Article
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- A Novel Nutraceuticals Mixture Improves Liver Steatosis by Preventing Oxidative Stress and Mitochondrial Dysfunction in a NAFLD Model.Nutrients · 2021Article
- Immunity as Cornerstone of Non-Alcoholic Fatty Liver Disease: The Contribution of Oxidative Stress in the Disease Progression.International journal of molecular sciences · 2021Review
- Water route for proton pumping in mitochondrial complex I.Nature structural & molecular biology · 2020Article
- Brain Ischemia/Reperfusion Injury and Mitochondrial Complex I Damage.Biochemistry. Biokhimiia · 2019Review
- The effect of palmitic acid on inflammatory response in macrophages: an overview of molecular mechanisms.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2019Review
- Mitochondrial respiration and ROS emission during β-oxidation in the heart: An experimental-computational study.PLoS computational biology · 2017Article
- Modulation of the conformational state of mitochondrial complex I as a target for therapeutic intervention.Interface focus · 2017Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Palmitate rapidly and reversibly inhibits the uncoupled NADH oxidase activity catalysed by activated complex I in inside-out bovine heart submitochondrial particles (IC50 extrapolated to zero enzyme concentration is equal to 9 microM at 25 degrees C, pH 8.0). The NADH:hexa-ammineruthenium reductase activity of complex I is insensitive to palmitate. Partial (approximately 50%) inhibition of the NADH:external quinone reductase activity is seen at saturating palmitate concentration and the residual activity is fully sensitive to piericidin. The uncoupled succinate oxidase activity is considerably less sensitive to palmitate. Only a slight stimulation of tightly coupled respiration with NADH as the substrate is seen at optimal palmitate concentrations, whereas complete relief of the respiratory control is observed with succinate as the substrate. Palmitate prevents the turnover-induced activation of the de-activated complex I (IC50 extrapolated to zero enzyme concentration is equal to 3 microM at 25 degrees C, pH 8.0). The mode of action of palmitate on the NADH oxidase is qualitatively temperature-dependent. Rapid and reversible inhibition of the complex I catalytic activity and its de-active to active state transition are seen at 25 degrees C, whereas the time-dependent irreversible inactivation of the NADH oxidase proceeds at 37 degrees C. Palmitate drastically increases the rate of spontaneous de-activation of complex I in the absence of NADH. Taken together, these results suggest that free fatty acids act as specific complex I-directed inhibitors; at a physiologically relevant temperature (37 degrees C), their inhibitory effects on mitochondrial NADH oxidation is due to perturbation of the pseudo-reversible active-de-active complex I transition.
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