ArticleBiochemistry2014
Electron-transfer pathways in the heme and quinone-binding domain of complex II (succinate dehydrogenase).
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Iron-Sulfur Cluster Targeting: A Novel Perspective for Treating Alcohol-Related Lipid Metabolic Diseases.Journal of biochemical and molecular toxicology · 2026Review
- Computational Modeling Analysis of Kinetics of Fumarate Reductase Activity and ROS Production during Reverse Electron Transfer in Mitochondrial Respiratory Complex II.International journal of molecular sciences · 2023Article
- Mitochondrial iron-sulfur clusters: Structure, function, and an emerging role in vascular biology.Redox biology · 2021Review
- SDHB Suppresses the Tumorigenesis and Development of ccRCC by Inhibiting Glycolysis.Frontiers in oncology · 2021Article
- Rotating Magnetic Fields Inhibit Mitochondrial Respiration, Promote Oxidative Stress and Produce Loss of Mitochondrial Integrity in Cancer Cells.Frontiers in oncology · 2021Article
- Hysteresis and bistability in the succinate-CoQ reductase activity and reactive oxygen species production in the mitochondrial respiratory complex II.Redox biology · 2020Article
- Computational Modeling Analysis of Generation of Reactive Oxygen Species by Mitochondrial Assembled and Disintegrated Complex II.Frontiers in physiology · 2020Article
- Review
- Mammalian iron-sulphur proteins: novel insights into biogenesis and function.Nature reviews. Molecular cell biology · 2015Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Single electron transfers have been examined in complex II (succinate:ubiquinone oxidoreductase) by the method of pulse radiolysis. Electrons are introduced into the enzyme initially at the [3Fe-4S] and ubiquinone sites followed by intramolecular equilibration with the b heme of the enzyme. To define thermodynamic and other controlling parameters for the pathways of electron transfer in complex II, site-directed variants were constructed and analyzed. Variants at SdhB-His207 and SdhB-Ile209 exhibit significantly perturbed electron transfer between the [3Fe-4S] cluster and ubiquinone. Analysis of the data using Marcus theory shows that the electronic coupling constants for wild-type and variant enzyme are all small, indicating that electron transfer occurs by diabatic tunneling. The presence of the ubiquinone is necessary for efficient electron transfer to the heme, which only slowly equilibrates with the [3Fe-4S] cluster in the absence of the quinone.
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Registered trials
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