ArticleBiochemistry2015
Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 74 citations in OpenAlex.
- Neuropathology of Friedreich ataxia and its links to metabolic pathways.Neurodegenerative disease management · 2026Review
- Chemical modulation of Miro1 alleviates cell-type-specific vulnerabilities in Friedreich's ataxia.Cell chemical biology · 2026Article
- Nanobodies as tools for studying human frataxin biology.Communications biology · 2026Article
- Article
- Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe-S Cluster Biosynthesis.Biochemistry · 2025Article
- Two-stage binding of mitochondrial ferredoxin-2 to the core iron-sulfur cluster assembly complex.Nature communications · 2024Article
- Searching for Frataxin Function: Exploring the Analogy with Nqo15, the Frataxin-like Protein of Respiratory Complex I fromInternational journal of molecular sciences · 2024Article
- Targeting ferroptosis and ferritinophagy: new targets for cardiovascular diseases.Journal of Zhejiang University. Science. B · 2024Review
- Human frataxin, the Friedreich ataxia deficient protein, interacts with mitochondrial respiratory chain.Cell death & disease · 2023Article
- Article
- During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.The Journal of biological chemistry · 2022Article
- Cerebrospinal Fluid Proteomics in Friedreich Ataxia Reveals Markers of Neurodegeneration and Neuroinflammation.Frontiers in neuroscience · 2022Article
- N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization.Nature communications · 2021Article
- Review
- Frataxins Emerge as New Players of the Intracellular Antioxidant Machinery.Antioxidants (Basel, Switzerland) · 2021Article
- Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021Review
- Extra-mitochondrial mouse frataxin and its implications for mouse models of Friedreich's ataxia.Scientific reports · 2020Article
- Hereditary Ataxia: A Focus on Heme Metabolism and Fe-S Cluster Biogenesis.International journal of molecular sciences · 2020Review
- Evaluation of antibodies for western blot analysis of frataxin protein isoforms.Journal of immunological methods · 2019Article
- Mechanism of activation of the human cysteine desulfurase complex by frataxin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Iron-sulfur (Fe-S) clusters function as protein cofactors for a wide variety of critical cellular reactions. In human mitochondria, a core Fe-S assembly complex [called SDUF and composed of NFS1, ISD11, ISCU2, and frataxin (FXN) proteins] synthesizes Fe-S clusters from iron, cysteine sulfur, and reducing equivalents and then transfers these intact clusters to target proteins. In vitro assays have relied on reducing the complexity of this complicated Fe-S assembly process by using surrogate electron donor molecules and monitoring simplified reactions. Recent studies have concluded that FXN promotes the synthesis of [4Fe-4S] clusters on the mammalian Fe-S assembly complex. Here the kinetics of Fe-S synthesis reactions were determined using different electron donation systems and by monitoring the products with circular dichroism and absorbance spectroscopies. We discovered that common surrogate electron donor molecules intercepted Fe-S cluster intermediates and formed high-molecular weight species (HMWS). The HMWS are associated with iron, sulfide, and thiol-containing proteins and have properties of a heterogeneous solubilized mineral with spectroscopic properties remarkably reminiscent of those of [4Fe-4S] clusters. In contrast, reactions using physiological reagents revealed that FXN accelerates the formation of [2Fe-2S] clusters rather than [4Fe-4S] clusters as previously reported. In the preceding paper [Fox, N. G., et al. (2015) Biochemistry 54, DOI: 10.1021/bi5014485], [2Fe-2S] intermediates on the SDUF complex were shown to readily transfer to uncomplexed ISCU2 or apo acceptor proteins, depending on the reaction conditions. Our results indicate that FXN accelerates a rate-limiting sulfur transfer step in the synthesis of [2Fe-2S] clusters on the human Fe-S assembly complex.
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