ArticleThe Journal of biological chemistry2016
The Structure of the Complex between Yeast Frataxin and Ferrochelatase: CHARACTERIZATION AND PRE-STEADY STATE REACTION OF FERROUS IRON DELIVERY AND HEME SYNTHESIS.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Protoporphyrin IX Binds to Iron(II)-Loaded and to Zinc-Loaded Human Frataxin.Life (Basel, Switzerland) · 2023Article
- Recent Advances in the Elucidation of Frataxin Biochemical Function Open Novel Perspectives for the Treatment of Friedreich's Ataxia.Frontiers in neuroscience · 2022Review
- Cockayne syndrome group A and ferrochelatase finely tune ribosomal gene transcription and its response to UV irradiation.Nucleic acids research · 2021Article
- Frataxins Emerge as New Players of the Intracellular Antioxidant Machinery.Antioxidants (Basel, Switzerland) · 2021Article
- Review
- Mechanism of the Affinity-Enhancing Effect of Isatin on Human Ferrochelatase and Adrenodoxin Reductase Complex Formation: Implication for Protein Interactome Regulation.International journal of molecular sciences · 2020Article
- Making and breaking heme.Current opinion in structural biology · 2019Review
- Mitoferrin-1 is required for brain energy metabolism and hippocampus-dependent memory.Neuroscience letters · 2019Article
- Iron Hack - A symposium/hackathon focused on porphyrias, Friedreich's ataxia, and other rare iron-related diseases.F1000Research · 2019Article
- Characterization of a new N-terminally acetylated extra-mitochondrial isoform of frataxin in human erythrocytes.Scientific reports · 2018Article
- Iron in Friedreich Ataxia: A Central Role in the Pathophysiology or an Epiphenomenon?Pharmaceuticals (Basel, Switzerland) · 2018Review
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.Archives of biochemistry and biophysics · 2018Article
- Nitric oxide prevents Aft1 activation and metabolic remodeling in frataxin-deficient yeast.Redox biology · 2018Article
- Unraveling the Role of Heme in Neurodegeneration.Frontiers in neuroscience · 2018Review
- Early cerebellar deficits in mitochondrial biogenesis and respiratory chain complexes in the KIKO mouse model of Friedreich ataxia.Disease models & mechanisms · 2017Article
- Iron-induced oligomerization of human FXN81-210 and bacterial CyaY frataxin and the effect of iron chelators.PloS one · 2017Article
- Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Frataxin is a mitochondrial iron-binding protein involved in iron storage, detoxification, and delivery for iron sulfur-cluster assembly and heme biosynthesis. The ability of frataxin from different organisms to populate multiple oligomeric states in the presence of metal ions, e.g. Fe(2+) and Co(2+), led to the suggestion that different oligomers contribute to the functions of frataxin. Here we report on the complex between yeast frataxin and ferrochelatase, the terminal enzyme of heme biosynthesis. Protein-protein docking and cross-linking in combination with mass spectroscopic analysis and single-particle reconstruction from negatively stained electron microscopic images were used to verify the Yfh1-ferrochelatase interactions. The model of the complex indicates that at the 2:1 Fe(2+)-to-protein ratio, when Yfh1 populates a trimeric state, there are two interaction interfaces between frataxin and the ferrochelatase dimer. Each interaction site involves one ferrochelatase monomer and one frataxin trimer, with conserved polar and charged amino acids of the two proteins positioned at hydrogen-bonding distances from each other. One of the subunits of the Yfh1 trimer interacts extensively with one subunit of the ferrochelatase dimer, contributing to the stability of the complex, whereas another trimer subunit is positioned for Fe(2+) delivery. Single-turnover stopped-flow kinetics experiments demonstrate that increased rates of heme production result from monomers, dimers, and trimers, indicating that these forms are most efficient in delivering Fe(2+) to ferrochelatase and sustaining porphyrin metalation. Furthermore, they support the proposal that frataxin-mediated delivery of this potentially toxic substrate overcomes formation of reactive oxygen species.
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