ArticleActa crystallographica. Section D, Biological crystallography2015
Time-lapse anomalous X-ray diffraction shows how Fe(2+) substrate ions move through ferritin protein nanocages to oxidoreductase sites.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- Ferritin Iron Mineralisation: Route of FeAngewandte Chemie (International ed. in English) · 2026Article
- Impact of the three-fold channel substitution D131N on kinetics of translocation of FeDalton transactions (Cambridge, England : 2003) · 2026Article
- Cavity acidification limits ferritin iron biomineralization.Journal of inorganic biochemistry · 2026Article
- Structural Insight Into a Human H Ferritin@Gold-Monocarbene Adduct: Aurophilicity Revealed in a Biological Context.Angewandte Chemie (International ed. in English) · 2025Article
- Observation of the Assembly of the Nascent Mineral Core at the Nucleation Site of Human Mitochondrial Ferritin.Journal of the American Chemical Society · 2025Article
- Flexible iron: disorder in the ironome brings order to protein structure and function.Frontiers in molecular biosciences · 2025Article
- Encapsulated Ferritin-like Proteins: A Structural Perspective.Biomolecules · 2024Review
- Optical Monitoring ofNano letters · 2023Article
- Second Coordination Sphere Effects on the Mechanistic Pathways for Dioxygen Activation by a Ferritin: Involvement of a Tyr Radical and the Identification of a Cation Binding Site.Chembiochem : a European journal of chemical biology · 2022Article
- Ferritin: A Promising Nanoreactor and Nanocarrier for Bionanotechnology.ACS bio & med chem Au · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood ClamFrontiers in molecular biosciences · 2022Article
- Key carboxylate residues for iron transit through the prokaryotic ferritinMicrobiology (Reading, England) · 2021Article
- Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.FEBS open bio · 2021Article
- Reaction of OProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration.Frontiers in neuroscience · 2019Review
- Cancer cell death induced by ferritins and the peculiar role of their labile iron pool.Oncotarget · 2018Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Observation of gold sub-nanocluster nucleation within a crystalline protein cage.Nature communications · 2017Article
- Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (μProceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Ferritin superfamily protein cages reversibly synthesize internal biominerals, Fe2O3·H2O. Fe(2+) and O2 (or H2O2) substrates bind at oxidoreductase sites in the cage, initiating biomineral synthesis to concentrate iron and prevent potentially toxic reactions products from Fe(2+)and O2 or H2O2 chemistry. By freezing ferritin crystals of Rana catesbeiana ferritin M (RcMf) at different time intervals after exposure to a ferrous salt, a series of high-resolution anomalous X-ray diffraction data sets were obtained that led to crystal structures that allowed the direct observation of ferrous ions entering, moving along and binding at enzyme sites in the protein cages. The ensemble of crystal structures from both aerobic and anaerobic conditions provides snapshots of the iron substrate bound at different cage locations that vary with time. The observed differential occupation of the two iron sites in the enzyme oxidoreductase centre (with Glu23 and Glu58, and with Glu58, His61 and Glu103 as ligands, respectively) and other iron-binding sites (with Glu53, His54, Glu57, Glu136 and Asp140 as ligands) reflects the approach of the Fe(2+) substrate and its progression before the enzymatic cycle 2Fe(2+) + O2 → Fe(3+)-O-O-Fe(3+) → Fe(3+)-O(H)-Fe(3+) and turnover. The crystal structures also revealed different Fe(2+) coordination compounds bound to the ion channels located at the threefold and fourfold symmetry axes of the cage.
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