Identification of the ferroxidase centre in ferritin
Abstract
Ferroxidase activity in human H‐chain ferritin has been studied with the aid of site‐directed mutagenesis. A site discovered by X‐ray crystallography has now been identified as the ferroxidase centre. This centre is present only in H‐chains and is located within the four‐helix bundle of the chain fold.
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Saccharomyces cerevisiae cells lacking the YFH1 gene showed low levels of cytochrome and ferrochelatase.
“It was demonstrated that Saccharomyces cerevisiae cells lacking the YFH1 gene, the yeast homologue of the human frataxin gene, showed low levels of cytochrome and ferrochelatase (181).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [181]
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Self-citationConditional deletion of ferritin H in mice induces loss of iron storage and liver damage #
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“The Fth allele was generated by crossing mice carrying the Fth allele to transgenic mice with β-actinFlpE recombinase.(3) Mice with the Fth allele on mixed genetic background (C57 BL/6 x 129/Sv) were crossed with the Mx-Cre transgenic mice(4) to obtain Fth;Mx-Cre (mutant) and Fth;+ (control) mice.”
BackgroundMethodMechanism of catalysis of Fe(II) oxidation by ferritin H chains
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Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell
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Iron detoxifying activity of ferritin
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“Two of these deletions were localized in regions corresponding to loops in the horse L chain (7) and human H chain (17, 18, 31) (whose crystal structures have been solved); a single-amino-acid deletion localized to helix D; and a 2-amino-acid deletion localized to the region corresponding to helix E.”
BackgroundNeuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation
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Self-citationIdentification of the ferroxidase centre of Escherichia coli bacterioferritin
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Self-citationDalton perspectives. Biomineralization: the hard part of bioinorganic chemistry!
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Self-citationFormation of iron(III)-tyrosinate is the fastest reaction observed in ferritin
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Role of H and L Subunits in Mouse Ferritin
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Self-citationCloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)
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Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
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Interactions and Reactions of Ferritin with DNA
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Macrophage activation syndrome: Serological markers and treatment with anti-thymocyte globulin
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- Authors
- Lawson, D. M., Treffry, A., Artymiuk, P. J., Harrison, P. M., Yewdall, S. J., Luzzago, A., Cesareni, G., Levi, S., & Arosio, P.
- Affiliations
- University of Sheffield (GB)
- European Molecular Biology Laboratory (DE)
- University of Rome Tor Vergata (IT)
- University of Milan (IT)
- Corresponding author
- Artymiuk, Peter J.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1989-08-28
- Volume
- 254
- Issue
- 1-2
- Pages
- 207-210
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1987119816
- Cited by
- 312
- References
- 13
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 8 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 5 · 2019: 5 · 2018: 8 · 2017: 2 · 2016: 9 · 2015: 8 · 2014: 8 · 2013: 11 · 2012: 10
- FWCI
- 8.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion)
- Archivio Istituzionale della Ricerca - Università Vita-Salute San Raffaele (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- ferritin, iron oxidation, site-directed mutagenesis, four-helix bundle, protein structure, iron storage
- MeSH terms
- Animals, Binding Sites, Ferritins, Horses, Humans, Mutation, Oxidoreductases, Protein Conformation, Recombinant Proteins, X-Ray Diffraction, Rats
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