The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
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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“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]
Citations
Cites
FERRITIN: STRUCTURE, GENE REGULATION, AND CELLULAR FUNCTION IN ANIMALS, PLANTS, AND MICROORGANISMS
Theil, E. C. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.001445 · Cited by 1,337
Ferritin: design and formation of an iron-storage molecule
Ford, G. C., Harrison, P. M., Rice, D. W., Smith, J. M., Treffry, A., WHITE, J. L., & Yariv, J. (1984) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1984.0046 · Cited by 567
Self-citationOn ferritin heterogeneity. Further evidence for heteropolymers.
Arosio, P., Adelman, T. G., & Drysdale, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34741-5 · Cited by 457
Self-citationLevi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A., & Arosio, P. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81326-1 · Cited by 378
Self-citationThe formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake
Macara, I. G., Hoy, T. G., & Harrison, P. M. (1972) · Biochemical Journal · doi:10.1042/bj1260151 · Cited by 242
Self-citationBryce, C. F. A., & Crichton, R. R. (1973) · Biochemical Journal · doi:10.1042/bj1330301 · Cited by 112
Iron binding by horse spleen apoferritin. A vanadyl(IV) EPR spin probe study.
Chasteen, N. D., & Theil, E. C. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34433-8 · Cited by 111
Iron incorporation into apoferritin. The role of apoferritin as a ferroxidase.
Bakker, G., & Boyer, R. F. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69288-9 · Cited by 104
The formation of ferritin from apoferritin. Catalytic action of apoferritin
Macara, I. G., Hoy, T. G., & Harrison, P. M. (1973) · Biochemical Journal · doi:10.1042/bj1350343 · Cited by 73
Self-citationSpectroscopic studies on the binding of Iron, Terbium, and Zinc by Apoferritin
Treffry, A., & Harrison, P. M. (1984) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(84)85035-7 · Cited by 69
Self-citation
Research works printed but not linked: 6
- Treffry A., 1989, FEBS Lett.
- Levi S., 1989, Biochemistry
- Wagstaff M., 1978, Biochem. J., 199, 567
- Levi S., 1989, Biochem. J.
- Lawson D.M., 1989, Inorganic Biochemistry Discussion Group, Christmas meeting
- Bauminger E.R., 1989, Biochemistry
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Items 301–312 of 312
Winzerling, J. J., & Pham, D. Q. ‐. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00058-2
Carhart, J. M. (2017) · doi:10.18297/etd/2827
“Ferritin heavy chain conducts ferroxidase activity that is necessary for iron deposition into the nanocage by converting ferrous iron to ferric iron (85).”
Backgroundrole of brain iron loading in redox-epigenetic regulation of psychiatrics-like behavior
Ye, X. (2018) · Digital Repository Service (Northeastern University) · doi:10.17760/d20285816
Ferritin and Serine Hydroxymethyltransferase
Stover, P. J. (2006) · CRC Press eBooks · doi:10.1201/9781420004847.ch11
Perry, G. L. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.5008958.4940056
Eden, M. E. V., & Aust, S. D. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm0308
Iron Metabolism and Ferroptosis
Zheng, H., & Toyokuni, S. (2023) · Springer eBooks · doi:10.1007/978-3-031-39171-2_2
Oxidative Modification of Ferritin Induced by Salsolinol, Catechol Neurotoxin
Kang, J. H. (2008) · Bulletin of the Korean Chemical Society · doi:10.5012/bkcs.2008.29.12.2390
Kar, R., Saha, S., Sikder, K., Manna, D., Chakraborti, S., & Basu, A. (2026) · Folia Microbiologica · doi:10.1007/s12223-026-01434-0
Namikawa, Y., Negishi, L., Kurumizaka, H., & Suzuki, M. (2026) · FEBS Journal · doi:10.1111/febs.70601
Liu, S., Chen, W., Chen, X. H., Cai, Y., Cheng, L., Guo, H., Lin, F., Kang, Y., Wang, F., ZHAO, Y., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107519
Mechanisms of Ferritin Iron Incorporation: A Study with Recombinant and Mutant Human Ferritins
Levi, S., Luzzago, A., Santambrogio, P., Cozzi, A., Cesareni, G., & Arosio, P. (1991) · Springer eBooks · doi:10.1007/978-1-4615-3810-3_24
Self-citation
Metadata
- 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 › Biochemistry › 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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