Cited by 312Iron Metabolism and DisordersMetal-Catalyzed Oxygenation MechanismsHemoglobin structure and function

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Identification of the ferroxidase centre in ferritin

Lawson, David M., Treffry, Amyra, Artymiuk, Peter J., Harrison, Pauline M., Yewdall, Stephen J., Luzzago, Alessandra, Cesareni, Gianne, Levi, Sonia, Arosio, Paolo·1989·FEBS Letters

DOI 10.1016/0014-5793(89)81040-3

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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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The Ferroxidase Centre of Escherichia coli Bacterioferritin Plays a Key Role in the Reductive Mobilisation of the Mineral Iron Core
Bradley, J. M., Bugg, Z., Sackey, A., Andrews, S. C., Wilson, M. T., Svistunenko, D. A., Moore, G. R., & Brun, N. E. L. (2024) · Angewandte Chemie · doi:10.1002/ange.202401379 · Cited by 2
Tumor potential biomarker: ferritin heavy chain promotes proliferation and migration of oral squamous cell carcinoma
Huang, W., Hu, M., Zhang, Y., Han, Y., & Hou, J. (2025) · Oral Surgery Oral Medicine Oral Pathology and Oral Radiology · doi:10.1016/j.oooo.2025.09.012 · Cited by 2
Functional Characterization of Salmonella Typhimurium Encoded YciF, a Domain of Unknown Function (DUF892) Family Protein, and Its Role in Protection during Bile and Oxidative Stress
Singh, M., Penmatsa, A., & Nandi, D. (2023) · Journal of Bacteriology · doi:10.1128/jb.00059-23 · Cited by 2
“following the ferroxidase activity (41, 42).”
Temporal and spatial resolution of magnetosome degradation at the subcellular level in a 3D lung carcinoma model
Gubieda, A. G., Gandarias, L., Pósfai, M., Pattammattel, A., Fdez-Gubieda, M. L., Abad, A., & Garcı́a-Prieto, A. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02788-8 · Cited by 2
“FTH1 encodes the heavy chain of ferritin, this subunit has ferroxidase activity [37] and can oxidize Fe 2 + to Fe 3 + to protect the cell from oxidative stress and inhibit ferroptosis [38].”
Background
In silico molecular interaction analysis of phytochemicals extracted from Ornithogalum narbonense flowers
Aytar, E. C., Torunoğlu, E. İ., Aydın, B., & Durmaz, A. (2024) · In Silico Pharmacology · doi:10.1007/s40203-024-00272-7 · Cited by 2
“A mutant of H-ferritin generated by mutating two residues in the ferroxidase centre (Glu62 and His65) was able to form stable ferritin complexes but lacked detectable ferroxidase activity (Lawson et al. 1989 ).”
HFE-Related Hemochromatosis May Be a Primary Kupffer Cell Disease
Kouroumalis, E., Tsomidis, I., & Voumvouraki, A. (2025) · Biomedicines · doi:10.3390/biomedicines13030683 · Cited by 2
“Ferritin may contain up to 4500 iron atoms in a complex structure comprised of 24 chains, both heavy (H) with ferroxidase activity, and light (L) chains [32,33].”
Iron Metabolism and Ferroptosis
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An Insight into the Importance of Ferritins in the Physiology of Mycobacterium tuberculosis: Unique Structural and Functional Properties
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Sulfolobus as a model organism for the study of diverse biological interests : forays into thermal virology and oxidative stress
Wiedenheft, B. (2006) · Montana State University ScholarWorks (Montana State University) · Cited by 2
Computational insight into the binding of bryostatin 1 with ferritin: implication of natural compounds in Alzheimer’s disease therapeutics
Shahwan, M. J., Alhumaydhi, F. A., Sharaf, S. E., Alghamdi, B. S. A., Baeesa, S. S., Tayeb, H. O., Ashraf, G. M., & Shamsi, A. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2092552 · Cited by 1
“The FtH-subunit holds a ferroxidase centre, which catalyzes the oxidation as well as detoxification of ferrous ion (Fe2þ) to its fewer reactive appearance ferric ion (Fe3þ) whereas the FtL-subunit holds glutamate residues, which assist Fe3þ mineralization to long-standing storage (Chasteen & Harrison, 1999; Lawson et…”
Background
Multiple Proton Translocation Paths Reveal a Novel Function of Ferritin as a Source of Protons for Cellular Metabolism
Vaigundan, D., Nandha, S. R., Palaniappan, C., & Checker, R. (2024) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416524500467 · Cited by 1
Cloning and characterization of two ferritin subunit genes from bay scallop, Argopecten irradians (Lamarck 1819)
HeYang, X., Wu, Z., & Yu, S. X. (2011) · Cited by 1
Secretion of Ferritin Protein of Periserrula leucophyryna in Bacillus subtilis and Its Feed Efficiency
Choi, J. W. (2016) · KSBB Journal · doi:10.7841/ksbbj.2016.31.2.105 · Cited by 1
Ferritin ☆
Winzerling, J. J., & Pham, D. Q. ‐. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.04049-8 · Cited by 1
Molecular insights into two ferritin subunits from red-lip mullet (Liza haematocheila): Detectable antibacterial activity with its expressional response against immune stimulants
Jung, S., Kim, M., Lim, C., Elvitigala, D. A. S., & Lee, J. (2022) · Gene · doi:10.1016/j.gene.2022.146923 · Cited by 1
Bio‐controlled Growth of Oxides and Metallic Nanoparticles
Coradin, T., Brayner, R., Fiévet, F., & Livage, J. (2007) · doi:10.1002/9783527621446.ch5 · Cited by 1
Ferritin stimulation of a monokine inhibitor of lipopolysaccharide-augmented myelopoiesis is ferroxidase dependent
Kreisberg, R., Broxmeyer, H. E., & Moore, R. N. (1994) · Infection and Immunity · doi:10.1128/iai.62.7.2991-2994.1994 · Cited by 1
Influence of site-directed mutagenesis on protein assembly and solubility of tadpole H-chain ferritin
Kim, K. (1998) · Biotechnology and Bioprocess Engineering · doi:10.1007/bf02932504 · Cited by 1
Studies of the Protein Interaction Network Required for Enterobactin Biosynthesis in Escherichia coli
Khalil, S. (2011) · Spectrum Research Repository (Concordia University) · Cited by 1
Iron Storage Proteins
Crichton, R. R. (2016) · doi:10.1002/9781118925645.ch9 · Cited by 1
Functional characterization of Salmonella Typhimurium encoded YciF, a domain of unknown function (DUF892) family protein, and its role in protection during bile and oxidative stressPreprint
Singh, M., Penmatsa, A., & Nandi, D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.20.524870 · Cited by 1
A comparative study of the antiproliferative activity of iron chelators PIH, SIH and their light-activated caged derivatives in skin cells
Aroun, A. (2010) · The University of Bath Online Publications Store (The University of Bath) · Cited by 1
INTERAC TION OF FERRITIN WITH TRAN SITION METAL IONS AND CHELATES
Zhang, L. (2011) · ScholarlyCommons (University of Pennsylvania)
Effects of pharmaceutical modulation of protein aggregation on lifespan in Caenorhabditis elegans
Klang, I. M. (2015) · Figshare
Ferritin from the spleen of the Antarctic teleostTrematomus bernacchii
Cavallo, S., Mignogna, G., Giangiacomo, L., Stefanini, S., & Chiancone, E. (2000) · The European Zoological Journal · doi:10.1080/11250000009356356
Molecular cloning and expression analysis of a ferritin H subunit from rock bream, Oplegnathus fasciatus
Kwon, M., Jeong, J.-M., Kim, J., & Park, C. (2013) · Journal of fish pathology · doi:10.7847/jfp.2013.26.3.295
The role of iron in rheumatoid arthritis
Al-Qenaei, A. (2008) · The University of Bath Online Publications Store (The University of Bath)
Paracrystalline Inclusions ofa NovelFerritin Containing Nonheme Iron, Produced bytheHumanGastric Pathogen Helicobacter pylon: Evidence fora ThirdClass ofFerritins
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Design and production of protein nanostructures for biomolecular detection
Jääskeläinen, A. (2009) · UTUPub (University of Turku)
Cloning and characterization of a novel ferritin from the marine diatom Pseudo-nitzschia multiseries
Moccia, L. P. (2008) · cIRcle (University of British Columbia) · doi:10.14288/1.0052359
“Ferritins are part of a broad group of di-iron carboxylate proteins that bind and oxidize Fe(II) (Levi et al., 1988; Lawson et al., 1989; Nordlund and Eklund, 1995; Treffry et al., 1997), and store many atoms of Fe(III) within a ferrihydrite mineral core with the rough stoichiometry 9Fe2O3•5H2O…”
Background
Ferritin and Serine Hydroxymethyltransferase
Stover, P. J. (2006) · CRC Press eBooks · doi:10.1201/9780849332296.ch11
Functional Studies of Ferritin 3-Fold Axis: Effects of Mutations Near Subunit Interaction Sites
Pancorbo, B. (2000) · NCSU Libraries Repository (North Carolina State University Libraries)
The effects of quercetin on iron metabolism
Hoque, R. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University)

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.
ORCID: Levi, Sonia
Arosio, Paolo
Venue: FEBS Letters
Publisher: Wiley
Published: 1989-08-28
Volume: 254
Issue: 1-2
Pages: 207-210
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/0014-5793(89)81040-3
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4435 d)
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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Identification of the ferroxidase centre in ferritin

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