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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Treffry A., 1989, FEBS Lett.
Levi S., 1989, Biochemistry
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Background
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Background
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“Heavy-chain ferritin (H-ferritin) participates by converting the more toxic Fe to Fe, while light-chain ferritin (L-ferritin) is primarily involved in long-term iron storage (31,54).”
Background
A teleostean counterpart of ferritin M subunit from rock bream (Oplegnathus fasciatus): An active constituent in iron chelation and DNA protection against oxidative damage, with a modulated expression upon pathogen stress
Elvitigala, D. A. S., Premachandra, H. K. A., Whang, I., Oh, M., Jung, S., Park, C., & Lee, J. (2013) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2013.08.012 · Cited by 24
Effect of the charge distribution along the “ferritin-like” pores of the proteins from the Dps family on the iron incorporation process
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Thermal Stability of Human Ferritin: Concentration Dependence and Enhanced Stability of an N-Terminal Fusion Mutant
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Characterization of the H- and L-Subunit Ratios of Ferritins by Sodium Dodecyl Sulfate–Capillary Gel Electrophoresis
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Self-citation
Differential response of two ferritin subunit genes (VpFer1 and VpFer2) from Venerupis philippinarum following pathogen and heavy metals challenge
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“In addition, VpFer2 demonstrated highly similarities of the ferritin H subunit signatures [1,37] (Fig.”
Background
Silver nanoparticle synthesis in human ferritin by photochemical reduction
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Trace Metal Utilization in Chloroplasts
Merchant, S. (2007) · Advances in photosynthesis and respiration · doi:10.1007/978-1-4020-4061-0_10 · Cited by 21
“ions by the ferroxidase activity of the ferritin subunits (Lawson et al., 1989).”
Background
Iron Loading into Ferritin by an Intracellular Ferroxidase
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Identification and characterization of a ferritin gene involved in the immune defense response of scallop Chlamys farreri
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Human ferritin H‐chains can be obtained in non‐assembled stable forms which have ferroxidase activity
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Self-citation
Ferroxidase activity of ferritin: Effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation
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Pathogenic mechanism and modeling of neuroferritinopathy
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Intrinsically Magnetic Cells: A Review on Their Natural Occurrence and Synthetic Generation
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Active human ferritin H/L-hybrid and sequence effect on folding efficiency in Escherichia coli
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Human mitochondrial ferritin exhibits highly unusual iron-O2 chemistry distinct from that of cytosolic ferritins
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The iron content and ferritin contribution in fresh, dried, and toasted nori, Pyropia yezoensis
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A Molecular Dynamics and Computational Study of Ligand Docking and Electron Transfer in Ferritins
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Ferritin Gene Coding Sequences Are Conserved Among Eight Hard Tick Species (Ixodida: Ixodidae)
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Paragonimus westermani: molecular cloning, expression, and characterization of a recombinant yolk ferritin
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Cloning and characterization of two ferritin subunit genes from bay scallop, Argopecten irradians (Lamarck 1819)
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“complex [5, 6], while the L subunit facilitates the assembly”
Background
Long-distance signaling of iron deficiency in plants
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The location of exon boundaries in the multimeric iron-storage protein ferritin
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“The site of Fe(II) oxidation is at a metal centre recently discovered in the crystal structure of recombinant human H-chain ferritin and shown to account for ferroxidase activity by following the effects of specific sequence changes (Lawson 1990; Lawson et al. 1989 ).”
BackgroundSelf-citation
Iron loading into ferritin can be stimulated or inhibited by the presence of cations and anions: A specific role for phosphate
Cutler, C., Bravo, A., Ray, A. D., & Watt, R. K. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.08.004 · Cited by 16
Hyperthermostable recombinant human heteropolymer ferritin derived from a novel plasmid design
Srivastava, A. K., Scalcione, L. J., Arosio, P., & Bou‐Abdallah, F. (2022) · Protein Science · doi:10.1002/pro.4543 · Cited by 16
Self-citation

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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