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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It is widely accepted that iron deposition in the iron storage protein ferritin in vitro involves Fe(II) oxidation, and that ferritin facilitates this oxidation at a ferroxidase site on the protein. However, these views have recently been questioned, with the protein ferroxidase activity instead being attributed to autoxidation from the buffer alone. Ligand exchange between another protein with ferroxidase activity and ferritin has been proposed as an alternative mechanism for iron incorporation into ferritin. In the present work, a pH stat apparatus is used to eliminate the influence of buffers on iron(II) oxidation. Here we show that the recent experiments questioning the ferroxidase activity of ferritin were flawed by inadequate pH control, that buffers actually retard rather than facilitate iron(II) oxidation, and that horse spleen ferritin has ferroxidase activity when measured under proper experimental conditions. Furthermore, high pH (7.0), a high Fe(II) concentration and the presence of Fe(III) all favour Fe(II) autoxidation in the presence or absence of ferritin.
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The iron in the central cavity of ferritin is maintained as ferric Fe3+ due to the ferroxidase activity of FTH1.
“The iron in the central cavity is maintained as small crystalline particles in its ferric Fe3+ form due to the ferroxidase activity of FTH1 (Hentze et al., 1986; Yang and Chasteen, 1999).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Yang and Chasteen, 1999
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The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works
Identification of the ferroxidase centre in ferritin
Lawson, D. M., Treffry, A., Artymiuk, P. J., Harrison, P. M., Yewdall, S. J., Luzzago, A., Cesareni, G., Levi, S., & Arosio, P. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81040-3 · Cited by 312 · see citing works
Analysis of the effects of changes in rate and rhythm upon electrical activity in the heart
Boyet, M. R., & Jewell, B. R. (1981) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(81)90003-1 · Cited by 279 · see citing works
(1995) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(99)80009-3 · Cited by 12 · see citing works
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The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003797200 · Cited by 242 · see citing works
The Ferroxidase Activity of Yeast Frataxin
Park, S., Gakh, O., Mooney, S. M., & Isaya, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206711200 · Cited by 88 · see citing works
Unveiling ferroptosis as a promising therapeutic avenue for colorectal cancer and colitis treatment
Kao, A. T., Cabanlong, C. V., Padilla, K., & Xue, X. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.025 · Cited by 30 · see citing works
- Authors
- YANG, X., & CHASTEEN, N. D.
- Affiliations
- University of New Hampshire (US)
- ORCID
- YANG, Xiaoke
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1999-03-08
- Volume
- 338
- Issue
- 3
- Pages
- 615-618
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1220094
- OpenAlex
- W2043595508
- Cited by
- 52
- References
- 4
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 4 · 2023: 2 · 2022: 1 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 4
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R37 GM20194, R37GM020194)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- ferritin, ferroxidase activity, iron(II) oxidation, iron storage, pH effect, buffering effect, horse spleen ferritin, iron incorporation, ligand exchange
- MeSH terms
- Animals, Buffers, Ceruloplasmin, Ferritins, Horses, Hydrogen-Ion Concentration, Iron, Oxidation-Reduction
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