Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)
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Abstract The kinetics of the catalysis of Fe(II) oxidation by crystalline human ferroxidase (ceruloplasmin) has been studied under various conditions at 30°. Two Km values with respect to Fe(II), Km1 = 0.6 µm and Km2 = 50 µm, were obtained at pH 6.5, at which ferroxidase gave the maximum activity of 550 Fe(II) per ferroxidase per min in an acetate buffer. Competition between the two substrates, p-phenylenediamine and Fe(II), was observed. The stoichiometry of Fe(II), ferroxidase, and oxygen, determined from the experimental data, was 4:1:1.
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Hepcidin is synthesized by the liver as an 84-amino acid precursor, processed and secreted as a final 25-amino acid peptide.
“Hepcidin is synthesized by the liver as an 84–amino acid precursor, which is processed and then secreted as a final 25–amino acid peptide (232).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [232]
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- Authors
- Osaki, S.
- Affiliations
- Florida State University (US)
- Corresponding author
- Osaki, Shigemasa
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1966-11
- Volume
- 241
- Issue
- 21
- Pages
- 5053-5059
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1520189306
- Cited by
- 160
- References
- 17
- Citations by year
- 2026: 1 · 2025: 4 · 2022: 1 · 2021: 3 · 2019: 5 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 3 · 2013: 4 · 2012: 10
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- ceruloplasmin, ferroxidase, Fe(II) oxidation, enzyme kinetics, crystalline enzyme, Michaelis constant, substrate competition, p-phenylenediamine, oxygen stoichiometry, iron oxidation
- MeSH terms
- Aniline Compounds, Ascorbic Acid, Catalysis, Ceruloplasmin, Crystallization, Humans, Hydrogen-Ion Concentration, Iron, Kinetics, Oxidoreductases, Spectrophotometry
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