Exchange of Heme among Hemoglobins and between Hemoglobin and Albumin
Open accessAbstract
Intact heme groups undergo exchange between molecules of human hemoglobin under physiological conditions. This phenomenon requires the presence of ferrihemoglobin and is blocked by heme ligands or the prior binding of hemoglobin to haptoglobin. The kinetics of heme exchange between hemoglobins A and F allows a calculation of the rate constants for the dissociation of heme and globin. The rate of exchange of hemes between the non-α chains of ferrihemoglobins A and F is approximately 8 times that between the α chains. Mixtures of ferrihemoglobins and oxyhemoglobins exchange hemes at a rate greater than predicted from the rates of exchange observed in mixtures containing only oxyhemoglobin or ferrihemoglobin. Ferriheme groups also undergo exchange between hemoglobin not bound to haptoglobin and methemalbumin, although at equilibrium the affinity of human albumin for ferriheme is only about one-fifteenth that of globin. Only primate albumins possess appreciable affinity for ferriheme; albumins from the nonprimate species examined appeared to be incapable of forming methemalbumin. Depletion of hemes from ferrihemoglobin by excess human albumin leads to the accumulation of free, precipitable globin.
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Free iron (Fe3+) may dissociate from methemoglobin.
“Another source of oxidants is free iron (Fe3+), which may dissociate from metHb (26).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [26]
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- Authors
- Bunn, H. F., & Jandl, J. H.
- Affiliations
- Harvard University (US)
- ORCID
- Bunn, H F
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1968-02
- Volume
- 243
- Issue
- 3
- Pages
- 465-475
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1509804778
- Cited by
- 415
- References
- 37
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 8 · 2023: 4 · 2022: 6 · 2021: 5 · 2020: 19 · 2019: 12 · 2018: 11 · 2017: 8 · 2016: 17 · 2015: 12 · 2014: 9 · 2013: 12 · 2012: 9
- FWCI
- 12.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- hemoglobin, hemoglobin A, fetal hemoglobin, methemoglobin, methemalbumin, human serum albumin, haptoglobin, globin, oxyhemoglobin
- MeSH terms
- Animals, Haplorhini, Blood Proteins, Carbon Isotopes, Cattle, Chromatography, Ion Exchange, Dialysis, Dogs, Electron Transport, Electrophoresis, Guinea Pigs, Haptoglobins, Heme, Hemoglobins, Hemoglobins, Abnormal, Hydrogen-Ion Concentration, Iron Isotopes, Kinetics, Mathematics, Methylcellulose, Protein Binding, Rabbits, Serum Albumin, Temperature, Rats
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