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Transfer of Heme from Ferrihemoglobin and Ferrihemoglobin Isolated Chains to Hemopexin
Abstract
Incubation of ferrihemoglobin as well as of hemoglobin isolated chains in ferri‐form with hemopexin at pH 7.0 leads to the gradual transfer of heme to the hemopexin molecules until the equilibrium is attained. The reaction of ferrihemoglobin with hemopexin can be described as a four‐stage process involving successive transfer of the four heme groups from hemoglobin tetramer to the four molecules of hemopexin. The heme binding sites of the hemoglobin molecule are nonequivalent and cooperative. The transfer of heme from the isolated hemoglobin chains in ferri‐form occurs as the simple competitive reaction which can be characterized by a single equilibrium constant. The affinity constant value for the binding of heme to the single binding center of hemopexin molecule was estimated as 1.9 × 10 14× M−1. The direct transfer of heme from hemoglobin to hemopexin may occur in vivo as a part of hemoglobin degradation process.
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“Free heme released into the plasma by the dissolution of hemoproteins from lysed erythrocytes is quickly scavenged by albumin, hemopexin, and the serum lipocalin 𝛂 1 -microglobulin (13, 23, 44, 75).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [44]
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Research works printed but not linked: 24
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Cited by
Sorted by citations
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473
Accelerated autoxidation and heme loss due to instability of sickle hemoglobin.
Hebbel, R. P., Morgan, W. T., Eaton, J. W., & Hedlund, B. E. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.1.237 · Cited by 306
Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
Anzaldi, L. L., & Skaar, E. P. (2010) · Infection and Immunity · doi:10.1128/iai.00613-10 · Cited by 295
Hemopexin and haptoglobin: allies against heme toxicity from hemoglobin not contenders
Smith, A., & McCulloh, R. J. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00187 · Cited by 258
IL-22 controls iron-dependent nutritional immunity against systemic bacterial infections
Sakamoto, K., Kim, Y.-G., Hara, H., Kamada, N., Caballero-Flores, G., Tolosano, E., Soares, M. P., Puente, J. L., Inohara, N., & Núñez, G. (2017) · Science Immunology · doi:10.1126/sciimmunol.aai8371 · Cited by 127
Metadata
- Authors
- Hrkal, Z., Vodrážka, Z., & Kalousek, I.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1974-03
- Volume
- 43
- Issue
- 1
- Pages
- 73-78
- ISSN
- 0014-2956
- 1432-1033
- Cited by
- 198
- References
- 0
- Language
- en
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- Hrkal, Z., Vodrážka, Z., & Kalousek, I. (1974). Transfer of Heme from Ferrihemoglobin and Ferrihemoglobin Isolated Chains to Hemopexin. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1974.tb03386.x
