Abstract
Degradation of the haem of haemoglobin (used as a chemical probe of the haem–protein relationship), suggests that reconstituted human haemoglobin contains significant haem disorder. This results from the insertion of haem into globin with an orientation 180° different from the natural orientation. Haem disorder also slowly occurs in methaemoglobin solutions.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bonnett R., McDonagh A. F. The meso-reactivity of porphyrins and related compounds. VI. Oxidative cleavage of the haem system. The four isomeric biliverdins of the IX series. J Chem Soc Perkin 1. 1973;9:881–888. doi: 10.1039/p19730000881. [DOI] [PubMed] [Google Scholar]
- Brown N. A., King R. F., Shillcock M. E., Brown S. B. Haemoglobin catabolism: the role of ferrihaems in studies of the degradation pathway. Biochem J. 1974 Jan;137(1):135–137. doi: 10.1042/bj1370135. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown S. B., Chabot A. A., Enderby E. A., North A. C. Orientation of oxygen in oxyhaemoproteins and its implications for haem catabolism. Nature. 1981 Jan 1;289(5793):93–95. doi: 10.1038/289093a0. [DOI] [PubMed] [Google Scholar]
- Brown S. B., Docherty J. C. Haem degradation in abnormal haemoglobins. Biochem J. 1978 Sep 1;173(3):985–987. doi: 10.1042/bj1730985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown S. B. Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitro. Biochem J. 1976 Oct 1;159(1):23–27. doi: 10.1042/bj1590023. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bunn H. F., Jandl J. H. Exchange of heme among hemoglobin molecules. Proc Natl Acad Sci U S A. 1966 Sep;56(3):974–978. doi: 10.1073/pnas.56.3.974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bunn H. F., Jandl J. H. Exchange of heme among hemoglobins and between hemoglobin and albumin. J Biol Chem. 1968 Feb 10;243(3):465–475. [PubMed] [Google Scholar]
- La Mar G. N., Budd D. L., Viscio D. B., Smith K. M., Langry K. C. Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5755–5759. doi: 10.1073/pnas.75.12.5755. [DOI] [PMC free article] [PubMed] [Google Scholar]
- La Mar G. N., Smith K. M., Gersonde K., Sick H., Overkamp M. Proton nuclear nagnetic resonance characterization of heme disorder in monomeric insect hemoglobins. J Biol Chem. 1980 Jan 10;255(1):66–70. [PubMed] [Google Scholar]
- Perutz M. F. Structure and mechanism of haemoglobin. Br Med Bull. 1976 Sep;32(3):195–208. doi: 10.1093/oxfordjournals.bmb.a071363. [DOI] [PubMed] [Google Scholar]
- Steigemann W., Weber E. Structure of erythrocruorin in different ligand states refined at 1.4 A resolution. J Mol Biol. 1979 Jan 25;127(3):309–338. doi: 10.1016/0022-2836(79)90332-2. [DOI] [PubMed] [Google Scholar]
- WINTERHALTER K. H., HUEHNS E. R. PREPARATIONS, PROPERTIES, AND SPECIFIC RECOMBINATION OF ALPHA-BETA-GLOBIN SUBUNITS. J Biol Chem. 1964 Nov;239:3699–3705. [PubMed] [Google Scholar]
