Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 Oct 1;223(1):205–209. doi: 10.1042/bj2230205

Formation of bile pigments by coupled oxidation of cobalt-substituted haemoglobin and myoglobin.

D I Vernon, S B Brown
PMCID: PMC1144281  PMID: 6497839

Abstract

Treatment of cobalt-substituted haemoglobin and myoglobin with ascorbate and molecular O2 (coupled oxidation) resulted in biliverdin formation from the cobalt(II) derivatives but not from the cobalt(III) derivatives. This was apparently due to the inability of ascorbate to reduce cobalt(III) haemoproteins. Isomer analysis of the biliverdins produced from coupled oxidation of cobalt(II) oxyhaemoglobin suggested that the orientation of the cobalt protoporphyrin IX in the haem pocket differed slightly from that of the haem in native haemoglobin.

Full text

PDF
205

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 'Carra P. O., Colleran E. HAEM catabolism and coupled oxidation of haemproteins. FEBS Lett. 1969 Nov 29;5(4):295–298. doi: 10.1016/0014-5793(69)80372-8. [DOI] [PubMed] [Google Scholar]
  2. Bonnett R., Dimsdale M. J. The meso-reactivity of porphyrins and related compounds. V. The meso-oxidation of metalloporphyrins. J Chem Soc Perkin 1. 1972;20:2540–2548. doi: 10.1039/p19720002540. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. Dickinson L. C., Chien C. W. Comparative biological chemistry of cobalt hemoglobin. J Biol Chem. 1973 Jul 25;248(14):5005–5011. [PubMed] [Google Scholar]
  8. Docherty J. C., Brown S. B. Haem disorder in reconstituted human haemoglobin. Biochem J. 1982 Dec 1;207(3):583–587. doi: 10.1042/bj2070583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HUISMAN T. H., DOZY A. M. Studies on the heterogeneity of hemoglobin. V. Binding of hemoglobin with oxidized glutathione. J Lab Clin Med. 1962 Aug;60:302–319. [PubMed] [Google Scholar]
  10. Hoffman B. M., Petering D. H. Coboglobins: oxygen-carrying cobalt-reconstituted hemoglobin and myoglobin. Proc Natl Acad Sci U S A. 1970 Oct;67(2):637–643. doi: 10.1073/pnas.67.2.637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hoffman B. M., Spilburg C. A., Petering D. H. Coboglobins: cobalt substitution and the nature of the prosthetic group--apoprotein interaction in hemoglobin and myoglobin. Cold Spring Harb Symp Quant Biol. 1972;36:343–348. doi: 10.1101/sqb.1972.036.01.045. [DOI] [PubMed] [Google Scholar]
  12. King R. F., Brown S. B. The mechanism of haem catabolism. A study of haem breakdown in spleen microsomal fraction and in a model system by 18O labelling and metal substitution. Biochem J. 1978 Jul 15;174(1):103–109. doi: 10.1042/bj1740103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Maines M. D., Kappas A. Enzymatic oxidation of cobalt protoporphyrin IX: observations on the mechanism of heme oxygenase action. Biochemistry. 1977 Feb 8;16(3):419–423. doi: 10.1021/bi00622a012. [DOI] [PubMed] [Google Scholar]
  15. Schacter B. A., Waterman M. R. Activity of various metalloporphyrin protein complexes with microsomal heme oxygenase. Life Sci. 1974 Jan 1;14(1):47–53. doi: 10.1016/0024-3205(74)90244-6. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Yonetani T., Asakura T. Studies on cytochrome c peroxidase. XV. Comparison of manganese porphyrin-containing cytochrome c peroxidase, horseradish peroxidase, and myoglobin. J Biol Chem. 1969 Sep 10;244(17):4580–4588. [PubMed] [Google Scholar]
  18. Yonetani T., Yamamoto H., Woodrow G. V., 3rd Studies on cobalt myoglobins and hemoglobins. I. Preparation and optical properties of myoglobins and hemoglobins containing cobalt proto-, meso-, and deuteroporphyrins and thermodynamic characterization of their reversible oxygenation. J Biol Chem. 1974 Feb 10;249(3):682–690. [PubMed] [Google Scholar]
  19. Yoshida T., Kikuchi G. Reaction of the microsomal heme oxygenase with cobaltic protoporphyrin IX, and extremely poor substrate. J Biol Chem. 1978 Dec 10;253(23):8479–8482. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES