Skip to main content
Biochemical Journal logoLink to Biochemical Journal
letter
. 1984 Oct 1;223(1):279–280. doi: 10.1042/bj2230279

A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: oxidation, dissociation, or displacement?

K Shikama
PMCID: PMC1144293  PMID: 6497843

Full text

PDF
279

Selected References

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

  1. Brown W. D., Mebine L. B. Autoxidation of oxymyoglobins. J Biol Chem. 1969 Dec 25;244(24):6696–6701. [PubMed] [Google Scholar]
  2. Fridovich I. Superoxide dismutases. Annu Rev Biochem. 1975;44:147–159. doi: 10.1146/annurev.bi.44.070175.001051. [DOI] [PubMed] [Google Scholar]
  3. GEORGE P., STRATMANN C. J. The oxidation of myoglobin to metmyglobin by oxygen. 2. The relation between the first order rate constant and the partial pressure of oxygen. Biochem J. 1952 Jun;51(3):418–425. doi: 10.1042/bj0510418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GEORGE P., STRATMANN C. J. The oxidation of myoglobin to metmyoglobin by oxygen. III. Kinetic studies in the presence of carbon monoxide, and at different hydrogen-ion concentrations with considerations regarding the stability of oxymyoglobin. Biochem J. 1954 Aug;57(4):568–573. doi: 10.1042/bj0570568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Goto T., Shikama K. Autoxidation of native oxymyoglobin from bovine heart muscle. Arch Biochem Biophys. 1974 Aug;163(2):476–481. doi: 10.1016/0003-9861(74)90504-9. [DOI] [PubMed] [Google Scholar]
  6. Gotoh T., Shikama K. Generation of the superoxide radical during autoxidation of oxymyoglobin. J Biochem. 1976 Aug;80(2):397–399. doi: 10.1093/oxfordjournals.jbchem.a131289. [DOI] [PubMed] [Google Scholar]
  7. Misra H. P., Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem. 1972 Nov 10;247(21):6960–6962. [PubMed] [Google Scholar]
  8. Phillips S. E., Schoenborn B. P. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature. 1981 Jul 2;292(5818):81–82. doi: 10.1038/292081a0. [DOI] [PubMed] [Google Scholar]
  9. Satoh Y., Shikama K. Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism. J Biol Chem. 1981 Oct 25;256(20):10272–10275. [PubMed] [Google Scholar]
  10. Sawada Y., Iyanagi T., Yamazaki I. Relation between redox potentials and rate constants in reactions coupled with the system oxygen-superoxide. Biochemistry. 1975 Aug 26;14(17):3761–3764. doi: 10.1021/bi00688a007. [DOI] [PubMed] [Google Scholar]
  11. Shikama K., Sugawara Y. Autoxidation of native oxymyoglobin. Kinetic analysis of the pH profile. Eur J Biochem. 1978 Nov 15;91(2):407–413. doi: 10.1111/j.1432-1033.1978.tb12693.x. [DOI] [PubMed] [Google Scholar]
  12. Sugawara Y., Shikama K. Autoxidation of native oxymyoglobin. Thermodynamic analysis of the pH profile. Eur J Biochem. 1980 Sep;110(1):241–246. doi: 10.1111/j.1432-1033.1980.tb04861.x. [DOI] [PubMed] [Google Scholar]
  13. Suzuki T., Shikama K. Stability properties of sperm whale oxymyoglobin. Arch Biochem Biophys. 1983 Jul 15;224(2):695–699. doi: 10.1016/0003-9861(83)90257-6. [DOI] [PubMed] [Google Scholar]
  14. WEISS J. J. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN. Nature. 1964 Apr 4;202:83–84. doi: 10.1038/202083b0. [DOI] [PubMed] [Google Scholar]
  15. Wallace W. J., Houtchens R. A., Maxwell J. C., Caughey W. S. Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J Biol Chem. 1982 May 10;257(9):4966–4977. [PubMed] [Google Scholar]
  16. Wallace W. J., Maxwell J. C., Caughey W. S. A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes. FEBS Lett. 1974 Jul 1;43(1):33–36. doi: 10.1016/0014-5793(74)81099-9. [DOI] [PubMed] [Google Scholar]
  17. YAMAZAKI I., YOKOTA K. N., SHIKAMA K. PREPARATION OF CRYSTALLINE OXYMYOGLOBIN FROM HORSE HEART. J Biol Chem. 1964 Dec;239:4151–4153. [PubMed] [Google Scholar]

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

RESOURCES