Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1973 Oct;135(2):361–365. doi: 10.1042/bj1350361

Oxidation of deuteroferrihaem by hydrogen peroxide

Peter Jones 1, Kenneth Prudhoe 1, Terrence Robson 1
PMCID: PMC1165831  PMID: 4764268

Abstract

1. The oxidation of deuteroferrihaem by H2O2 to bile pigment and CO was studied both by stopped-flow kinetic spectrophotometry and mass spectrometry, at 25°C, I=0.1m. 2. Spectrophotometric studies imply that, at constant pH, the rate of bile pigment formation is first-order with respect to [H2O2] and also proportional to [deuteroferrihaem monomer]. The effect of pH on the apparent second-order rate constant suggests that acid-ionization of deuteroferrihaem monomer is important in the reaction mechanism. 3. The relative rates of formation of O2 (from catalytic decomposition of H2O2) and CO (from oxidation of ferrihaem) have been measured by mass spectrometry. The results are in excellent agreement with those obtained by combining kinetic data for catalytic decomposition (Jones et al., 1973, preceding paper) with the spectrophotometric results for deuteroferrihaem oxidation.

Full text

PDF

Selected References

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

  1. ANAN F. K., MASON H. S. An 018 study of the hemoglobin degradation to biliverdin in the model reaction. J Biochem. 1961 Jun;49:765–767. doi: 10.1093/oxfordjournals.jbchem.a127369. [DOI] [PubMed] [Google Scholar]
  2. BOYLAND E., SIMS P. Metabolism of polycylic compounds. XI. The conversion of naphthalene into 2-hydroxy-1-naphthyl sulphate in the rabbit. Biochem J. 1957 May;66(1):38–40. doi: 10.1042/bj0660038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brown S. B., Dean T. C., Jones P. Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution. Biochem J. 1970 May;117(4):733–739. doi: 10.1042/bj1170733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brown S. B., Dean T. C., Jones P. Catalatic activity of iron(3)-centred catalysts. Role of dimerization in the catalytic action of ferrihaems. Biochem J. 1970 May;117(4):741–744. doi: 10.1042/bj1170741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Jones P., Robson T., Brown S. B. The catalase activity of ferrihaems. Biochem J. 1973 Oct;135(2):353–359. doi: 10.1042/bj1350353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Portsmouth D., Beal E. A. The peroxidase activity of deuterohemin. Eur J Biochem. 1971 Apr 30;19(4):479–487. doi: 10.1111/j.1432-1033.1971.tb01338.x. [DOI] [PubMed] [Google Scholar]
  7. SJOSTRAND T. The in vitro formation of carbon monoxide in blood. Acta Physiol Scand. 1952 Feb 12;24(4):314–332. doi: 10.1111/j.1748-1716.1952.tb00848.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES