Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1955 Jun;60(2):310–325. doi: 10.1042/bj0600310

Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions

D Keilin 1, E F Hartree 1
PMCID: PMC1215698  PMID: 14389241

Full text

PDF
310

Selected References

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

  1. AVIS P. G., BERGEL F., BRAY R. C., SHOOTER K. V. A crystalline material with xanthine oxidase activity. Nature. 1954 Jun 26;173(4417):1230–1231. doi: 10.1038/1731230a0. [DOI] [PubMed] [Google Scholar]
  2. BENTLEY R., NEUBERGER A. The mechanism of the action of notation. Biochem J. 1949;45(5):584–590. doi: 10.1042/bj0450584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CHANCE B. Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase. J Biol Chem. 1952 Feb;194(2):471–481. [PubMed] [Google Scholar]
  4. CHANCE B., GREENSTEIN D. S., ROUGHTON F. J. W. The mechanism of catalase action. I. Steady-state analysis. Arch Biochem Biophys. 1952 Jun;37(2):301–321. doi: 10.1016/0003-9861(52)90194-x. [DOI] [PubMed] [Google Scholar]
  5. CHANCE B. The kinetics and stoichiometry of the transition from the primary to the secondary peroxidase peroxide complexes. Arch Biochem Biophys. 1952 Dec;41(2):416–424. doi: 10.1016/0003-9861(52)90470-0. [DOI] [PubMed] [Google Scholar]
  6. Chance B. The Properties of the Enzyme-Substrate Compounds of Horse-Radish and Lacto-Peroxidase. Science. 1949 Feb 25;109(2826):204–208. doi: 10.1126/science.109.2826.204-a. [DOI] [PubMed] [Google Scholar]
  7. Dixon M. A note on peroxidase specificity. Biochem J. 1934;28(6):2061–2064. doi: 10.1042/bj0282061. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Elliott K. A. Oxidations catalysed by horseradish- and milk-peroxidases. Biochem J. 1932;26(4):1281–1290. doi: 10.1042/bj0261281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GEORGE P., IRVINE D. H. The reaction between metmyoglobin and alkyl hydro-peroxides. Biochem J. 1953 Sep;55(2):230–236. doi: 10.1042/bj0550230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. GEORGE P., IRVINE D. H. The reaction between metmyoglobin and hydrogen peroxide. Biochem J. 1952 Nov;52(3):511–517. doi: 10.1042/bj0520511. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GEORGE P. Redox reactions of catalase intermediate compounds and a new peroxidatic role for catalase. Biochem J. 1952 Dec;52(4):xix–xix. [PubMed] [Google Scholar]
  12. GEORGE P. The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. I. Titration with reducing agents. Biochem J. 1953 May;54(2):267–276. doi: 10.1042/bj0540267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Harrison D. C., Thurlow S. The Secondary Oxidation of some Substances of Physiological Interest. Biochem J. 1926;20(2):217–231. doi: 10.1042/bj0200217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. KEILIN D., HARTREE E. F. Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem J. 1951 Jun;49(1):88–104. doi: 10.1042/bj0490088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. KEILIN D., HARTREE E. F. Reaction of methaemoglobin with hydrogen peroxide. Nature. 1950 Sep 23;166(4221):513–514. doi: 10.1038/166513a0. [DOI] [PubMed] [Google Scholar]
  16. KEILIN D., HARTREE E. F. Reactions of methaemoglobin and catalase with peroxides and hydrogen donors. Nature. 1954 Apr 17;173(4407):720–723. doi: 10.1038/173720a0. [DOI] [PubMed] [Google Scholar]
  17. KEILIN D., HARTREE E. F. Specificity of glucose oxidase (notatin). Biochem J. 1952 Jan;50(3):331–341. doi: 10.1042/bj0500331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. KENTEN R. H., MANN P. J. G. The action of peroxidase systems on ferrocyanide, molybdate, tungstate and vanadate. Biochem J. 1951 Nov;50(1):29–34. doi: 10.1042/bj0500029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. KNOX W. E. The action of peroxidases with enzymically generated peroxide in the presence of catalase. Biochim Biophys Acta. 1954 May;14(1):117–126. doi: 10.1016/0006-3002(54)90138-9. [DOI] [PubMed] [Google Scholar]
  20. Keilin D., Hartree E. F. Properties of azide-catalase. Biochem J. 1945;39(2):148–157. doi: 10.1042/bj0390148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Keilin D., Hartree E. F. Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochem J. 1945;39(4):293–301. [PMC free article] [PubMed] [Google Scholar]
  22. Morris D. L. Quantitative Determination of Carbohydrates With Dreywood's Anthrone Reagent. Science. 1948 Mar 5;107(2775):254–255. doi: 10.1126/science.107.2775.254. [DOI] [PubMed] [Google Scholar]
  23. THEORELL H., EHRENBERG A. Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase. Arch Biochem Biophys. 1952 Dec;41(2):442–461. [PubMed] [Google Scholar]
  24. Thurlow S. Studies on Xanthine Oxidase: Relation of Xanthine Oxidase and similar Oxidising Systems to Bach's Oxygenase. Biochem J. 1925;19(2):175–187. doi: 10.1042/bj0190175. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES