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. 1961 Nov;81(2):365–374. doi: 10.1042/bj0810365

The action of anions on catalase peroxide compounds

P Nicholls 1
PMCID: PMC1243349  PMID: 14479445

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Selected References

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

  1. BEERS R. F., Jr, SIZER I. W. Progressive inhibition of the catalase-hydrogen peroxide system by acetate, chloride and azide. Arch Biochem Biophys. 1956 Jan;60(1):115–125. doi: 10.1016/0003-9861(56)90403-9. [DOI] [PubMed] [Google Scholar]
  2. BEERS R. F., Jr, SIZER I. W. Sulfide inhibition of catalase. Science. 1954 Jul 2;120(3105):32–33. doi: 10.1126/science.120.3105.32. [DOI] [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. Peroxidase heme linkages. Arch Biochem Biophys. 1952 Sep;40(1):153–164. doi: 10.1016/0003-9861(52)90083-0. [DOI] [PubMed] [Google Scholar]
  5. CHANCE B. The effect of pH upon the equilibria of catalase compounds. J Biol Chem. 1952 Feb;194(2):483–496. [PubMed] [Google Scholar]
  6. CHANCE B. The reactions of catalase in the presence of the notatin system. Biochem J. 1950 Apr;46(4):387–402. doi: 10.1042/bj0460387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DOUCE A. L., SCHWALENBERG R. R. Further investigation of the reducibility of lyophilized catalase. Science. 1950 Jun 16;111(2894):654–654. doi: 10.1126/science.111.2894.654. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. GEORGE P. The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. 2. Formation and decomposition. Biochem J. 1953 Sep;55(2):220–230. doi: 10.1042/bj0550220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Herbert D., Pinsent J. Crystalline bacterial catalase. Biochem J. 1948;43(2):193–202. doi: 10.1042/bj0430193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. KEILIN D., HARTREE E. F. Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions. Biochem J. 1955 Jun;60(2):310–325. doi: 10.1042/bj0600310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. KEILIN D., NICHOLLS P. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochim Biophys Acta. 1958 Aug;29(2):302–307. doi: 10.1016/0006-3002(58)90189-6. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Keilin D., Hartree E. F. Properties of glucose oxidase (notatin): Addendum. Sedimentation and diffusion of glucose oxidase (notatin). Biochem J. 1948;42(2):221–229. [PMC free article] [PubMed] [Google Scholar]
  17. LASER H. The effect of low oxygen tension on the activity of aerobic dehydrogenases. Proc R Soc Lond B Biol Sci. 1952 Oct 16;140(899):230–243. doi: 10.1098/rspb.1952.0060. [DOI] [PubMed] [Google Scholar]
  18. NICHOLLS P. The formation and properties of sulphmyoglobin and sulphcatalase. Biochem J. 1961 Nov;81:374–383. doi: 10.1042/bj0810374. [DOI] [PMC free article] [PubMed] [Google Scholar]

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