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Selected References
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- CHANCE B. The properties of the enzyme-substrate compounds of horseradish peroxidase and peroxides; the reaction of complex II with ascorbic acid. Arch Biochem. 1949 Dec;24(2):389–409. [PubMed] [Google Scholar]
- CHANCE B. The transition from the primary to the secondary peroxidase-peroxide complex. Arch Biochem Biophys. 1952 May;37(1):235–237. doi: 10.1016/0003-9861(52)90181-1. [DOI] [PubMed] [Google Scholar]
- 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]
- GEORGE P. Chemical nature of the secondary hydrogen peroxide compound formed by cytochrome-c peroxidase and horseradish peroxidase. Nature. 1952 Apr 12;169(4302):612–613. doi: 10.1038/169612a0. [DOI] [PubMed] [Google Scholar]
- GEORGE P., IRVINE D. H. Reaction of methmyoglobin with hydrogen peroxide. Nature. 1951 Jul 28;168(4265):164–165. doi: 10.1038/168164b0. [DOI] [PubMed] [Google Scholar]
- 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]
- Keilin D., Hartree E. F. Activity of the cytochrome system in heart muscle preparations. Biochem J. 1947;41(4):500–502. doi: 10.1042/bj0410500. [DOI] [PMC free article] [PubMed] [Google Scholar]
- THEORELL H., EHRENBERG A., CHANCE B. Electronic structure of the peroxidase-peroxide complexes. Arch Biochem Biophys. 1952 May;37(1):237–239. doi: 10.1016/0003-9861(52)90182-3. [DOI] [PubMed] [Google Scholar]