The oxidation of dithiothreitol by peroxidases and oxygen

Horseradish peroxidase (1.11.1.7), lactoperoxidase (1.11.1.7), and the fragment of cytochrome c known as microperoxidase have been shown to catalyze the oxidation of reduced dithiothreitol in an oxygen-consuming reaction. Evidence for horseradish peroxidase intermediates compound III and compound II...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 445; no. 2; pp. 324 - 329
Main Authors Olsen, J, Davis, L
Format Journal Article
LanguageEnglish
Published Netherlands 14.09.1976
Subjects
Catalase - metabolism
Dithiothreitol
Horseradish Peroxidase - metabolism
Kinetics
Lactoperoxidase - metabolism
Oxidation-Reduction
Oxygen Consumption
Peroxidases - metabolism
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Summary:Horseradish peroxidase (1.11.1.7), lactoperoxidase (1.11.1.7), and the fragment of cytochrome c known as microperoxidase have been shown to catalyze the oxidation of reduced dithiothreitol in an oxygen-consuming reaction. Evidence for horseradish peroxidase intermediates compound III and compound II has been observed, although ferroperoxidase was not identified during the course of the reaction. The stoichiometry has been extablished as 1 : 1 for oxygen consumed to dithiothreitol oxidized. Cysteine and glutathione have also been shown to be substrates for horseradish peroxidase oxidase reaction.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-3002
DOI:10.1016/0005-2744(76)90086-3