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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Published in | Biochimica et biophysica acta Vol. 445; no. 2; pp. 324 - 329 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Netherlands
14.09.1976
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Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-3002 |
DOI: | 10.1016/0005-2744(76)90086-3 |