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Olsen J, Davis L. The oxidation of dithiothreitol by peroxidases and oxygen. Biochim Biophys Acta. 1976;445(2):324-9doi: 10.1016/0005-2744(76)90086-3.
Olsen, J., & Davis, L. (1976). The oxidation of dithiothreitol by peroxidases and oxygen. Biochimica et biophysica acta, 445(2), 324-9. https://doi.org/10.1016/0005-2744(76)90086-3
Olsen, J, and Davis, L. "The oxidation of dithiothreitol by peroxidases and oxygen." Biochimica et biophysica acta vol. 445,2 (1976): 324-9. doi: https://doi.org/10.1016/0005-2744(76)90086-3
Olsen J, Davis L. The oxidation of dithiothreitol by peroxidases and oxygen. Biochim Biophys Acta. 1976 Sep 14;445(2):324-9. doi: 10.1016/0005-2744(76)90086-3. PMID: 953035.
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Biochim Biophys Acta. 1976 Sep 14;445(2):324-9. doi: 10.1016/0005-2744(76)90086-3.

The oxidation of dithiothreitol by peroxidases and oxygen.

Biochimica et biophysica acta

J Olsen, L Davis

PMID: 953035 DOI: 10.1016/0005-2744(76)90086-3

Abstract

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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