| Oxidation of NAD dimers by horseradish peroxidase. | |
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MedLine Citation:
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PMID: 3994664 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both horseradish-peroxidase-catalysed oxidation and peroxidation of (NAD)2. |
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Authors:
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L Avigliano; V Carelli; A Casini; A Finazzi-Agrò; F Liberatore |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 226 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1985 Mar |
Date Detail:
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Created Date: 1985-05-24 Completed Date: 1985-05-24 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 391-5 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Chromatography, High Pressure Liquid Horseradish Peroxidase / metabolism* Hydrogen-Ion Concentration Macromolecular Substances Models, Chemical NAD / metabolism* Oxidation-Reduction Peroxidases / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Macromolecular Substances; 53-84-9/NAD; EC 1.11.1.-/Horseradish Peroxidase; EC 1.11.1.-/Peroxidases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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