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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-5-13
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pubmed:abstractText |
We obtained spectroscopic evidence in support of salicylate-dependent inactivation of horseradish peroxidase-C. Addition of salicylate to the enzyme arrested at a temporal inactive state (Compound III) in the presence of H2O2, resulted in rapid and irreversible inactivation of the enzyme yielding verdohemoproteins (P-670). Multiple roles for salicylate in peroxidase-catalyzed reactions are discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0916-8451
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
646-50
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
Spectroscopic evidence that salicylic acid converts a temporally inactivated form of horseradish peroxidase (compound III) to the irreversibly inactivated verdohemoprotein (P-670).
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pubmed:affiliation |
UMR INRA-UHP Interactions Arbre/Micro-Organismes, Centre Institut National de la Recherche Agronomique de Nancy, Champenoux, France. kawanotom@sci.hiroshima-u.ac.jp
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pubmed:publicationType |
Journal Article
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