Reactions of heme peroxidases with peroxynitrite
The interaction of peroxynitrite, produced by ozonation of azide, with two heme peroxidases (horseradish peroxidase and lactoperoxidase) was studied. Enzymes retained full activity after incubation with peroxynitrite at neutral pH. Lactoperoxidase alone was found to catalyze peroxynitrite decomposit...
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| Veröffentlicht in: | IUBMB life 2000-01, Vol.49 (1), p.11-15 |
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| creator | Gebicka, L Gebicki, J L |
| description | The interaction of peroxynitrite, produced by ozonation of azide, with two heme peroxidases (horseradish peroxidase and lactoperoxidase) was studied. Enzymes retained full activity after incubation with peroxynitrite at neutral pH. Lactoperoxidase alone was found to catalyze peroxynitrite decomposition, whereas horseradish peroxidase accelerated peroxynitrite decomposition only in the presence of certain substrates. For example, in the presence of guaiacol the catalyzing effect was clear, but in the presence of trolox was only noticeable. |
| doi_str_mv | 10.1080/152165400306304 |
| format | Article |
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Enzymes retained full activity after incubation with peroxynitrite at neutral pH. Lactoperoxidase alone was found to catalyze peroxynitrite decomposition, whereas horseradish peroxidase accelerated peroxynitrite decomposition only in the presence of certain substrates. For example, in the presence of guaiacol the catalyzing effect was clear, but in the presence of trolox was only noticeable.</description><identifier>ISSN: 1521-6543</identifier><identifier>EISSN: 1521-6551</identifier><identifier>DOI: 10.1080/152165400306304</identifier><identifier>PMID: 10772335</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Guaiacol - metabolism ; Horseradish Peroxidase - metabolism ; Kinetics ; Lactoperoxidase - metabolism ; Nitrates - metabolism ; Oxidoreductases - metabolism ; Plants - enzymology ; Substrate Specificity ; Time Factors</subject><ispartof>IUBMB life, 2000-01, Vol.49 (1), p.11-15</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10772335$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gebicka, L</creatorcontrib><creatorcontrib>Gebicki, J L</creatorcontrib><title>Reactions of heme peroxidases with peroxynitrite</title><title>IUBMB life</title><addtitle>IUBMB Life</addtitle><description>The interaction of peroxynitrite, produced by ozonation of azide, with two heme peroxidases (horseradish peroxidase and lactoperoxidase) was studied. Enzymes retained full activity after incubation with peroxynitrite at neutral pH. Lactoperoxidase alone was found to catalyze peroxynitrite decomposition, whereas horseradish peroxidase accelerated peroxynitrite decomposition only in the presence of certain substrates. For example, in the presence of guaiacol the catalyzing effect was clear, but in the presence of trolox was only noticeable.</description><subject>Animals</subject><subject>Guaiacol - metabolism</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Kinetics</subject><subject>Lactoperoxidase - metabolism</subject><subject>Nitrates - metabolism</subject><subject>Oxidoreductases - metabolism</subject><subject>Plants - enzymology</subject><subject>Substrate Specificity</subject><subject>Time Factors</subject><issn>1521-6543</issn><issn>1521-6551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkM1Lw0AQxRdRbK2evUlO3mJnv7LJUYpVoSBI72GzO6ErSTbupmj_e1NSRJzLDI_fPHiPkFsKDxRyWFLJaCYFAIeMgzgj86OSZlLS899b8Bm5ivEDxlFQXJIZBaUY53JO4B21GZzvYuLrZIctJj0G_-2sjhiTLzfsJuHQuSG4Aa_JRa2biDenvSDb9dN29ZJu3p5fV4-b1DChhlQgt8awAiqKwkpha85zzAQTGRaisEIxDbLWCpXNNVamMJLVudBoCmCWL8j9ZNsH_7nHOJStiwabRnfo97FUFOSYMhvB5QSa4GMMWJd9cK0Oh5JCeeyo_NfR-HF3st5XLdo__FQK_wGx32Dv</recordid><startdate>200001</startdate><enddate>200001</enddate><creator>Gebicka, L</creator><creator>Gebicki, J L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200001</creationdate><title>Reactions of heme peroxidases with peroxynitrite</title><author>Gebicka, L ; Gebicki, J L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c247t-4e3dcc290b1e4d54df338e64246e949d472a05fa7e7d8aebc9c52f84aec902d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Guaiacol - metabolism</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Kinetics</topic><topic>Lactoperoxidase - metabolism</topic><topic>Nitrates - metabolism</topic><topic>Oxidoreductases - metabolism</topic><topic>Plants - enzymology</topic><topic>Substrate Specificity</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gebicka, L</creatorcontrib><creatorcontrib>Gebicki, J L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>IUBMB life</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gebicka, L</au><au>Gebicki, J L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reactions of heme peroxidases with peroxynitrite</atitle><jtitle>IUBMB life</jtitle><addtitle>IUBMB Life</addtitle><date>2000-01</date><risdate>2000</risdate><volume>49</volume><issue>1</issue><spage>11</spage><epage>15</epage><pages>11-15</pages><issn>1521-6543</issn><eissn>1521-6551</eissn><abstract>The interaction of peroxynitrite, produced by ozonation of azide, with two heme peroxidases (horseradish peroxidase and lactoperoxidase) was studied. Enzymes retained full activity after incubation with peroxynitrite at neutral pH. Lactoperoxidase alone was found to catalyze peroxynitrite decomposition, whereas horseradish peroxidase accelerated peroxynitrite decomposition only in the presence of certain substrates. For example, in the presence of guaiacol the catalyzing effect was clear, but in the presence of trolox was only noticeable.</abstract><cop>England</cop><pmid>10772335</pmid><doi>10.1080/152165400306304</doi><tpages>5</tpages></addata></record> |
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| subjects | Animals Guaiacol - metabolism Horseradish Peroxidase - metabolism Kinetics Lactoperoxidase - metabolism Nitrates - metabolism Oxidoreductases - metabolism Plants - enzymology Substrate Specificity Time Factors |
| title | Reactions of heme peroxidases with peroxynitrite |
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