Reactions of the NAD radical with higher oxidation states of horseradish peroxidase
The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(...
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| Veröffentlicht in: | Biochemistry (Easton) 1990-02, Vol.29 (8), p.2080-2084 |
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| container_title | Biochemistry (Easton) |
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| creator | Kobayashi, Kazuo Hayashi, Koichiro Swallow, A. John |
| description | The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(8) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of NAD. with native compound II at pH 10.0 nor with diacetyldeutero-compound II at pH 5.0-8.0 could be detected. Other reducing species generated by pulse radiolysis, such as hydrated electron (eaq-), superoxide anion (O2-), and benzoate anion radical, could not reduce compound II of the enzyme to the ferric state, although the methylviologen radical reduced it. The results are discussed in relation to the mechanism of catalysis of the one-electron oxidation of substrates by peroxidase. |
| doi_str_mv | 10.1021/bi00460a017 |
| format | Article |
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John</creator><creatorcontrib>Kobayashi, Kazuo ; Hayashi, Koichiro ; Swallow, A. John</creatorcontrib><description>The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(8) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of NAD. with native compound II at pH 10.0 nor with diacetyldeutero-compound II at pH 5.0-8.0 could be detected. Other reducing species generated by pulse radiolysis, such as hydrated electron (eaq-), superoxide anion (O2-), and benzoate anion radical, could not reduce compound II of the enzyme to the ferric state, although the methylviologen radical reduced it. The results are discussed in relation to the mechanism of catalysis of the one-electron oxidation of substrates by peroxidase.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00460a017</identifier><identifier>PMID: 2328239</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Ferric Compounds - metabolism ; Fundamental and applied biological sciences. Psychology ; Horseradish Peroxidase - metabolism ; Kinetics ; NAD - metabolism ; NAD super(+) ; Oxidation-Reduction ; Oxidoreductases ; Peroxidases - metabolism</subject><ispartof>Biochemistry (Easton), 1990-02, Vol.29 (8), p.2080-2084</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a415t-39153d71ec483a95a83d0830ff457ca9a25c9c06706fab6c416c9023ad316dbd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00460a017$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00460a017$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>315,781,785,2766,27078,27926,27927,56740,56790</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19587226$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2328239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobayashi, Kazuo</creatorcontrib><creatorcontrib>Hayashi, Koichiro</creatorcontrib><creatorcontrib>Swallow, A. John</creatorcontrib><title>Reactions of the NAD radical with higher oxidation states of horseradish peroxidase</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(8) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of NAD. with native compound II at pH 10.0 nor with diacetyldeutero-compound II at pH 5.0-8.0 could be detected. Other reducing species generated by pulse radiolysis, such as hydrated electron (eaq-), superoxide anion (O2-), and benzoate anion radical, could not reduce compound II of the enzyme to the ferric state, although the methylviologen radical reduced it. The results are discussed in relation to the mechanism of catalysis of the one-electron oxidation of substrates by peroxidase.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Ferric Compounds - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Kinetics</subject><subject>NAD - metabolism</subject><subject>NAD super(+)</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>Peroxidases - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0EtvEzEUBWALgUpaWLFG8ga6qKa9tsf2eFn6AqnqmwqxsW48HsYlyQTfidr-eyZNVFggsbKuzqcj6zD2TsCuACn2xgmgNIAg7As2ElpCUTqnX7IRAJhCOgOv2SbR3XCWYMsNtiGVrKRyI3Z9FTH0qZsR7xret5Gf7R_yjHUKOOH3qW95m360MfPuIdW4lJx67OOTb7tMcYmp5fOYnwjFN-xVgxOKb9fvFvt6fHRz8Lk4PT_5crB_WmApdF8oJ7SqrYihrBQ6jZWqoVLQNKW2AR1KHVwAY8E0ODahFCY4kAprJUw9rtUW-7jqnefu1yJS76eJQpxMcBa7BXnrrHSg1X-h0No4a2CAOysYckeUY-PnOU0xP3oBfrm1_2vrQb9f1y7G01g_2_W4Q_5hnSMNazYZZyHRn0qnKyulGVyxcon6-PCcY_7pjVVW-5uLay9vv53cXny69N8Hv73yGMjfdYs8G1b-5w9_A4j2oUY</recordid><startdate>19900227</startdate><enddate>19900227</enddate><creator>Kobayashi, Kazuo</creator><creator>Hayashi, Koichiro</creator><creator>Swallow, A. 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John</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a415t-39153d71ec483a95a83d0830ff457ca9a25c9c06706fab6c416c9023ad316dbd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Ferric Compounds - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Kinetics</topic><topic>NAD - metabolism</topic><topic>NAD super(+)</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases</topic><topic>Peroxidases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobayashi, Kazuo</creatorcontrib><creatorcontrib>Hayashi, Koichiro</creatorcontrib><creatorcontrib>Swallow, A. 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John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reactions of the NAD radical with higher oxidation states of horseradish peroxidase</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1990-02-27</date><risdate>1990</risdate><volume>29</volume><issue>8</issue><spage>2080</spage><epage>2084</epage><pages>2080-2084</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(8) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of NAD. with native compound II at pH 10.0 nor with diacetyldeutero-compound II at pH 5.0-8.0 could be detected. Other reducing species generated by pulse radiolysis, such as hydrated electron (eaq-), superoxide anion (O2-), and benzoate anion radical, could not reduce compound II of the enzyme to the ferric state, although the methylviologen radical reduced it. The results are discussed in relation to the mechanism of catalysis of the one-electron oxidation of substrates by peroxidase.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2328239</pmid><doi>10.1021/bi00460a017</doi><tpages>5</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Ferric Compounds - metabolism Fundamental and applied biological sciences. Psychology Horseradish Peroxidase - metabolism Kinetics NAD - metabolism NAD super(+) Oxidation-Reduction Oxidoreductases Peroxidases - metabolism |
| title | Reactions of the NAD radical with higher oxidation states of horseradish peroxidase |
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