Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase
Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where the spectrum of horseradish peroxidase compound I i...
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| Veröffentlicht in: | The Journal of biological chemistry 1981-02, Vol.256 (3), p.1091-1093 |
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| container_title | The Journal of biological chemistry |
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| creator | Satterlee, J D Erman, J E |
| description | Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase
compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where
the spectrum of horseradish peroxidase compound I is similar to that of the native protein, cytochrome c peroxidase compound
I exhibits only broad resonances near 17 and 30 ppm from 2,2-dimethyl-2-silapentane-5-sulfonate. No unique resonances attributable
to cytochrome c peroxidase compound II could be identified. These results define the molecular conditions for which resolved
hyperfine resonances of the iron(IV) states of heme proteins may be observed when the data presented here are compared with
the data from horseradish peroxidase. Oxidation of cytochrome c peroxidase while it is complexed to ferricytochrome c reveals
that the heme resonances of cytochrome c are not influenced by the oxidation state of cytochrome c peroxidase. |
| doi_str_mv | 10.1016/S0021-9258(19)69928-X |
| format | Article |
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compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where
the spectrum of horseradish peroxidase compound I is similar to that of the native protein, cytochrome c peroxidase compound
I exhibits only broad resonances near 17 and 30 ppm from 2,2-dimethyl-2-silapentane-5-sulfonate. No unique resonances attributable
to cytochrome c peroxidase compound II could be identified. These results define the molecular conditions for which resolved
hyperfine resonances of the iron(IV) states of heme proteins may be observed when the data presented here are compared with
the data from horseradish peroxidase. Oxidation of cytochrome c peroxidase while it is complexed to ferricytochrome c reveals
that the heme resonances of cytochrome c are not influenced by the oxidation state of cytochrome c peroxidase.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)69928-X</identifier><identifier>PMID: 6256380</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Cytochrome-c Peroxidase - metabolism ; Ferrocyanides ; Heme - analysis ; Horseradish Peroxidase ; Magnetic Resonance Spectroscopy ; Oxidation-Reduction ; Peroxidases - metabolism ; Protein Binding ; Saccharomyces cerevisiae - enzymology</subject><ispartof>The Journal of biological chemistry, 1981-02, Vol.256 (3), p.1091-1093</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-ad37513274c3544d7e31bf890844c3d7502c387d52751269ba77a31a0ba3883e3</citedby><cites>FETCH-LOGICAL-c378t-ad37513274c3544d7e31bf890844c3d7502c387d52751269ba77a31a0ba3883e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6256380$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Satterlee, J D</creatorcontrib><creatorcontrib>Erman, J E</creatorcontrib><title>Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase
compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where
the spectrum of horseradish peroxidase compound I is similar to that of the native protein, cytochrome c peroxidase compound
I exhibits only broad resonances near 17 and 30 ppm from 2,2-dimethyl-2-silapentane-5-sulfonate. No unique resonances attributable
to cytochrome c peroxidase compound II could be identified. These results define the molecular conditions for which resolved
hyperfine resonances of the iron(IV) states of heme proteins may be observed when the data presented here are compared with
the data from horseradish peroxidase. Oxidation of cytochrome c peroxidase while it is complexed to ferricytochrome c reveals
that the heme resonances of cytochrome c are not influenced by the oxidation state of cytochrome c peroxidase.</description><subject>Cytochrome-c Peroxidase - metabolism</subject><subject>Ferrocyanides</subject><subject>Heme - analysis</subject><subject>Horseradish Peroxidase</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Oxidation-Reduction</subject><subject>Peroxidases - metabolism</subject><subject>Protein Binding</subject><subject>Saccharomyces cerevisiae - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1LwzAUhoMoOj9-wqB4IXpRTZqmSS5l-AWCggq7C2l6tkbXZiYZuv16MzeWm0De5z2HPAgNCb4mmFQ3bxgXJJcFE5dEXlVSFiIf76EBwYLmlJHxPhrskCN0HMInTqeU5BAdVgWrqMAD9PXqXXR91i_MDLTPOj3tIVqTeQiu172BzLTaaxPB25WONrFuksUWMvdrG7uCJrN9CjtorI4Q1qlZRmda77pUzubg16QOcIoOJnoW4Gx7n6CP-7v30WP-_PLwNLp9zg3lIua6oZwRWvDSUFaWDQdK6omQWJTppeEMF4YK3rAiYUUla825pkTjWlMhKNATdLGZO_fuewEhqs4GA7OZ7sEtguKslEkDSSDbgMa7EDxM1NzbTvulIlitJat_yWptUBGp_iWrceoNtwsWdfr3rrW1mvLzTd7aaftjPajaJiHQqQQomkZLQv8APhuE0Q</recordid><startdate>19810210</startdate><enddate>19810210</enddate><creator>Satterlee, J D</creator><creator>Erman, J E</creator><general>American Society for Biochemistry and Molecular Biology</general><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>19810210</creationdate><title>Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase</title><author>Satterlee, J D ; Erman, J E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-ad37513274c3544d7e31bf890844c3d7502c387d52751269ba77a31a0ba3883e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Cytochrome-c Peroxidase - metabolism</topic><topic>Ferrocyanides</topic><topic>Heme - analysis</topic><topic>Horseradish Peroxidase</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Oxidation-Reduction</topic><topic>Peroxidases - metabolism</topic><topic>Protein Binding</topic><topic>Saccharomyces cerevisiae - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Satterlee, J D</creatorcontrib><creatorcontrib>Erman, J E</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Satterlee, J D</au><au>Erman, J E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-02-10</date><risdate>1981</risdate><volume>256</volume><issue>3</issue><spage>1091</spage><epage>1093</epage><pages>1091-1093</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Oxidation of cytochrome c peroxidase with hydrogen peroxide to form the initial oxidized intermediate, cytochrome c peroxidase
compound I, drastically alters the proton hyperfine nmr spectrum. In contrast to studies of horseradish peroxidase, where
the spectrum of horseradish peroxidase compound I is similar to that of the native protein, cytochrome c peroxidase compound
I exhibits only broad resonances near 17 and 30 ppm from 2,2-dimethyl-2-silapentane-5-sulfonate. No unique resonances attributable
to cytochrome c peroxidase compound II could be identified. These results define the molecular conditions for which resolved
hyperfine resonances of the iron(IV) states of heme proteins may be observed when the data presented here are compared with
the data from horseradish peroxidase. Oxidation of cytochrome c peroxidase while it is complexed to ferricytochrome c reveals
that the heme resonances of cytochrome c are not influenced by the oxidation state of cytochrome c peroxidase.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6256380</pmid><doi>10.1016/S0021-9258(19)69928-X</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1981-02, Vol.256 (3), p.1091-1093 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75494911 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Cytochrome-c Peroxidase - metabolism Ferrocyanides Heme - analysis Horseradish Peroxidase Magnetic Resonance Spectroscopy Oxidation-Reduction Peroxidases - metabolism Protein Binding Saccharomyces cerevisiae - enzymology |
| title | Proton nuclear magnetic resonance characterization of the oxidized intermediates of cytochrome c peroxidase |
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