Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes
Direct electron transfer between covalently immobilized flavoenzymes and a cyanuric chloride-modified graphite electrode is observed via differential pulse voltammetry. L-Amino acid oxidase and xanthine oxidase display peaks arising from the reduction of flavin adenine dinucleotide. Peak current enh...
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| Veröffentlicht in: | Analytica chimica acta 1982-09, Vol.141, p.23-32 |
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| container_title | Analytica chimica acta |
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| creator | Ianniello, Robert M. Lindsay, Thomas J. Yacynych, Alexander M. |
| description | Direct electron transfer between covalently immobilized flavoenzymes and a cyanuric chloride-modified graphite electrode is observed via differential pulse voltammetry. L-Amino acid oxidase and xanthine oxidase display peaks arising from the reduction of flavin adenine dinucleotide. Peak current enhancements are observed for both covalently attached enzymes compared to their free and adsorbed state voltammograms. Studies concerning flavin removal and reconstitution indicate that xanthine oxidase contains multiple flavin chromophores which are nonequivalent. |
| doi_str_mv | 10.1016/S0003-2670(01)95307-3 |
| format | Article |
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L-Amino acid oxidase and xanthine oxidase display peaks arising from the reduction of flavin adenine dinucleotide. Peak current enhancements are observed for both covalently attached enzymes compared to their free and adsorbed state voltammograms. Studies concerning flavin removal and reconstitution indicate that xanthine oxidase contains multiple flavin chromophores which are nonequivalent.</description><identifier>ISSN: 0003-2670</identifier><identifier>EISSN: 1873-4324</identifier><identifier>DOI: 10.1016/S0003-2670(01)95307-3</identifier><language>eng</language><publisher>Elsevier B.V</publisher><subject>electrodes ; electron transfer ; immobilized enzymes ; L-amino-acid oxidase ; xanthine oxidase</subject><ispartof>Analytica chimica acta, 1982-09, Vol.141, p.23-32</ispartof><rights>1982</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-60d1ae8b8c8e1d3c014cef9b4d3fd23c286cdc240db418c0a4841e22bb4f72503</citedby><cites>FETCH-LOGICAL-c406t-60d1ae8b8c8e1d3c014cef9b4d3fd23c286cdc240db418c0a4841e22bb4f72503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003267001953073$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Ianniello, Robert M.</creatorcontrib><creatorcontrib>Lindsay, Thomas J.</creatorcontrib><creatorcontrib>Yacynych, Alexander M.</creatorcontrib><title>Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes</title><title>Analytica chimica acta</title><description>Direct electron transfer between covalently immobilized flavoenzymes and a cyanuric chloride-modified graphite electrode is observed via differential pulse voltammetry. L-Amino acid oxidase and xanthine oxidase display peaks arising from the reduction of flavin adenine dinucleotide. Peak current enhancements are observed for both covalently attached enzymes compared to their free and adsorbed state voltammograms. Studies concerning flavin removal and reconstitution indicate that xanthine oxidase contains multiple flavin chromophores which are nonequivalent.</description><subject>electrodes</subject><subject>electron transfer</subject><subject>immobilized enzymes</subject><subject>L-amino-acid oxidase</subject><subject>xanthine oxidase</subject><issn>0003-2670</issn><issn>1873-4324</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><recordid>eNqFkM1LAzEQxYMoWKt_grAn0cPq5KO725NI_YSCB_XkIWSTiY1kNzXZFtq_3m2rXr3MMMx7D96PkFMKlxRocfUCADxnRQnnQC_GIw5lzvfIgFYlzwVnYp8M_iSH5Cilz_5kFMSAvN-6iLrL0PczhjbromqTxZi5NnNNE2rn3RpNZr1aBmzXqwYzPcPGaeX9KmuCcdb1_4-o5jPX4W-SwXRMDqzyCU9-9pC83d-9Th7z6fPD0-RmmmsBRZcXYKjCqq50hdRwDVRotONaGG4N45pVhTaaCTC1oJUGJSpBkbG6FrZkI-BDcrbLncfwtcDUycYljd6rFsMiScpHBRO07IWjnVDHkFJEK-fRNSquJAW5QSm3KOWGkwQqtygl733XOx_2LZYOo0zaYavRbOFJE9w_Cd8tLH1L</recordid><startdate>19820901</startdate><enddate>19820901</enddate><creator>Ianniello, Robert M.</creator><creator>Lindsay, Thomas J.</creator><creator>Yacynych, Alexander M.</creator><general>Elsevier B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19820901</creationdate><title>Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes</title><author>Ianniello, Robert M. ; Lindsay, Thomas J. ; Yacynych, Alexander M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-60d1ae8b8c8e1d3c014cef9b4d3fd23c286cdc240db418c0a4841e22bb4f72503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>electrodes</topic><topic>electron transfer</topic><topic>immobilized enzymes</topic><topic>L-amino-acid oxidase</topic><topic>xanthine oxidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ianniello, Robert M.</creatorcontrib><creatorcontrib>Lindsay, Thomas J.</creatorcontrib><creatorcontrib>Yacynych, Alexander M.</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Analytica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ianniello, Robert M.</au><au>Lindsay, Thomas J.</au><au>Yacynych, Alexander M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes</atitle><jtitle>Analytica chimica acta</jtitle><date>1982-09-01</date><risdate>1982</risdate><volume>141</volume><spage>23</spage><epage>32</epage><pages>23-32</pages><issn>0003-2670</issn><eissn>1873-4324</eissn><abstract>Direct electron transfer between covalently immobilized flavoenzymes and a cyanuric chloride-modified graphite electrode is observed via differential pulse voltammetry. L-Amino acid oxidase and xanthine oxidase display peaks arising from the reduction of flavin adenine dinucleotide. Peak current enhancements are observed for both covalently attached enzymes compared to their free and adsorbed state voltammograms. Studies concerning flavin removal and reconstitution indicate that xanthine oxidase contains multiple flavin chromophores which are nonequivalent.</abstract><pub>Elsevier B.V</pub><doi>10.1016/S0003-2670(01)95307-3</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2670 |
| ispartof | Analytica chimica acta, 1982-09, Vol.141, p.23-32 |
| issn | 0003-2670 1873-4324 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_13562417 |
| source | Elsevier ScienceDirect Journals |
| subjects | electrodes electron transfer immobilized enzymes L-amino-acid oxidase xanthine oxidase |
| title | Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes |
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