Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction
The efficient immobilization and orientation of bilirubin oxidase from Myrothecium verrucaria on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter is reported. By comparing the use of different types of porphyrin, the rational effect of the...
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| Veröffentlicht in: | Chemistry : a European journal 2015-11, Vol.21 (47), p.16868-16873 |
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| creator | Lalaoui, Noémie Le Goff, Alan Holzinger, Michael Cosnier, Serge |
| description | The efficient immobilization and orientation of bilirubin oxidase from Myrothecium verrucaria on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter is reported. By comparing the use of different types of porphyrin, the rational effect of the porphyrin structure on both the immobilization and orientation of the enzyme is demonstrated. The best performances were obtained for protoporphyrin IX, which is the natural precursor of bilirubin. These electrodes exhibit full orientation of the enzyme, as confirmed by the observable non‐catalytic redox system corresponding to the T1 copper center associated with pure Nernstian electrocatalytic behavior with high catalytic currents of almost 5 mA cm−2 at neutral pH.
Facing the right way: Bilirubin oxidase from Myrothecium verrucaria can be efficiently immobilized and oriented on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter (see figure). |
| doi_str_mv | 10.1002/chem.201502377 |
| format | Article |
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Facing the right way: Bilirubin oxidase from Myrothecium verrucaria can be efficiently immobilized and oriented on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter (see figure).</description><subject>Biocatalysis</subject><subject>carbon nanotubes</subject><subject>Chemical Sciences</subject><subject>Chemistry</subject><subject>Copper - chemistry</subject><subject>electrochemistry</subject><subject>Electrodes</subject><subject>Electron Transport</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immobilization</subject><subject>Multi wall carbon nanotubes</subject><subject>Nanotubes</subject><subject>Nanotubes, Carbon - chemistry</subject><subject>Orientation</subject><subject>Oxidase</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases Acting on CH-CH Group Donors - chemistry</subject><subject>Oxidoreductases Acting on CH-CH Group Donors - metabolism</subject><subject>oxygen reduction</subject><subject>porphyrinoids</subject><subject>Porphyrins</subject><subject>Porphyrins - chemistry</subject><subject>Precursors</subject><issn>0947-6539</issn><issn>1521-3765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1v0zAchiMEYmVw5YgicYFDys9xbNfHrWpXRFknxNfNcmyHerhxsZNtQeJ_x123CnGBk7-e97HlN8ueIxgjgPKNWpvNuAREoMSMPchGiJSowIySh9kIeMUKSjA_yp7EeAkAnGL8ODsqaVWlKRllv-a9c0O-Cta0ndH5qXU29LVt89WN1TKa3Lf5hQ_b9RBsW8z7VnXWt9LZn4meylCn83PZ-q6vTT5zRnXBaxPzxof7pZKddENnVXIO30ybfzC6v9U8zR410kXz7G48zj7NZx-ni2K5Ons7PVkWihLEilpyXgMBUkHZaIawBIUlBa0xIGwYU1ArhmqGja6aCaWorrjWDaeNwQbV-Dh7vfeupRPbYDcyDMJLKxYnS7HbA5QugopdocS-2rPb4H_0JnZiY6MyzsnW-D4KxCYUTaAs-X-gGDGeAiShL_9CL30f0j_eUkARMEITNd5TKvgYg2kOj0Ugdn2LXd_i0HcKvLjT9vXG6AN-X3AC-B64ts4M_9CJ6WL2_k95sc_a2JmbQ1aG74IyzIj4cn4mLih85e-WC_EZ_wY8jcZ_</recordid><startdate>20151116</startdate><enddate>20151116</enddate><creator>Lalaoui, Noémie</creator><creator>Le Goff, Alan</creator><creator>Holzinger, Michael</creator><creator>Cosnier, Serge</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><general>Wiley-VCH Verlag</general><scope>BSCLL</scope><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>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>K9.</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-6765-5859</orcidid><orcidid>https://orcid.org/0000-0002-1313-2876</orcidid><orcidid>https://orcid.org/0000-0003-3700-4673</orcidid><orcidid>https://orcid.org/0000-0002-8290-4374</orcidid></search><sort><creationdate>20151116</creationdate><title>Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction</title><author>Lalaoui, Noémie ; Le Goff, Alan ; Holzinger, Michael ; Cosnier, Serge</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6517-ba99b0505402fd713a0c3a60dd3013e77c0bc71b73ed4f8661b49ddf96fe3e1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Biocatalysis</topic><topic>carbon nanotubes</topic><topic>Chemical Sciences</topic><topic>Chemistry</topic><topic>Copper - chemistry</topic><topic>electrochemistry</topic><topic>Electrodes</topic><topic>Electron Transport</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immobilization</topic><topic>Multi wall carbon nanotubes</topic><topic>Nanotubes</topic><topic>Nanotubes, Carbon - chemistry</topic><topic>Orientation</topic><topic>Oxidase</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases Acting on CH-CH Group Donors - chemistry</topic><topic>Oxidoreductases Acting on CH-CH Group Donors - metabolism</topic><topic>oxygen reduction</topic><topic>porphyrinoids</topic><topic>Porphyrins</topic><topic>Porphyrins - chemistry</topic><topic>Precursors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lalaoui, Noémie</creatorcontrib><creatorcontrib>Le Goff, Alan</creatorcontrib><creatorcontrib>Holzinger, Michael</creatorcontrib><creatorcontrib>Cosnier, Serge</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Chemistry : a European journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lalaoui, Noémie</au><au>Le Goff, Alan</au><au>Holzinger, Michael</au><au>Cosnier, Serge</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction</atitle><jtitle>Chemistry : a European journal</jtitle><addtitle>Chem. Eur. J</addtitle><date>2015-11-16</date><risdate>2015</risdate><volume>21</volume><issue>47</issue><spage>16868</spage><epage>16873</epage><pages>16868-16873</pages><issn>0947-6539</issn><eissn>1521-3765</eissn><coden>CEUJED</coden><abstract>The efficient immobilization and orientation of bilirubin oxidase from Myrothecium verrucaria on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter is reported. By comparing the use of different types of porphyrin, the rational effect of the porphyrin structure on both the immobilization and orientation of the enzyme is demonstrated. The best performances were obtained for protoporphyrin IX, which is the natural precursor of bilirubin. These electrodes exhibit full orientation of the enzyme, as confirmed by the observable non‐catalytic redox system corresponding to the T1 copper center associated with pure Nernstian electrocatalytic behavior with high catalytic currents of almost 5 mA cm−2 at neutral pH.
Facing the right way: Bilirubin oxidase from Myrothecium verrucaria can be efficiently immobilized and oriented on multi‐walled carbon nanotube electrodes by using π‐stacked porphyrins as a direct electron‐transfer promoter (see figure).</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>26449635</pmid><doi>10.1002/chem.201502377</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-6765-5859</orcidid><orcidid>https://orcid.org/0000-0002-1313-2876</orcidid><orcidid>https://orcid.org/0000-0003-3700-4673</orcidid><orcidid>https://orcid.org/0000-0002-8290-4374</orcidid></addata></record> |
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| subjects | Biocatalysis carbon nanotubes Chemical Sciences Chemistry Copper - chemistry electrochemistry Electrodes Electron Transport Enzymes Enzymes, Immobilized - chemistry Hydrogen-Ion Concentration Immobilization Multi wall carbon nanotubes Nanotubes Nanotubes, Carbon - chemistry Orientation Oxidase Oxidation-Reduction Oxidoreductases Acting on CH-CH Group Donors - chemistry Oxidoreductases Acting on CH-CH Group Donors - metabolism oxygen reduction porphyrinoids Porphyrins Porphyrins - chemistry Precursors |
| title | Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction |
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