Coupling of pyrroloquinoline quinone dependent glucose dehydrogenase to (cytochrome c/DNA)-multilayer systems on electrodes
The redox protein cytochrome c (cyt c) assembles into electro-active multilayers on gold electrodes by the help of deoxyribonucleic acid (DNA) as a negatively-charged building block. The feasibility of this electro-active system as a novel interface for the immobilization of enzymes on electrodes is...
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Veröffentlicht in: | Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2012-12, Vol.88, p.97-102 |
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description | The redox protein cytochrome c (cyt c) assembles into electro-active multilayers on gold electrodes by the help of deoxyribonucleic acid (DNA) as a negatively-charged building block. The feasibility of this electro-active system as a novel interface for the immobilization of enzymes on electrodes is investigated in this study. Therefore the known reaction of cyt c and PQQ-GDH is confined to the immobilized state of both molecules. We find that electron-transfer from the substrate via PQQ-GDH and cyt c molecules, towards the electrode occurs; thus the system can be considered as an artificial signal chain.
First, a monolayer of cyt c is prepared on a thiol-modified gold electrode and investigated with PQQ-GDH in solution. Cyclic voltammetric measurements prove that a small catalytic current occurs in the presence of the substrate. Next, both proteins are immobilized. We use the layer-by-layer deposition technique to assemble cyt c with DNA in multiple layers and a terminal layer of PQQ-GDH: (cyt c/DNA)n/PQQ-GDH. It is found that a catalytic current flows when glucose is present, proving that this system relies on inter-protein electron-transfer. The current intensity can be increased from 0.1nA, at the monolayer system, up to 3.7nA, at the (cyt c/DNA)4/PQQ-GDH electrode. This bi-protein multilayer system can follow different glucose concentrations in a linear dynamic range between 25nM and 0.5μM at its pH optimum, i.e. pH 6. Therefore this system is of limited importance for sensing but it represents a new biomimetic signal chain by arranging proteins in multiple layers on electrodes, making direct electron exchange feasible.
► Novel electro-active interface for the immobilization of enzymes is created. ► Direct electron exchange between PQQ-GDH and cyt c is achieved in immobilized state. ► Biomimetic signal chain from glucose via PQQ-GDH and cyt c is established. ► Sensitivity of the system is tunable to a certain extent by the number of layers. |
doi_str_mv | 10.1016/j.bioelechem.2012.06.003 |
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First, a monolayer of cyt c is prepared on a thiol-modified gold electrode and investigated with PQQ-GDH in solution. Cyclic voltammetric measurements prove that a small catalytic current occurs in the presence of the substrate. Next, both proteins are immobilized. We use the layer-by-layer deposition technique to assemble cyt c with DNA in multiple layers and a terminal layer of PQQ-GDH: (cyt c/DNA)n/PQQ-GDH. It is found that a catalytic current flows when glucose is present, proving that this system relies on inter-protein electron-transfer. The current intensity can be increased from 0.1nA, at the monolayer system, up to 3.7nA, at the (cyt c/DNA)4/PQQ-GDH electrode. This bi-protein multilayer system can follow different glucose concentrations in a linear dynamic range between 25nM and 0.5μM at its pH optimum, i.e. pH 6. Therefore this system is of limited importance for sensing but it represents a new biomimetic signal chain by arranging proteins in multiple layers on electrodes, making direct electron exchange feasible.
► Novel electro-active interface for the immobilization of enzymes is created. ► Direct electron exchange between PQQ-GDH and cyt c is achieved in immobilized state. ► Biomimetic signal chain from glucose via PQQ-GDH and cyt c is established. ► Sensitivity of the system is tunable to a certain extent by the number of layers.</description><identifier>ISSN: 1567-5394</identifier><identifier>EISSN: 1878-562X</identifier><identifier>DOI: 10.1016/j.bioelechem.2012.06.003</identifier><identifier>PMID: 22814119</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Acinetobacter calcoaceticus - enzymology ; Animals ; Cattle ; Cytochrome c ; Cytochromes c - chemistry ; Cytochromes c - metabolism ; DNA ; DNA - chemistry ; DNA - metabolism ; Electrochemistry ; Electrodes ; Electron Transport ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Glucose - analysis ; Glucose - chemistry ; Glucose 1-Dehydrogenase - chemistry ; Glucose 1-Dehydrogenase - metabolism ; Mediated electron transfer ; Models, Molecular ; Multilayer ; Nucleic Acid Conformation ; PQQ Cofactor - chemistry ; PQQ Cofactor - metabolism ; PQQ-GDH ; Protein Conformation</subject><ispartof>Bioelectrochemistry (Amsterdam, Netherlands), 2012-12, Vol.88, p.97-102</ispartof><rights>2012 Elsevier B.V.</rights><rights>Copyright © 2012 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1567539412000874$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22814119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wettstein, Ch</creatorcontrib><creatorcontrib>Möhwald, H.</creatorcontrib><creatorcontrib>Lisdat, F.</creatorcontrib><title>Coupling of pyrroloquinoline quinone dependent glucose dehydrogenase to (cytochrome c/DNA)-multilayer systems on electrodes</title><title>Bioelectrochemistry (Amsterdam, Netherlands)</title><addtitle>Bioelectrochemistry</addtitle><description>The redox protein cytochrome c (cyt c) assembles into electro-active multilayers on gold electrodes by the help of deoxyribonucleic acid (DNA) as a negatively-charged building block. The feasibility of this electro-active system as a novel interface for the immobilization of enzymes on electrodes is investigated in this study. Therefore the known reaction of cyt c and PQQ-GDH is confined to the immobilized state of both molecules. We find that electron-transfer from the substrate via PQQ-GDH and cyt c molecules, towards the electrode occurs; thus the system can be considered as an artificial signal chain.
First, a monolayer of cyt c is prepared on a thiol-modified gold electrode and investigated with PQQ-GDH in solution. Cyclic voltammetric measurements prove that a small catalytic current occurs in the presence of the substrate. Next, both proteins are immobilized. We use the layer-by-layer deposition technique to assemble cyt c with DNA in multiple layers and a terminal layer of PQQ-GDH: (cyt c/DNA)n/PQQ-GDH. It is found that a catalytic current flows when glucose is present, proving that this system relies on inter-protein electron-transfer. The current intensity can be increased from 0.1nA, at the monolayer system, up to 3.7nA, at the (cyt c/DNA)4/PQQ-GDH electrode. This bi-protein multilayer system can follow different glucose concentrations in a linear dynamic range between 25nM and 0.5μM at its pH optimum, i.e. pH 6. Therefore this system is of limited importance for sensing but it represents a new biomimetic signal chain by arranging proteins in multiple layers on electrodes, making direct electron exchange feasible.
► Novel electro-active interface for the immobilization of enzymes is created. ► Direct electron exchange between PQQ-GDH and cyt c is achieved in immobilized state. ► Biomimetic signal chain from glucose via PQQ-GDH and cyt c is established. ► Sensitivity of the system is tunable to a certain extent by the number of layers.</description><subject>Acinetobacter calcoaceticus - enzymology</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cytochrome c</subject><subject>Cytochromes c - chemistry</subject><subject>Cytochromes c - metabolism</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>Electrochemistry</subject><subject>Electrodes</subject><subject>Electron Transport</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Glucose - analysis</subject><subject>Glucose - chemistry</subject><subject>Glucose 1-Dehydrogenase - chemistry</subject><subject>Glucose 1-Dehydrogenase - metabolism</subject><subject>Mediated electron transfer</subject><subject>Models, Molecular</subject><subject>Multilayer</subject><subject>Nucleic Acid Conformation</subject><subject>PQQ Cofactor - chemistry</subject><subject>PQQ Cofactor - metabolism</subject><subject>PQQ-GDH</subject><subject>Protein Conformation</subject><issn>1567-5394</issn><issn>1878-562X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS1ERUvhLyAvyyKpH7GdLMuUl1S1myKxs-z4ZsYjJw52ghTx5_HQIpas7kOfru45ByFMSU0JldfH2voIAfoDjDUjlNVE1oTwF-iCtqqthGTfX5ZeSFUJ3jXn6HXOR0JIS5V4hc4Za2lDaXeBfu3iOgc_7XEc8LylFEP8sfoplh3gP12pDmaYHEwL3oe1j_m0OWwuxT1MpkxLxFf9tsT-kOIIuL--vb95X41rWHwwGySct7zAmHGc8OntJUUH-Q06G0zI8Pa5XqJvnz4-7r5Udw-fv-5u7irghC-VE9RQA5KJZhisVMayvqNMArcdt04IZwbSyKYdhLACmo4rKzs5DNwyYdTAL9HV0905FW2QFz363EMIZoK4Zk0FIUqqYsn_UdKSthVUsYK-e0ZXO4LTc_KjSZv-620BPjwBULT99JB07j1MPTifigXaRV_u6VOg-qj_BapPgWoidQmU_wbYY5h5</recordid><startdate>201212</startdate><enddate>201212</enddate><creator>Wettstein, Ch</creator><creator>Möhwald, H.</creator><creator>Lisdat, F.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>7QO</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>201212</creationdate><title>Coupling of pyrroloquinoline quinone dependent glucose dehydrogenase to (cytochrome c/DNA)-multilayer systems on electrodes</title><author>Wettstein, Ch ; Möhwald, H. ; Lisdat, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e303t-d51a1ae6254ffb67ab2c9126e3b93bd55daf04648f55b5e4937b696ff3b25a7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Acinetobacter calcoaceticus - enzymology</topic><topic>Animals</topic><topic>Cattle</topic><topic>Cytochrome c</topic><topic>Cytochromes c - chemistry</topic><topic>Cytochromes c - metabolism</topic><topic>DNA</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>Electrochemistry</topic><topic>Electrodes</topic><topic>Electron Transport</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Glucose - analysis</topic><topic>Glucose - chemistry</topic><topic>Glucose 1-Dehydrogenase - chemistry</topic><topic>Glucose 1-Dehydrogenase - metabolism</topic><topic>Mediated electron transfer</topic><topic>Models, Molecular</topic><topic>Multilayer</topic><topic>Nucleic Acid Conformation</topic><topic>PQQ Cofactor - chemistry</topic><topic>PQQ Cofactor - metabolism</topic><topic>PQQ-GDH</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wettstein, Ch</creatorcontrib><creatorcontrib>Möhwald, H.</creatorcontrib><creatorcontrib>Lisdat, F.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Bioelectrochemistry (Amsterdam, Netherlands)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wettstein, Ch</au><au>Möhwald, H.</au><au>Lisdat, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Coupling of pyrroloquinoline quinone dependent glucose dehydrogenase to (cytochrome c/DNA)-multilayer systems on electrodes</atitle><jtitle>Bioelectrochemistry (Amsterdam, Netherlands)</jtitle><addtitle>Bioelectrochemistry</addtitle><date>2012-12</date><risdate>2012</risdate><volume>88</volume><spage>97</spage><epage>102</epage><pages>97-102</pages><issn>1567-5394</issn><eissn>1878-562X</eissn><abstract>The redox protein cytochrome c (cyt c) assembles into electro-active multilayers on gold electrodes by the help of deoxyribonucleic acid (DNA) as a negatively-charged building block. The feasibility of this electro-active system as a novel interface for the immobilization of enzymes on electrodes is investigated in this study. Therefore the known reaction of cyt c and PQQ-GDH is confined to the immobilized state of both molecules. We find that electron-transfer from the substrate via PQQ-GDH and cyt c molecules, towards the electrode occurs; thus the system can be considered as an artificial signal chain.
First, a monolayer of cyt c is prepared on a thiol-modified gold electrode and investigated with PQQ-GDH in solution. Cyclic voltammetric measurements prove that a small catalytic current occurs in the presence of the substrate. Next, both proteins are immobilized. We use the layer-by-layer deposition technique to assemble cyt c with DNA in multiple layers and a terminal layer of PQQ-GDH: (cyt c/DNA)n/PQQ-GDH. It is found that a catalytic current flows when glucose is present, proving that this system relies on inter-protein electron-transfer. The current intensity can be increased from 0.1nA, at the monolayer system, up to 3.7nA, at the (cyt c/DNA)4/PQQ-GDH electrode. This bi-protein multilayer system can follow different glucose concentrations in a linear dynamic range between 25nM and 0.5μM at its pH optimum, i.e. pH 6. Therefore this system is of limited importance for sensing but it represents a new biomimetic signal chain by arranging proteins in multiple layers on electrodes, making direct electron exchange feasible.
► Novel electro-active interface for the immobilization of enzymes is created. ► Direct electron exchange between PQQ-GDH and cyt c is achieved in immobilized state. ► Biomimetic signal chain from glucose via PQQ-GDH and cyt c is established. ► Sensitivity of the system is tunable to a certain extent by the number of layers.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>22814119</pmid><doi>10.1016/j.bioelechem.2012.06.003</doi><tpages>6</tpages></addata></record> |
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subjects | Acinetobacter calcoaceticus - enzymology Animals Cattle Cytochrome c Cytochromes c - chemistry Cytochromes c - metabolism DNA DNA - chemistry DNA - metabolism Electrochemistry Electrodes Electron Transport Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Glucose - analysis Glucose - chemistry Glucose 1-Dehydrogenase - chemistry Glucose 1-Dehydrogenase - metabolism Mediated electron transfer Models, Molecular Multilayer Nucleic Acid Conformation PQQ Cofactor - chemistry PQQ Cofactor - metabolism PQQ-GDH Protein Conformation |
title | Coupling of pyrroloquinoline quinone dependent glucose dehydrogenase to (cytochrome c/DNA)-multilayer systems on electrodes |
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