Electrodeposited nanoscale zinc oxide particles: facilitating the electron transfer of immobilised protein and biosensing
The electron transfer of redox-active sites of immobilised haemoglobin (Hb) has been studied by voltammetric experiments. The electrode surface was modified by nanoparticles (NPs) to make a suitable substrate for electric wiring of protein molecules and efficient electron transferring. Hence, the Hb...
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| Veröffentlicht in: | Micro & nano letters 2017-07, Vol.12 (7), p.425-429 |
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| creator | Bayandori Moghaddam, Abdolmajid |
| description | The electron transfer of redox-active sites of immobilised haemoglobin (Hb) has been studied by voltammetric experiments. The electrode surface was modified by nanoparticles (NPs) to make a suitable substrate for electric wiring of protein molecules and efficient electron transferring. Hence, the Hb/zinc oxide NPs/platinum electrode was prepared by chronoamperometric deposition of the NPs and immobilisation of protein molecules. The electrochemical behaviour of the prepared biosensor was quasi-reversible and showed a pair of redox peaks with a formal potential (E0′) of 214 mV. Additionally, the electron transfer rate constant (ks) of immobilised Hb was about 0.621 s−1. Biocatalytic reduction of hydrogen peroxide was also examined on the prepared biosensor. Result indicated to good sensitivity, wide linear range and low detection limit of 6 μM. |
| doi_str_mv | 10.1049/mnl.2016.0563 |
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The electrode surface was modified by nanoparticles (NPs) to make a suitable substrate for electric wiring of protein molecules and efficient electron transferring. Hence, the Hb/zinc oxide NPs/platinum electrode was prepared by chronoamperometric deposition of the NPs and immobilisation of protein molecules. The electrochemical behaviour of the prepared biosensor was quasi-reversible and showed a pair of redox peaks with a formal potential (E0′) of 214 mV. Additionally, the electron transfer rate constant (ks) of immobilised Hb was about 0.621 s−1. Biocatalytic reduction of hydrogen peroxide was also examined on the prepared biosensor. Result indicated to good sensitivity, wide linear range and low detection limit of 6 μM.</description><identifier>ISSN: 1750-0443</identifier><identifier>EISSN: 1750-0443</identifier><identifier>DOI: 10.1049/mnl.2016.0563</identifier><language>eng</language><publisher>Stevenage: The Institution of Engineering and Technology</publisher><subject>biocatalytic reduction ; biochemistry ; biosensor ; Biosensors ; catalysis ; charge exchange ; chemical variables measurement ; chronoamperometric deposition ; detection limit ; electric wiring ; Electrochemical analysis ; electrochemical electrodes ; electrochemical sensors ; electrode surface ; electrodeposition ; Electrodes ; Electron transfer ; electron transfer rate constant ; Electrons ; H2O2 ; Hemoglobin ; hydrogen compounds ; Hydrogen peroxide ; II‐VI semiconductors ; immobilised haemoglobin ; molecular biophysics ; nanofabrication ; Nanoparticles ; nanoscale zinc oxide particles ; nanosensors ; oxidation ; Platinum ; protein molecule immobilisation ; Proteins ; quasireversible electrochemical behaviour ; reaction rate constants ; redox‐active sites ; reduction (chemical) ; semiconductor growth ; Substrates ; voltage 214 mV ; voltammetry ; voltammetry (chemical analysis) ; wide band gap semiconductors ; Wiring ; zinc compounds ; Zinc oxide ; Zinc oxides ; Zinc plating ; ZnO‐Pt</subject><ispartof>Micro & nano letters, 2017-07, Vol.12 (7), p.425-429</ispartof><rights>The Institution of Engineering and Technology</rights><rights>2017 The Institution of Engineering and Technology</rights><rights>Copyright The Institution of Engineering & Technology Jul 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3763-424fad22da323989535ae3a59750c965c9d507c5f1d2120535de789e316f67b03</citedby><cites>FETCH-LOGICAL-c3763-424fad22da323989535ae3a59750c965c9d507c5f1d2120535de789e316f67b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1049%2Fmnl.2016.0563$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1049%2Fmnl.2016.0563$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,11566,27928,27929,45578,45579,46056,46480</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1049%2Fmnl.2016.0563$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc></links><search><creatorcontrib>Bayandori Moghaddam, Abdolmajid</creatorcontrib><title>Electrodeposited nanoscale zinc oxide particles: facilitating the electron transfer of immobilised protein and biosensing</title><title>Micro & nano letters</title><description>The electron transfer of redox-active sites of immobilised haemoglobin (Hb) has been studied by voltammetric experiments. The electrode surface was modified by nanoparticles (NPs) to make a suitable substrate for electric wiring of protein molecules and efficient electron transferring. Hence, the Hb/zinc oxide NPs/platinum electrode was prepared by chronoamperometric deposition of the NPs and immobilisation of protein molecules. The electrochemical behaviour of the prepared biosensor was quasi-reversible and showed a pair of redox peaks with a formal potential (E0′) of 214 mV. Additionally, the electron transfer rate constant (ks) of immobilised Hb was about 0.621 s−1. Biocatalytic reduction of hydrogen peroxide was also examined on the prepared biosensor. Result indicated to good sensitivity, wide linear range and low detection limit of 6 μM.</description><subject>biocatalytic reduction</subject><subject>biochemistry</subject><subject>biosensor</subject><subject>Biosensors</subject><subject>catalysis</subject><subject>charge exchange</subject><subject>chemical variables measurement</subject><subject>chronoamperometric deposition</subject><subject>detection limit</subject><subject>electric wiring</subject><subject>Electrochemical analysis</subject><subject>electrochemical electrodes</subject><subject>electrochemical sensors</subject><subject>electrode surface</subject><subject>electrodeposition</subject><subject>Electrodes</subject><subject>Electron transfer</subject><subject>electron transfer rate constant</subject><subject>Electrons</subject><subject>H2O2</subject><subject>Hemoglobin</subject><subject>hydrogen compounds</subject><subject>Hydrogen peroxide</subject><subject>II‐VI semiconductors</subject><subject>immobilised haemoglobin</subject><subject>molecular biophysics</subject><subject>nanofabrication</subject><subject>Nanoparticles</subject><subject>nanoscale zinc oxide particles</subject><subject>nanosensors</subject><subject>oxidation</subject><subject>Platinum</subject><subject>protein molecule immobilisation</subject><subject>Proteins</subject><subject>quasireversible electrochemical behaviour</subject><subject>reaction rate constants</subject><subject>redox‐active sites</subject><subject>reduction (chemical)</subject><subject>semiconductor growth</subject><subject>Substrates</subject><subject>voltage 214 mV</subject><subject>voltammetry</subject><subject>voltammetry (chemical analysis)</subject><subject>wide band gap semiconductors</subject><subject>Wiring</subject><subject>zinc compounds</subject><subject>Zinc oxide</subject><subject>Zinc oxides</subject><subject>Zinc plating</subject><subject>ZnO‐Pt</subject><issn>1750-0443</issn><issn>1750-0443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp9kM1PGzEQxVeoSKTAkbulqoceNvXHejfujSJCK4VwgbPl2OPW0a692I5o-tfjaHvIgXIaS_N7b55fVV0RPCe4EV8H388pJu0c85adVDPScVzjpmEfjt5n1ceUthg3He3ErNrf9qBzDAbGkFwGg7zyIWnVA_rrvEbhjzOARhWz0z2kb8gq7XqXVXb-F8q_AcHk4FGOyicLEQWL3DCETeFScRxjyOA8Ut6gjQsJfCrai-rUqj7B5b95Xj0tbx9vftSrh7ufN9erWrOuZXVDG6sMpUYxysRCcMYVMMVF-ZAWLdfCcNxpbomhhOKyNtAtBDDS2rbbYHZefZp8S4znHaQst2EXfTkpiRC44VjQRaHqidIxpBTByjG6QcW9JFge2pWlXXloVx7aLXw78S-uh_37sLxfX9PvS0xKuiL8MgkdHCf5z5HPb7D369WR92gsewXx4JjP</recordid><startdate>201707</startdate><enddate>201707</enddate><creator>Bayandori Moghaddam, Abdolmajid</creator><general>The Institution of Engineering and Technology</general><general>John Wiley & Sons, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7TB</scope><scope>7U5</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>L7M</scope></search><sort><creationdate>201707</creationdate><title>Electrodeposited nanoscale zinc oxide particles: facilitating the electron transfer of immobilised protein and biosensing</title><author>Bayandori Moghaddam, Abdolmajid</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3763-424fad22da323989535ae3a59750c965c9d507c5f1d2120535de789e316f67b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>biocatalytic reduction</topic><topic>biochemistry</topic><topic>biosensor</topic><topic>Biosensors</topic><topic>catalysis</topic><topic>charge exchange</topic><topic>chemical variables measurement</topic><topic>chronoamperometric deposition</topic><topic>detection limit</topic><topic>electric wiring</topic><topic>Electrochemical analysis</topic><topic>electrochemical electrodes</topic><topic>electrochemical sensors</topic><topic>electrode surface</topic><topic>electrodeposition</topic><topic>Electrodes</topic><topic>Electron transfer</topic><topic>electron transfer rate constant</topic><topic>Electrons</topic><topic>H2O2</topic><topic>Hemoglobin</topic><topic>hydrogen compounds</topic><topic>Hydrogen peroxide</topic><topic>II‐VI semiconductors</topic><topic>immobilised haemoglobin</topic><topic>molecular biophysics</topic><topic>nanofabrication</topic><topic>Nanoparticles</topic><topic>nanoscale zinc oxide particles</topic><topic>nanosensors</topic><topic>oxidation</topic><topic>Platinum</topic><topic>protein molecule immobilisation</topic><topic>Proteins</topic><topic>quasireversible electrochemical behaviour</topic><topic>reaction rate constants</topic><topic>redox‐active sites</topic><topic>reduction (chemical)</topic><topic>semiconductor growth</topic><topic>Substrates</topic><topic>voltage 214 mV</topic><topic>voltammetry</topic><topic>voltammetry (chemical analysis)</topic><topic>wide band gap semiconductors</topic><topic>Wiring</topic><topic>zinc compounds</topic><topic>Zinc oxide</topic><topic>Zinc oxides</topic><topic>Zinc plating</topic><topic>ZnO‐Pt</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bayandori Moghaddam, Abdolmajid</creatorcontrib><collection>CrossRef</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Micro & nano letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Bayandori Moghaddam, Abdolmajid</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electrodeposited nanoscale zinc oxide particles: facilitating the electron transfer of immobilised protein and biosensing</atitle><jtitle>Micro & nano letters</jtitle><date>2017-07</date><risdate>2017</risdate><volume>12</volume><issue>7</issue><spage>425</spage><epage>429</epage><pages>425-429</pages><issn>1750-0443</issn><eissn>1750-0443</eissn><abstract>The electron transfer of redox-active sites of immobilised haemoglobin (Hb) has been studied by voltammetric experiments. The electrode surface was modified by nanoparticles (NPs) to make a suitable substrate for electric wiring of protein molecules and efficient electron transferring. Hence, the Hb/zinc oxide NPs/platinum electrode was prepared by chronoamperometric deposition of the NPs and immobilisation of protein molecules. The electrochemical behaviour of the prepared biosensor was quasi-reversible and showed a pair of redox peaks with a formal potential (E0′) of 214 mV. Additionally, the electron transfer rate constant (ks) of immobilised Hb was about 0.621 s−1. Biocatalytic reduction of hydrogen peroxide was also examined on the prepared biosensor. Result indicated to good sensitivity, wide linear range and low detection limit of 6 μM.</abstract><cop>Stevenage</cop><pub>The Institution of Engineering and Technology</pub><doi>10.1049/mnl.2016.0563</doi><tpages>5</tpages></addata></record> |
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| subjects | biocatalytic reduction biochemistry biosensor Biosensors catalysis charge exchange chemical variables measurement chronoamperometric deposition detection limit electric wiring Electrochemical analysis electrochemical electrodes electrochemical sensors electrode surface electrodeposition Electrodes Electron transfer electron transfer rate constant Electrons H2O2 Hemoglobin hydrogen compounds Hydrogen peroxide II‐VI semiconductors immobilised haemoglobin molecular biophysics nanofabrication Nanoparticles nanoscale zinc oxide particles nanosensors oxidation Platinum protein molecule immobilisation Proteins quasireversible electrochemical behaviour reaction rate constants redox‐active sites reduction (chemical) semiconductor growth Substrates voltage 214 mV voltammetry voltammetry (chemical analysis) wide band gap semiconductors Wiring zinc compounds Zinc oxide Zinc oxides Zinc plating ZnO‐Pt |
| title | Electrodeposited nanoscale zinc oxide particles: facilitating the electron transfer of immobilised protein and biosensing |
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