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  <doc>
    <id>1390</id>
    <completedYear>2019</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>4533</pageFirst>
    <pageLast>4540</pageLast>
    <pageNumber/>
    <edition/>
    <issue>17</issue>
    <volume>6</volume>
    <type>article</type>
    <publisherName>Wiley</publisherName>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Electrochemical Activity Determination of Catechol-O-methyl Transferase by Selective Dopamine Detection</title>
    <abstract language="eng">For the treatment of Parkinson's disease, as one of the most frequent diseases of the central nervous system, several key enzymes for dopamine metabolism [e. g. catechol-O-methyl transferase (COMT)] are drug targets. For an efficient and long-lasting treatment, the activity of this enzyme should be monitored. In this study, an electrochemical approach using differential pulse voltammetry (DPV) is introduced for the activity determination. The applied electrode material, fluorine-doped tin oxide (FTO), is characterized by a clear discrimination between substrate and product of COMT, a high stability of the dopamine signal during consecutive measurements, and a linear dependency on the dopamine concentration in the range of the maximum reaction rate of COMT. Despite these advantageous results, dopamine detection in the complete activity assay is influenced by each of the added essential assay components, even though none of the added components reveal a current signal at the FTO electrode itself. After adjusting the potential range and the assay composition, these effects can be circumvented. By following the dopamine concentrations during COMT action, it can be shown that the activity of COMT can be detected by using differential pulse voltammetry (DPV) at an FTO electrode and, by analyzing different COMT amounts, quantification can be demonstrated.</abstract>
    <parentTitle language="eng">ChemElectroChem</parentTitle>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-13900</identifier>
    <enrichment key="opus.import.date">2021-04-07T08:20:21+00:00</enrichment>
    <enrichment key="opus.source">sword</enrichment>
    <enrichment key="opus.import.user">sword</enrichment>
    <enrichment key="opus.import.file">filename=phpOrq1vv</enrichment>
    <enrichment key="opus.import.checksum">b1a5d427c690597d93daf1cd17822d4d</enrichment>
    <enrichment key="SourceTitle">G. Göbel, A. Talke, U. Ahnert, F. Lisdat, ChemElectroChem 2019, 6, 4533.</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1002/celc.201900856</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 4.0 International</licence>
    <author>Gero Göbel</author>
    <author>Anja Talke</author>
    <author>Uwe Ahnert</author>
    <author>Fred Lisdat</author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>catechol-O-methyl transferase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>dopamine</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>flow system</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>fluorine-doped tin oxide</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>sensing</value>
    </subject>
    <collection role="ddc" number="541">Physikalische Chemie</collection>
    <collection role="institutes" number="">Fachbereich Ingenieur- und Naturwissenschaften</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="Import" number="import">Import</collection>
    <collection role="Funding" number="">Projekt DEAL</collection>
    <collection role="green_open_access" number="4">Hybrid Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/1390/celc.201900856.pdf</file>
  </doc>
  <doc>
    <id>580</id>
    <completedYear>2011</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber>10</pageNumber>
    <edition/>
    <issue>46</issue>
    <volume>9</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>2016-06-16</completedDate>
    <publishedDate>2011-10-07</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode</title>
    <abstract language="eng">An electrochemical sensor for p-aminophenyl phosphate (p APP) is reported. It is based on the electrochemical conversion of 4-aminophenol (4AP) at a quantum dot (QD) modified electrode under illumination. Without illumination no electron transfer and thus no oxidation of 4AP can occur. p APP as substrate is converted by the enzyme alkaline phosphatase (ALP) to generate 4AP as a product. The QDs are coupled via 1,4-benzenedithiol (BDT) linkage to the surface of a gold electrode and thus allow potential-controlled photocurrent generation. The photocurrent is modified by the enzyme reaction providing access to the substrate detection. In order to develop a photobioelectrochemical sensor the enzyme is immobilized on top of the photo-switchable layer of the QDs. Immobilization of ALP is required for the potential possibility of spatially resolved measurements. Geometries with immobilized ALP are compared versus having the ALP in solution. Data indicate that functional immobilization with layer-by-layer assembly is possible. Enzymatic activity of ALP and thus the photocurrent can be described by Michaelis- Menten kinetics. p APP is detected as proof of principle investigation within the range of 25 μM - 1 mM.</abstract>
    <parentTitle language="eng">Journal of Nanobiotechnology</parentTitle>
    <identifier type="issn">1477-3155</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-5808</identifier>
    <enrichment key="SourceTitle">Khalid, W., Göbel, G., Hühn, D. et al. Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode. J Nanobiotechnol 9, 46 (2011). https://doi.org/10.1186/1477-3155-9-46</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1186/1477-3155-9-46</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 2.0 Generic</licence>
    <author>Waqas Khalid</author>
    <author>Gero Göbel</author>
    <author>Dominik Hühn</author>
    <author>Jose-Maria Montenegro</author>
    <author>Pilar Rivera-Gil</author>
    <author>Fred Lisdat</author>
    <author>Wolfgang J. Parak</author>
    <collection role="ddc" number="660">Chemische Verfahrenstechnik</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="green_open_access" number="1">Gold Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/580/2F1477-3155-9-46.pdf</file>
  </doc>
  <doc>
    <id>623</id>
    <completedYear>2009</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>273</pageFirst>
    <pageLast>276</pageLast>
    <pageNumber/>
    <edition/>
    <issue>1</issue>
    <volume>1</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Biosensor based on an oxygen reducing bilirubin oxidase electrode</title>
    <abstract language="eng">An oxygen reducing electrode made of bilirubin oxidase and multi-walled carbon nanotubes (BOD-MWCNT-Au electrode) is coupled to enzymes catalysing oxygen-consuming reactions such as glucose oxidase (GOD) to result in a membrane-free bienzyme electrode. The feasibility of such a molecularly assembled system stabilized by covalent linkage has been demonstrated. The electrochemical characterisation of the bienzyme electrode reveals sensitivity to the enzyme substrate. The results indicate that the BOD-electrode provides a suitable platform for sensing analytes for which oxidases of high activity are available.</abstract>
    <parentTitle language="eng">Procedia Chemistry</parentTitle>
    <identifier type="issn">1876-6196</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-6237</identifier>
    <enrichment key="SourceTitle">G. Göbel et al. Biosensor based on an oxygen reducing bilirubin oxidase electrode. Procedia Chemistry 1 (2009) 273–276.</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1016/j.proche.2009.07.068</enrichment>
    <licence>Creative Commons - CC BY-NC-ND 3.0 - Namensnennung - Nicht-kommerziell - Keine Bearbeitung 3.0 Unported</licence>
    <author>Gero Göbel</author>
    <author>T. Dietz</author>
    <author>Fred Lisdat</author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>bienzyme sensor</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>bilirubin oxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>carbon nanotube</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>membran-free</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>mediator-less</value>
    </subject>
    <collection role="ddc" number="540">Chemie und zugeordnete Wissenschaften</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="green_open_access" number="1">Gold Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/623/1-s2.0-S1876619609000692-main.pdf</file>
  </doc>
  <doc>
    <id>1929</id>
    <completedYear>2024</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>160</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Qualitative and quantitative protease activity tests based on protein degradation in three-dimensional structures</title>
    <abstract language="eng">The pattern of the activity of proteases is related to distinct physiological states of living organisms. Often activity changes of a certain protease can be assigned to a specific disease. Hence, they are useful biomarkers and a simple and fast determination method of their activity could be a valuable tool for the efficient monitoring of numerous diseases. Here, two different methods for the qualitative and quantitative determination of protease activity are demonstrated using the model system of proteinase K. The first test system is based on a protein-modified and colored 3D silica structure that changes color when exposed to the enzyme. This method has also been used for the detection of matrix metallo-protease 2 (MMP2) with gelatine as protease substrate on the plates. The second detection system uses the decrease in the voltammetric signal of a cytochrome c/DNA multilayer electrode after incubation with a protease to quantitatively determine its proteolytic activity. While activities down to 0.15 U/ml can be detected with the first method, the second one provides detection limits of about 0.03 U/ml (for proteinase K.) The functionality of both systems can be demonstrated and ways for further enhancement of sensitivity have been elucidated.</abstract>
    <parentTitle language="eng">Bioelectrochemistry</parentTitle>
    <identifier type="issn">1567-5394</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-19294</identifier>
    <enrichment key="opus.import.data">@articleGöbel2024, address = "Amsterdam", publisher = "Elsevier", issn = "1567-5394", eissn = "1878-562X", abstract = "The pattern of the activity of proteases is related to distinct physiological states of living organisms. Often activity changes of a certain protease can be assigned to a specific disease. Hence, they are useful biomarkers and a simple and fast determination method of their activity could be a valuable tool for the efficient monitoring of numerous diseases. Here, two different methods for the qualitative and quantitative determination of protease activity are demonstrated using the model system of proteinase K. The first test system is based on a protein-modified and colored 3D silica structure that changes color when exposed to the enzyme. This method has also been used for the detection of matrix metallo-protease 2 (MMP2) with gelatine as protease substrate on the plates. The second detection system uses the decrease in the voltammetric signal of a cytochrome c/DNA multilayer electrode after incubation with a protease to quantitatively determine its proteolytic activity. While activities down to 0.15 U/ml can be detected with the first method, the second one provides detection limits of about 0.03U/ml (for proteinase K.) The functionality of both systems can be demonstrated and ways for further enhancement of sensitivity have been elucidated.", author = "Göbel, Gero and Müller, Florian and Talke, Anja and Ahnert, Uwe and Lisdat, Fred", doi = "10.1016/j.bioelechem.2024.108775", journal = "Bioelectrochemistry", keywords = "Multilayer electrode, Protease activity, Proteinase K, Silica gel", language = "eng", pages = "108775", title = "Qualitative and quantitative protease activity tests based on protein degradation in three-dimensional structures", volume = "160", year = "2024"</enrichment>
    <enrichment key="opus.import.dataHash">md5:123024a853cf042176dbcce315a469b8</enrichment>
    <enrichment key="opus.import.date">2024-07-18T07:25:21+00:00</enrichment>
    <enrichment key="opus.import.file">/tmp/phpAtYnHP</enrichment>
    <enrichment key="opus.import.format">bibtex</enrichment>
    <enrichment key="opus.import.id">6698c3616655e2.92728366</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1016/j.bioelechem.2024.108775</enrichment>
    <enrichment key="SourceTitle">Göbel, G., Müller, F., Talke, A., Ahnert, U., &amp; Lisdat, F. (2024). Qualitative and quantitative protease activity tests based on protein degradation in three-dimensional structures. Bioelectrochemistry, 160, 108775. doi:10.1016/j.bioelechem.2024.108775</enrichment>
    <enrichment key="opus.doi.autoCreate">false</enrichment>
    <enrichment key="opus.urn.autoCreate">true</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 4.0 International</licence>
    <author>Gero Göbel</author>
    <author>Florian Müller</author>
    <author>Anja Talke</author>
    <author>Uwe Ahnert</author>
    <author>Fred Lisdat</author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>multilayer electrode</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>protease activity</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>proteinase K</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>silica gel</value>
    </subject>
    <collection role="ddc" number="572">Biochemie</collection>
    <collection role="institutes" number="">Fachbereich Ingenieur- und Naturwissenschaften</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="green_open_access" number="4">Hybrid Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/1929/1-s2.0-S1567539424001373-main.pdf</file>
  </doc>
  <doc>
    <id>312</id>
    <completedYear>2013</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>deu</language>
    <pageFirst>17</pageFirst>
    <pageLast>22</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>17</volume>
    <type>articlewildau</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>2013-10-16</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="deu">Direkte Kontaktierung des Enzyms (PQQ)-GDH und Elektroden mit Hilfe von polymermodifizierten Nanoröhren für die Anwendung in Biobrennstoffzellen</title>
    <abstract language="deu">In dieser Studie präsentieren wir eine Enzymelektrode, bei der ein direkter Elektronentransfer (DET) zwischen der Pyrrolochinolinchinon-abhängigen Glukosedehydrogenase (PQQ)-GDH und einer Elektrode realisiert werden konnte. Hierfür wird eine Goldelektrode mit mehrwandigen Kohlenstoffnanoröhren [engl. multi-walled carbon nanotubes (MWCNT)] modifiziert, anschließend mit einem Copolymer aus Anilinderivaten überzogen und dann die (PQQ)-GDH (Acinetobacter calcoaceticus) kovalent immobilisiert. Die gepulste Polymersynthese wird hinsichtlich der Effektivität der bioelektrokatalytischen Umsetzung von Glukose optimiert. Die Glukoseoxidation startet bei einem Potential von -0,1 V vs. Ag/AgCl (1 M KCl) und Stromdichten von bis zu 500 μA/cm² (+0,1 V) können erreicht werden. Der Messbereich für Glukose liegt bei 0,1-5 mM (+0,1 V vs. Ag/AgCl). Der dynamische Bereich ist bei höherem Potential auf bis zu 100 mM (+0,4 V vs Ag/AgCl) erweitert. Die Elektrode wird als Anode in einer Biobrennstoffzelle (BBZ) mit einer Bilirubinoxidase-modifizierten MWCNT/Gold-Kathode eingesetzt. Beide Elektroden basieren auf einem DET. Das Zellpotential der BBZ beträgt 680 ±20 mV und sie erreicht eine maximale Leistungsdichte von 65 μW/cm² (bei einer Zellspannung von 350 mV).</abstract>
    <parentTitle language="deu">Wissenschaftliche Beiträge 2013</parentTitle>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-3127</identifier>
    <identifier type="doi">10.15771/0949-8214_2013_1_3</identifier>
    <identifier type="issn">0949-8214</identifier>
    <enrichment key="ZSTiteliD">16238</enrichment>
    <licence>Creative Commons - CC BY-NC-ND 3.0 DE - Namensnennung - Nicht-kommerziell - Keine Bearbeitung 3.0 Deutschland</licence>
    <author>Ivo Schubart</author>
    <author>Gero Göbel</author>
    <author>Fred Lisdat</author>
    <collection role="ddc" number="621">Angewandte Physik</collection>
    <collection role="ddc" number="660">Chemische Verfahrenstechnik</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="Publikationen_der_TH_Wildau" number="">Wissenschaftliche Beiträge</collection>
    <collection role="open_access" number="">open_access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/312/Direkte Kontaktierung des Enzyms (PQQ)-GDH und Elektroden mithilfe von polymermodifizierten Nanor Âhren f  r die  Anwendung in Biobrennstoffzellen.pdf</file>
  </doc>
  <doc>
    <id>81</id>
    <completedYear>2011</completedYear>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>deu</language>
    <pageFirst>13</pageFirst>
    <pageLast>21</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>15</volume>
    <type>articlewildau</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="deu">Entwicklung einer Glucosedehydrogenase-basierten Anode und deren Anwendung in einer Glucose/O2-Biobrennstoffzelle</title>
    <abstract language="deu">Unter Verwendung von mehrwandigen Kohlenstoffnanoröhren wurde in dieser Studie eine neuartige Anode zum Einsatz in Biobrennstoffzellen entwickelt. Dazu wurde das rekombinante Enzym Pyrrolochinolinchinon(PQQ)- abhängige Glucosedehydrogenase kovalent an eine aus PQQ bestehenden Zwischenschicht gekoppelt, welche zuvor an die Kohlenstoffnanoröhren adsorbiert war. Die Nanoröhren wurden aufgrund ihrer Thiolmodifikation chemisorptiv auf einer Goldelektrode gebunden. In glucosehaltiger Lösung konnte der Start eines katalytischen Stroms bei einem Potential von -80 mV vs. Ag/AgCl (1 MKCl) beobachtet werden. Unter Substratsättigung wurden Stromdichten im Bereich von 170 bis 200 μA/cm2 gemessen. Dieses System basiert auf einem mediatorvermittelten Elektronentransfer. Die entwickelte (PQQ)-GDH-MWCNT-Elektrode wurde mit einer MWCNT-modifizierten Elektrode kombiniert, bei der Bilirubinoxidase (BOD) als Biokatalysator fungiert. Daraus resultierte eine membranfreie Biobrennstoffzelle mit einem leichgewichtspotential von 600 mV und Leistungsdichten im Bereich von 20-25 μW/cm2.</abstract>
    <abstract language="eng">In this study a biofuel cell anode is developed on the basis of multi-walled carbon nanotubes (MWCNTs). Recombinant pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase is covalently coupled to a PQQ-layer which is adsorbed onto thiolmodified MWCNTs. The MWCNTs are chemisorbed to a gold electrode. In the presence of glucose a catalytic current starts at a potential of -80 mV vs. Ag/AgCl, 1 M KCl. Under substrate saturation current densities of 170 to 200 μA/cm2 can be achieved. The operation is based on mediated electron transfer of the enzyme. This (PQQ)-GDH-MWCNT-electrode is combined with a MWCNT-modifi ed electrode to which bilirubin oxidase (BOD) is covalently coupled. The resulting membrane-free biofuel cell has an open cell potential of 600 mV and can achieve power densities in the range of 20-25 μW/cm2.</abstract>
    <parentTitle language="deu">Wissenschaftliche Beiträge 2011</parentTitle>
    <identifier type="issn">0949-8214</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus-1039</identifier>
    <identifier type="opus3-id">103</identifier>
    <identifier type="doi">10.15771/0949-8214_2011_1_2</identifier>
    <enrichment key="InvalidVerification">123</enrichment>
    <enrichment key="ZSTiteliD">16238</enrichment>
    <licence>Creative Commons - CC BY-NC-ND 3.0 DE - Namensnennung - Nicht-kommerziell - Keine Bearbeitung 3.0 Deutschland</licence>
    <author>Christoph K. Tanne</author>
    <author>Gero Göbel</author>
    <author>Fred Lisdat</author>
    <collection role="ddc" number="572">Biochemie</collection>
    <collection role="ddc" number="621">Angewandte Physik</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="Publikationen_der_TH_Wildau" number="">Wissenschaftliche Beiträge</collection>
    <collection role="open_access" number="">open_access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/81/TH_WB2011_Beitrag02_Tanne_Goebel_Lisdat.pdf</file>
  </doc>
  <doc>
    <id>1526</id>
    <completedYear>2014</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>195</pageFirst>
    <pageLast>200</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume/>
    <type>conferenceobject</type>
    <publisherName>Society of Photo-Optical Instrumentation Engineers (SPIE)</publisherName>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Light-addressable amperometric electrodes for enzyme sensors based on direct quantum dot-electrode contacts</title>
    <abstract language="eng">Quantum dots allow the generation of charge carriers upon illumination. When these particles are attached to an electrode a photocurrent can be generated. This allows their use as a light-switchable layer on the surface. The QDs can not only exchange electronics with the electrode, but can also interact with donor or acceptor compounds in solution providing access to the construction of signal chains starting from an analytic molecule. The magnitude and the direction of the photocurrent depend on several factors such as electrode polarization, solution pH and composition. These defined dependencies have been evaluated with respect to the combination of QD-electrodes with enzyme reactions for sensorial purpose. CdSe/ZnS-QD-modified electrodes can be used to follow enzymatic reactions in solution based on the oxygen sensitivity. In order to develop a photoelectrochemical biosensor, e.g. glucose oxidase is immobilized on the CdSe/ZnS-electrode. One immobilization strategy applies the layer-by-layer-technique of GOD and a polyelectrolyte. Photocurrent measurements of such a sensor show a clear concentration dependent behavior. The principle of combing QD oxidase. The sensitivity of quantum dot electrodes can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be demonstrated that direct electron transfer from excited quantum dots can be achieved with the redox protein cytochrome c. This allows the detection of the protein, but also interaction partners such as a enzymes or superoxide.</abstract>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-15266</identifier>
    <enrichment key="opus.import.date">2021-09-17T07:35:01+00:00</enrichment>
    <enrichment key="opus.source">sword</enrichment>
    <enrichment key="opus.import.user">sword</enrichment>
    <enrichment key="opus.import.file">filename=phpqmOywh</enrichment>
    <enrichment key="opus.import.checksum">3624378cffb6863feb5638673b879ee2</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1117/12.2044601</enrichment>
    <enrichment key="CopyrightInfo">Copyright 2014 Society of Photo-Optical Instrumentation Engineers (SPIE). One print or electronic copy may be made for personal use only. Systematic reproduction and distribution, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper are prohibited.</enrichment>
    <enrichment key="SourceTitle">M. Riedel, G. Göbel, W. J. Parak, and F. Lisdat "Light-addressable amperometric electrodes for enzyme sensors based on direct quantum dot-electrode contacts", Proc. SPIE 8955, Colloidal Nanoparticles for Biomedical Applications IX, 89551M (24 March 2014); https://doi.org/10.1117/12.2044601</enrichment>
    <licence>Das Dokument ist urheberrechtlich geschützt.</licence>
    <author>Marc Riedel</author>
    <author>Gero Göbel</author>
    <author>Wolfgang J. Parak</author>
    <author>Fred Lisdat</author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>quantum dot electrode</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>enzyme sensor</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>signal chain</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>photobioelectrochemistry</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>light adressability</value>
    </subject>
    <collection role="ddc" number="572">Biochemie</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="Import" number="import">Import</collection>
    <collection role="green_open_access" number="2">Green Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/1526/89551M.pdf</file>
  </doc>
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