1 Ocak 2015 Dergi makalesi Açık Erişim

Yucesoy, Deniz Tanil; Karaca, Banu Taktak; Cetinel, Sibel; Caliskan, Huseyin Burak; Adali, Esref; Gul-Karaguler, Nevin; Tamerler, Candan

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/81519</identifier>
  <creators>
    <creator>
      <creatorName>Yucesoy, Deniz Tanil</creatorName>
      <givenName>Deniz Tanil</givenName>
      <familyName>Yucesoy</familyName>
      <affiliation>Univ Washington, Mat Sci &amp; Engn, Seattle, WA 98195 USA</affiliation>
    </creator>
    <creator>
      <creatorName>Karaca, Banu Taktak</creatorName>
      <givenName>Banu Taktak</givenName>
      <familyName>Karaca</familyName>
    </creator>
    <creator>
      <creatorName>Cetinel, Sibel</creatorName>
      <givenName>Sibel</givenName>
      <familyName>Cetinel</familyName>
      <affiliation>Istanbul Tech Univ, Mol Biol &amp; Genet, TR-80626 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Caliskan, Huseyin Burak</creatorName>
      <givenName>Huseyin Burak</givenName>
      <familyName>Caliskan</familyName>
      <affiliation>Istanbul Tech Univ, Mol Biol &amp; Genet, TR-80626 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Adali, Esref</creatorName>
      <givenName>Esref</givenName>
      <familyName>Adali</familyName>
      <affiliation>Istanbul Tech Univ, Fac Comp &amp; Informat, TR-80626 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Gul-Karaguler, Nevin</creatorName>
      <givenName>Nevin</givenName>
      <familyName>Gul-Karaguler</familyName>
      <affiliation>Istanbul Tech Univ, Mol Biol &amp; Genet, TR-80626 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Tamerler, Candan</creatorName>
      <givenName>Candan</givenName>
      <familyName>Tamerler</familyName>
    </creator>
  </creators>
  <titles>
    <title>Direct Bioelectrocatalysis At The Interfaces By Genetically Engineered Dehydrogenase</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2015</publicationYear>
  <dates>
    <date dateType="Issued">2015-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/81519</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1680/bbn.14.00022</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">There is an emerging interest in developing bio-functionalisation routes serving as platforms for assembling diverse enzymes onto material surfaces. Specifically, the fabrication of next-generation, laboratory-on-a-chip-based sensing and energy-harvesting systems requires controlled orientation and organisation of the proteins at the inorganic interfaces. Herein, the authors take the initial steps towards designing multifunctional, enzyme-based platforms by genetically integrating the engineered materialselective peptide tags for tethering redox enzymes onto electrode surfaces. The authors engineered a fusion protein that genetically conjugates gold-binding peptide to formate dehydrogenase derived from Candida methylica. The expressed proteins were tested for both enzyme activity and self-directed gold-surface functionalisation ability. Their findings demonstrate the successful self-immobilisation of the engineered enzyme onto different gold electrodes while retaining the catalytic activity. Building on the functionalisation by the peptides, a fusion enzyme-integrated circuit-based biosensor system was designed. The catalytic conversion of the formate by the engineered dehydrogenase was successfully monitored on the electrode surface at subsequent intervals. The engineered peptide-mediated self-integrated electrode systems can be extended to develop a wide range of biosensing and energy-harvesting platforms using different combinations of materials and biomolecules. This paper contains supporting information that will be made available online once the issue is published. In the meantime, if you wish to get a copy of the supplementary file, please contact the Journals Editor, Sarah Brown, at sarah. brown@ icepublishing. com.</description>
  </descriptions>
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