<?xml version="1.0" encoding="utf-8"?>
<export-example>
  <doc>
    <id>1363</id>
    <completedYear>2020</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>2125</pageFirst>
    <pageLast>2127</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>24</volume>
    <type>article</type>
    <publisherName>Springer Nature</publisherName>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Coupling biology to electrochemistry—future trends and needs</title>
    <abstract language="eng">The coupling of biological entities with electrodes has already quite some history and has reached a status which is not only based on phenomenological descriptions. Nowadays, we are able to effectively couple redox centres within protein molecules to electrochemical transducers. This allows the transduction of a biochemical reaction into an electrode signal with applications mainly in sensing and bioenergetics [1,2,3,4,5,6,7,8]. However, in most cases, this coupling is not direct, and shuttle molecules or side products of the reaction are used. But also for the direct coupling, significant progress has been made, and several enzymes and redox proteins can be addressed directly by electrodes [8,9,10,11,12,13]. The understanding of the functioning of developed systems is, however, in its infancy. Charge and electrostatic interactions have been mostly studied, and for small dipole molecules such as cytochrome c, the situation can be well described [14]. There is a lack of understanding for more complex enzyme molecules which brings a lot of trial and error into research.</abstract>
    <parentTitle language="eng">Journal of Solid State Electrochemistry</parentTitle>
    <identifier type="issn">1433-0768</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-13639</identifier>
    <enrichment key="SourceTitle">Lisdat, F. (2020). Coupling biology to electrochemistry—future trends and needs Journal of Solid State Electrochemistry. 24, 2125–2127.</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1007/s10008-020-04714-y</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 4.0 International</licence>
    <author>Fred Lisdat</author>
    <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="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/1363/Lisdat2020_CouplingBiologyToElectrochemis.pdf</file>
  </doc>
  <doc>
    <id>1362</id>
    <completedYear>2020</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>171</pageFirst>
    <pageLast>179</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>2</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Current limits of structural biology: The transient interaction between cytochrome c6 and photosystem I</title>
    <abstract language="eng">Trimeric photosystem I from the cyanobacterium Thermosynechococcus elongatus (TePSI) is an intrinsic membrane protein, which converts solar energy into electrical energy by oxidizing the soluble redox mediator cytochrome c6 (Cyt c6) and reducing ferredoxin. Here, we use cryo-electron microscopy and small angle neutron scattering (SANS) to characterize the transient binding of Cyt c6 to TePSI. The structure of TePSI cross-linked to Cyt c6 was solved at a resolution of 2.9 Å and shows additional cofactors as well as side chain density for 84% of the peptide chain of subunit PsaK, revealing a hydrophobic, membrane intrinsic loop that enables binding of associated proteins. Due to the poor binding specificity, Cyt c6 could not be localized with certainty in our cryo-EM analysis. SANS measurements confirm that Cyt c6 does not bind to TePSI at protein concentrations comparable to those for cross-linking. However, SANS data indicate a complex formation between TePSI and the non-native mitochondrial cytochrome from horse heart (Cyt cHH). Our study pinpoints the difficulty of identifying very small binding partners (less than 5% of the overall size) in EM structures when binding affinities are poor. We relate our results to well resolved co-structures with known binding affinities and recommend confirmatory methods for complexes with KM values higher than 20 μM.</abstract>
    <parentTitle language="eng">Current Research in Structural Biology</parentTitle>
    <identifier type="issn">2665-928X</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-13628</identifier>
    <enrichment key="opus.source">publish</enrichment>
    <enrichment key="SourceTitle">Kölsch, A., Radon, C., Golub, M., Baumert, A., Bürger, J., Mielke, T., et al. (2020). Current limits of structural biology: The transient interaction between cytochrome c6 and photosystem I Current Research in Structural Biology. 2, 171-179.</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1016/j.crstbi.2020.08.003</enrichment>
    <licence>Creative Commons - CC BY-NC-ND - Namensnennung - Nicht kommerziell - Keine Bearbeitungen 4.0 International</licence>
    <author>Adrian Kölsch</author>
    <author>C. Radon</author>
    <author>M. Golub</author>
    <author>A. Baumert</author>
    <author>Jörg Bürger</author>
    <author>Thorsten Mielke</author>
    <author>Fred Lisdat</author>
    <author>Artem Feoktystov</author>
    <author>Jörg Pieper</author>
    <author>Athina Zouni</author>
    <author>Petra Wendler</author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>photosystem I</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>cryo-EM</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Thermosynechococcus elongatus</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>small angle neutron scattering</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>cytochrome c6</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>electron transfer</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>photo-biotechnology</value>
    </subject>
    <collection role="ddc" number="570">Biowissenschaften; Biologie</collection>
    <collection role="institutes" number="">Fachbereich Ingenieur- und Naturwissenschaften</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/1362/1-s2.0-S2665928X20300179-main.pdf</file>
  </doc>
</export-example>
