@article{Gemmecker2015Phyto-32857,
  year={2015},
  doi={10.1371/journal.pone.0131717},
  title={Phytoene Desaturase from Oryza sativa : Oligomeric Assembly, Membrane Association and Preliminary 3D-Analysis},
  number={7},
  volume={10},
  journal={PLOS ONE},
  author={Gemmecker, Sandra and Schaub, Patrick and Koschmieder, Julian and Brausemann, Anton and Drepper, Friedel and Rodriguez-Franco, Marta and Ghisla, Sandro and Warscheid, Bettina and Einsle, Oliver and Beyer, Peter},
  note={Article Number: e0131717}
}

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    <dc:creator>Rodriguez-Franco, Marta</dc:creator>
    <dc:creator>Schaub, Patrick</dc:creator>
    <dc:language>eng</dc:language>
    <dc:contributor>Drepper, Friedel</dc:contributor>
    <dc:contributor>Brausemann, Anton</dc:contributor>
    <dc:contributor>Rodriguez-Franco, Marta</dc:contributor>
    <dcterms:abstract xml:lang="eng">Recombinant phytoene desaturase (PDS-His&lt;sub&gt;6&lt;/sub&gt;) from rice was purified to near-homogeneity and shown to be enzymatically active in a biphasic, liposome-based assay system. The protein contains FAD as the sole protein-bound redox-cofactor. Benzoquinones, not replaceable by molecular oxygen, serve as a final electron acceptor defining PDS as a 15-cis-phytoene (donor):plastoquinone oxidoreductase. The herbicidal PDS-inhibitor norflurazon is capable of arresting the reaction by stabilizing the intermediary FAD&lt;sub&gt;red&lt;/sub&gt;, while an excess of the quinone acceptor relieves this blockage, indicating competition. The enzyme requires its homo-oligomeric association for activity. The sum of data collected through gel permeation chromatography, non-denaturing polyacrylamide electrophoresis, chemical cross-linking, mass spectrometry and electron microscopy techniques indicate that the high-order oligomers formed in solution are the basis for an active preparation. Of these, a tetramer consisting of dimers represents the active unit. This is corroborated by our preliminary X-ray structural analysis that also revealed similarities of the protein fold with the sequence-inhomologous bacterial phytoene desaturase CRTI and other oxidoreductases of the GR2-family of flavoproteins. This points to an evolutionary relatedness of CRTI and PDS yielding different carotene desaturation sequences based on homologous protein folds.</dcterms:abstract>
    <dc:contributor>Warscheid, Bettina</dc:contributor>
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    <dc:creator>Drepper, Friedel</dc:creator>
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    <dc:creator>Beyer, Peter</dc:creator>
    <dcterms:issued>2015</dcterms:issued>
    <dc:contributor>Schaub, Patrick</dc:contributor>
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    <dc:creator>Ghisla, Sandro</dc:creator>
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    <dc:creator>Brausemann, Anton</dc:creator>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dc:contributor>Beyer, Peter</dc:contributor>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dc:contributor>Einsle, Oliver</dc:contributor>
    <dc:creator>Koschmieder, Julian</dc:creator>
    <dc:creator>Einsle, Oliver</dc:creator>
    <dc:contributor>Koschmieder, Julian</dc:contributor>
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    <dcterms:title>Phytoene Desaturase from Oryza sativa : Oligomeric Assembly, Membrane Association and Preliminary 3D-Analysis</dcterms:title>
    <dc:creator>Gemmecker, Sandra</dc:creator>
    <dc:creator>Warscheid, Bettina</dc:creator>
    <dc:contributor>Gemmecker, Sandra</dc:contributor>
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