@article{Seiffert2007Struc-7218,
  year={2007},
  title={Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase},
  number={9},
  volume={104},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  pages={3073--3077},
  author={Seiffert, Grażyna Bernadeta and Ullmann, G. Matthias and Messerschmidt, Albrecht and Schink, Bernhard and Kroneck, Peter M. H. and Einsle, Oliver}
}

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    <dcterms:bibliographicCitation>First publ. in: Proceedings of the National Academy of Sciences of the United States of America  104 (2007), 9, pp. 3073-3077</dcterms:bibliographicCitation>
    <dc:creator>Messerschmidt, Albrecht</dc:creator>
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    <dc:creator>Schink, Bernhard</dc:creator>
    <dcterms:title>Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase</dcterms:title>
    <dc:contributor>Seiffert, Grażyna Bernadeta</dc:contributor>
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    <dc:contributor>Kroneck, Peter M. H.</dc:contributor>
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    <dc:creator>Ullmann, G. Matthias</dc:creator>
    <dcterms:issued>2007</dcterms:issued>
    <dc:contributor>Messerschmidt, Albrecht</dc:contributor>
    <dc:creator>Seiffert, Grażyna Bernadeta</dc:creator>
    <dc:contributor>Schink, Bernhard</dc:contributor>
    <dc:creator>Kroneck, Peter M. H.</dc:creator>
    <dc:contributor>Ullmann, G. Matthias</dc:contributor>
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    <dcterms:abstract xml:lang="eng">The tungsten iron sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 Å now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.</dcterms:abstract>
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