Acetylene Hydratase : Part 5. Molybdenum/Tungsten

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SEIFFERT, Grazyna B., Dietmar ABT, Felix TENBRINK, David FISCHER, Oliver EINSLE, Peter M. H. KRONECK, 2008. Acetylene Hydratase : Part 5. Molybdenum/Tungsten. In: MESSERSCHMIDT, Albrecht, ed.. Handbook of Metalloproteins. Chichester, UK:John Wiley & Sons, Ltd. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met231

@incollection{Seiffert2008Acety-39244, title={Acetylene Hydratase : Part 5. Molybdenum/Tungsten}, year={2008}, doi={10.1002/0470028637.met231}, isbn={978-0-470-86981-9}, address={Chichester, UK}, publisher={John Wiley & Sons, Ltd}, booktitle={Handbook of Metalloproteins}, editor={Messerschmidt, Albrecht}, author={Seiffert, Grazyna B. and Abt, Dietmar and tenBrink, Felix and Fischer, David and Einsle, Oliver and Kroneck, Peter M. H.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Fischer, David</dc:creator> <dc:creator>Abt, Dietmar</dc:creator> <dc:contributor>Abt, Dietmar</dc:contributor> <dc:contributor>Kroneck, Peter M. H.</dc:contributor> <dc:contributor>tenBrink, Felix</dc:contributor> <bibo:uri rdf:resource=""/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Kroneck, Peter M. H.</dc:creator> <dcterms:issued>2008</dcterms:issued> <dc:creator>Einsle, Oliver</dc:creator> <dcterms:available rdf:datatype="">2017-06-13T09:23:28Z</dcterms:available> <dc:contributor>Einsle, Oliver</dc:contributor> <dc:creator>tenBrink, Felix</dc:creator> <dcterms:isPartOf rdf:resource=""/> <dcterms:abstract xml:lang="eng">The tungsten-iron-sulfur enzyme acetylene hydratase is a rather unique enzyme within the class of tungsten/molybdenum enzymes in the sense that it catalyzes a nonredox reaction, the addition of one molecule of water to the C[TRIPLE BOND]C bond of acetylene to form acetaldehyde. Its crystal structure (1.26 Å) reveals a close to octahedral, or trigonal antiprismatic tungsten center, which binds a water molecule that gets activated by an adjacent aspartate residue such that it can attack an acetylene molecule bound in a distinct, hydrophobic pocket. This requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe–4S] cluster. To gain access to this novel 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> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Acetylene Hydratase : Part 5. Molybdenum/Tungsten</dcterms:title> <dc:contributor>Fischer, David</dc:contributor> <dc:creator>Seiffert, Grazyna B.</dc:creator> <dc:date rdf:datatype="">2017-06-13T09:23:28Z</dc:date> <dc:language>eng</dc:language> <dspace:isPartOfCollection rdf:resource=""/> <dc:contributor>Seiffert, Grazyna B.</dc:contributor> </rdf:Description> </rdf:RDF>

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