Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase


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SCHINK, Bernhard, Peter KRONECK, Felix TEN BRINK, 2011. Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase. In: Journal of Bacteriology. 193(5), pp. 1229-1236. ISSN 0021-9193. eISSN 1098-5530

@article{Schink2011-03Explo-16695, title={Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase}, year={2011}, doi={10.1128/JB.01057-10}, number={5}, volume={193}, issn={0021-9193}, journal={Journal of Bacteriology}, pages={1229--1236}, author={Schink, Bernhard and Kroneck, Peter and Ten Brink, Felix} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/16695"> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-11T10:55:59Z</dcterms:available> <dc:language>eng</dc:language> <dcterms:issued>2011-03</dcterms:issued> <dc:contributor>Kroneck, Peter</dc:contributor> <dc:contributor>Ten Brink, Felix</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16695"/> <dc:creator>Ten Brink, Felix</dc:creator> <dcterms:title>Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase</dcterms:title> <dcterms:bibliographicCitation>First publ. in: Journal of Bacteriology ; 193 (2011), 5. - pp. 1229-1236</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">The soluble tungsten, iron-sulfur enzyme acetylene hydratase (AH) from mesophilic Pelobacter acetylenicus is a member of the dimethyl sulfoxide (DMSO) reductase family. It stands out from its class as it catalyzes a nonredox reaction, the addition of H₂O to acetylene (H-C≡C-H) to form acetaldehyde (CH₃CHO). Caught in its active W(IV) state, the high-resolution three-dimensional structure of AH offers an excellent starting point to tackle its unique chemistry and to identify catalytic amino acid residues within the active site cavity: Asp13 close to W(IV) coordinated to two molybdopterin-guanosine-dinucleotide ligands, Lys48 which couples the [4Fe-4S] cluster to the W site, and Ile142 as part of a hydrophobic ring at the end of the substrate access channel designed to accommodate the substrate acetylene. A protocol was developed to express AH in Escherichia coli and to produce active-site variants which were characterized with regard to activity and occupancy of the tungsten and iron-sulfur centers. By this means, fusion of the N-terminal chaperone binding site of the E. coli nitrate reductase NarG to the AH gene improved the yield and activity of AH and its variants significantly. Results from site-directed mutagenesis of three key residues, Asp13, Lys48, and Ile142, document their important role in catalysis of this unusual tungsten enzyme.</dcterms:abstract> <dc:creator>Kroneck, Peter</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-11T10:55:59Z</dc:date> <dc:creator>Schink, Bernhard</dc:creator> <dc:rights>deposit-license</dc:rights> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Schink, Bernhard</dc:contributor> </rdf:Description> </rdf:RDF>

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