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http://purl.uniprot.org/citations/9836629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9836629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9836629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9836629http://www.w3.org/2000/01/rdf-schema#comment"A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8 angstrom resolution by x-ray crystallography using multiwavelength anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the two-electron reduction of two protons to yield dihydrogen, was found to contain 20 gram atoms of iron per mole of protein, arranged into five distinct [Fe-S] clusters. The probable active-site cluster, previously termed the H-cluster, was found to be an unexpected arrangement of six iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe] subcluster both exist with an octahedral coordination geometry and are bridged to each other by three non-protein atoms, assigned as two sulfide atoms and one carbonyl or cyanide molecule. This structure provides insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.org/dc/terms/identifier"doi:10.1126/science.282.5395.1853"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.org/dc/terms/identifier"doi:10.1126/science.282.5395.1853"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Lanzilotta W.N."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Lanzilotta W.N."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Peters J.W."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Peters J.W."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Seefeldt L.C."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Seefeldt L.C."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Lemon B.J."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/author"Lemon B.J."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/pages"1853-1858"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/pages"1853-1858"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/title"X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8-A resolution."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/title"X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8-A resolution."xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/9836629http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/9836629http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9836629