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http://purl.uniprot.org/citations/3360752http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3360752http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3360752http://www.w3.org/2000/01/rdf-schema#comment"Two ferredoxins, Fd I and Fd II, were isolated and purified from Desulfovibrio vulgaris Miyazaki. The major component, Fd I, is an iron-sulfur protein of Mr 12,000, composed of two identical subunits. The absorption spectra of Fd I and Fd II have a broad absorption shoulder near 400 nm characteristic of iron-sulfur proteins. The purity index, A400/A280, of Fd I is 0.69, and its millimolar absorption coefficient at 400 nm is 3.73 per Fe. It contains two redox centers with discrete redox behaviors. The amino acid composition and the N-terminal sequence of Fd I are similar to those of Fd III of Desulfovibrio africanus Benghazi and Fd II of Desulfovibrio desulfuricans Norway. Fd I does not serve as an electron carrier for the hydrogenase of D. vulgaris Miyazaki, but it serves as a carrier for pyruvate dehydrogenase of this bacterium. The evolution of H2 from pyruvate was observed by a reconstructed system containing purified hydrogenase, cytochrome C3, Fd I, partially purified pyruvate dehydrogenase, and CoA. The H2-sulfite reducing system can be reconstructed from the purified hydrogenase, cytochrome C3, Fd I and desulfoviridin (sulfite reductase), but the reaction rate is very slow compared to that of the crude extract at the same molar ratio of the components."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a122216"xsd:string
http://purl.uniprot.org/citations/3360752http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a122216"xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Kondo S."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Kondo S."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Ogata M."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Ogata M."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Yagi T."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Yagi T."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Okawara N."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/author"Okawara N."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/pages"121-125"xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/pages"121-125"xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/title"Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/title"Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki."xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/volume"103"xsd:string
http://purl.uniprot.org/citations/3360752http://purl.uniprot.org/core/volume"103"xsd:string
http://purl.uniprot.org/citations/3360752http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3360752
http://purl.uniprot.org/citations/3360752http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3360752