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http://purl.uniprot.org/citations/8695637http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8695637http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8695637http://www.w3.org/2000/01/rdf-schema#comment"A cDNA with an open reading frame of 1929 bp (termed sir) was isolated from a lambda ZapII library of Arabidopsis thaliana leaf tissue. The polypeptide sequence deduced from the cDNA is homologous to the ferredoxin-dependent sulfite reductase (EC 1.8.7.1) from Synechococcus PCC7942 and distantly related to the hemoprotein subunit of Escherichia coli NADPH-dependent sulfite reductase (EC 1.8.1.2). A molecular mass of 71.98 kDa can be predicted for a ferredoxin sulfite reductase from A. thaliana. The polypeptide consists of 642 amino acids including a transit peptide of 66 residues (6.72 kDa) that is assumed to direct the protein into the plastid. For expression and enzymatic characterization of a putative A. thaliana ferredoxin sulfite reductase, the DNA of the transit peptide was deleted by a PCR method. The truncated cDNA clone was expressed as his-tag fusion protein. The modified gene product was enzymatically inactive but specific cross-reaction with polyclonal antibodies against ferredoxin sulfite reductase from Synechococcus is seen as confirmation of its identity as higher plant ferredoxin sulfite reductase."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.org/dc/terms/identifier"doi:10.1016/0167-4838(96)00066-0"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.org/dc/terms/identifier"doi:10.1016/0167-4838(96)00066-0"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Gisselmann G."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Gisselmann G."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Schwenn J.D."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Schwenn J.D."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Bruehl A."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Bruehl A."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Haverkamp T."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/author"Haverkamp T."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/pages"119-124"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/pages"119-124"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/title"A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/title"A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase."xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/volume"1295"xsd:string
http://purl.uniprot.org/citations/8695637http://purl.uniprot.org/core/volume"1295"xsd:string
http://purl.uniprot.org/citations/8695637http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8695637
http://purl.uniprot.org/citations/8695637http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8695637