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http://purl.uniprot.org/citations/8174709http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8174709http://www.w3.org/2000/01/rdf-schema#comment"A mutant of spinach ferredoxin-NADP+ reductase, in which Lys-88 has been changed to glutamine, has been obtained by site-directed mutagenesis. The mutant enzyme was fully active as a diaphorase, but partially impaired in ferredoxin-dependent cytochrome c reductase activity. By steady-state kinetics, the Km for ferredoxin of the K88Q enzyme was found to have increased 10-fold, whereas the kcat was unaffected by the amino acid replacement. The interaction between oxidized ferredoxin and the enzyme forms was also studied by spectrofluorimetric titration: Kd values of 110 and 10 nM were determined for the mutant and wild-type proteins, respectively. These data point out the importance of a positive charge at position 88 of the reductase for the interaction with ferredoxin, confirming previous cross-linking studies."xsd:string
http://purl.uniprot.org/citations/8174709http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(94)80565-2"xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/author"Aliverti A."xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/author"Zanetti G."xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/author"Corrado M.E."xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/pages"247-250"xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/title"Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin."xsd:string
http://purl.uniprot.org/citations/8174709http://purl.uniprot.org/core/volume"343"xsd:string
http://purl.uniprot.org/citations/8174709http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8174709
http://purl.uniprot.org/citations/8174709http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8174709
http://purl.uniprot.org/uniprot/#_P00455-mappedCitation-8174709http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8174709
http://purl.uniprot.org/uniprot/#_P00004-mappedCitation-8174709http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8174709
http://purl.uniprot.org/uniprot/#_P00221-mappedCitation-8174709http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8174709
http://purl.uniprot.org/uniprot/P00004http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8174709
http://purl.uniprot.org/uniprot/P00221http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8174709
http://purl.uniprot.org/uniprot/P00455http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8174709