| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/2000/01/rdf-schema#comment | "Reduced flavodoxin I (Fld1) is required in Escherichia coli for reductive radical generation in AdoMet-dependent radical enzymes and reductive activation of cobalamin-dependent methionine synthase. Ferredoxin (Fd) and flavodoxin II (Fld2) are also present, although their precise roles have not been ascertained. Ferredoxin (flavodoxin):NADP+ oxidoreductase (FNR) was discovered in E. coli as an NADPH-dependent reductant of Fld1 that facilitated generation of active methionine synthase in vitro; FNR and Fld1 will also supply electrons for the reductive cleavage of AdoMet essential for generating protein or substrate radicals in pyruvate formate-lyase, class III ribonucleotide reductase, biotin synthase, and, potentially, lipoyl synthase. As part of ongoing efforts to understand the various redox pathways that will support AdoMet-dependent radical enzymes in E. coli, we have examined the relative specificity of E. coli FNR for Fd, Fld1, and Fld2. While FNR will reduce all three proteins, Fd is the kinetically and thermodynamically preferred partner. Fd binds to FNR with high affinity (K(d)xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0003-9861(02)00421-6"xsd:string |
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| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/author | "Jarrett J.T."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/author | "Jarrett J.T."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/author | "Wan J.T."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/author | "Wan J.T."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/pages | "116-126"xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/pages | "116-126"xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/title | "Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/title | "Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/volume | "406"xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://purl.uniprot.org/core/volume | "406"xsd:string |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12234497 |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12234497 |
| http://purl.uniprot.org/citations/12234497 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12234497 |
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| http://purl.uniprot.org/citations/12234497 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12234497 |