http://purl.uniprot.org/citations/17261542 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17261542 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutants of flavin mononucleotide-binding protein (FMN-bp) were made by site-directed mutagenesis to investigate the role of carboxyl-terminal Leu122 of the pairing subunit in controlling redox potentials, binding the prosthetic group, and forming the tertiary and quaternary structure. We compared the oxidation-reduction potentials, FMN-binding properties, and higher structures of wild-type FMN-bp and four mutant proteins (L122Y, L122E, L122K and L122-deleted). We found that the redox potentials were affected by mutations. Also, the affinities of L122E, L122K and L122 deletion mutant apoproteins for FMN were lower than for the wild-type apoprotein, whereas the affinity of L122Y for FMN was increased. Analytical ultracentrifugation showed that the dissociation constants for dimerization of L122E and L122K were larger than for wild-type FMN-bp, whereas the dissociation constants for L122Y and the deletion mutant were lower than for the wild type. Finally, we determined the higher structures of L122Y, L122E and L122K mutants by X-ray crystallography. Our results show that the mutation of Leu122 in FMN-bp changes midpoint potentials, dissociation constants for FMN, and dimer formation, indicating that this residue is important in the pairing subunit."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvm051"xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Inoue H."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Higuchi Y."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Kitamura M."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Morimoto Y."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Yasuoka N."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Shibata N."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Suto K."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Hayashida T."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/author | "Terakawa K."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/name | "J Biochem"xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/pages | "459-468"xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/title | "Determination of the role of the Carboxyl-terminal leucine-122 in FMN-binding protein by mutational and structural analysis."xsd:string |
http://purl.uniprot.org/citations/17261542 | http://purl.uniprot.org/core/volume | "141"xsd:string |
http://purl.uniprot.org/citations/17261542 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17261542 |
http://purl.uniprot.org/citations/17261542 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17261542 |
http://purl.uniprot.org/uniprot/#_Q46604-mappedCitation-17261542 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17261542 |
http://purl.uniprot.org/uniprot/Q46604 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17261542 |