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http://purl.uniprot.org/citations/7893687http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7893687http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7893687http://www.w3.org/2000/01/rdf-schema#comment"The three-dimensional structure of NADH-cytochrome b5 reductase from pig liver microsomes has been determined at 2.4 A resolution by X-ray crystallography. The molecular structure reveals two domains, the FAD binding domain and the NADH domain. A large cleft lies between these two domains and contains the binding site for the FAD prosthetic group. The backbone structure of the FAD binding domain has a great similarity to that of ferredoxin-NADP+ reductase [Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) Science 251, 60-65], in spite of the relatively low sequence homology (about 15%) between the two enzymes. On the other hand, the structure of the NADH domain has several structural differences from that of the NADP+ domain of ferredoxin-NADP+ reductase. The size of the cleft between the two domains is larger in NADH-cytochrome b5 reductase than in ferredoxin-NADP+ reductase, which may be responsible for the observed difference in the nucleotide accessibility in the two enzymes."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.org/dc/terms/identifier"doi:10.1021/bi00009a004"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.org/dc/terms/identifier"doi:10.1021/bi00009a004"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Nishida H."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Nishida H."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Kobayashi K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Kobayashi K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Miki K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Miki K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Yamanaka M."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Yamanaka M."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Inaka K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Inaka K."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Kaida S."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/author"Kaida S."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/pages"2763-2767"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/pages"2763-2767"xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/title"Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution."xsd:string
http://purl.uniprot.org/citations/7893687http://purl.uniprot.org/core/title"Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution."xsd:string