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http://purl.uniprot.org/citations/9353305http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9353305http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9353305http://www.w3.org/2000/01/rdf-schema#comment"The structures of oxidized, reduced, nitrite-soaked oxidized and nitrite-soaked reduced nitrite reductase from Alcaligenes faecalis have been determined at 1.8-2.0 A resolution using data collected at -160 degrees C. The active site at cryogenic temperature, as at room temperature, contains a tetrahedral type II copper site liganded by three histidines and a water molecule. The solvent site is empty when crystals are reduced with ascorbate. A fully occupied oxygen-coordinate nitrite occupies the solvent site in crystals soaked in nitrite. Ascorbate-reduced crystals soaked in a glycerol-methanol solution and nitrite at -40 degrees C remain colorless at -160 degrees C but turn amber-brown when warmed, suggesting that NO is released. Nitrite is found at one-half occupancy. Five new solvent sites in the oxidized nitrite bound form exhibit defined but different occupancies in the other three forms. These results support a previously proposed mechanism by which nitrite is bound primarily by a single oxygen atom that is protonable, and after reduction and cleavage of that N-O bond, NO is released leaving the oxygen atom bound to the Cu site as hydroxide or water."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.45.28455"xsd:string
http://purl.uniprot.org/citations/9353305http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.45.28455"xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Turley S."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Turley S."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Adman E.T."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Adman E.T."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Murphy M.E."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/author"Murphy M.E."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/pages"28455-28460"xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/pages"28455-28460"xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/title"Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/title"Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications."xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9353305http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9353305http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9353305
http://purl.uniprot.org/citations/9353305http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9353305
http://purl.uniprot.org/citations/9353305http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9353305
http://purl.uniprot.org/citations/9353305http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9353305