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http://purl.uniprot.org/citations/20576851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20576851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20576851http://www.w3.org/2000/01/rdf-schema#comment"The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.org/dc/terms/identifier"doi:10.1126/science.1187303"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.org/dc/terms/identifier"doi:10.1126/science.1187303"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Ermler U."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Ermler U."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Michel H."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Michel H."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Warkentin E."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Warkentin E."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Xie H."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Xie H."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Buschmann S."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Buschmann S."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Langer J.D."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/author"Langer J.D."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/pages"327-330"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/pages"327-330"xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/title"The structure of cbb3 cytochrome oxidase provides insights into proton pumping."xsd:string
http://purl.uniprot.org/citations/20576851http://purl.uniprot.org/core/title"The structure of cbb3 cytochrome oxidase provides insights into proton pumping."xsd:string