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http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/7.-.-.-
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/7.1.1.-
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/7.1.-.-
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal center composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB)."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"While most bacterial enzymes consist of only 3-4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"The reduction of O2 to water is accompanied by the extrusion of four protons."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2000/01/rdf-schema#comment"The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist."xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#prefLabel"cytochrome-c oxidase"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7657607
http://purl.uniprot.org/enzyme/7.1.1.9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13787372
http://purl.uniprot.org/enzyme/7.1.1.9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13787373
http://purl.uniprot.org/enzyme/7.1.1.9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18353797
http://purl.uniprot.org/enzyme/7.1.1.9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7619069
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome oxidase"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"Warburg's respiratory enzyme"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"complex IV (mitochondrial electron transport)"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome a3"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome aa3"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome ba3"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome bb3"xsd:string
http://purl.uniprot.org/enzyme/7.1.1.9http://www.w3.org/2004/02/skos/core#altLabel"cytochrome caa3"xsd:string