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http://purl.uniprot.org/citations/31888984http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31888984http://www.w3.org/2000/01/rdf-schema#comment"Virtually all proton-pumping terminal respiratory oxygen reductases are members of the heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome c as a source of electrons, but a group of enzymes have evolved to directly oxidize membrane-bound quinols, usually menaquinol or ubiquinol. All of the quinol oxidases have an additional transmembrane helix (TM0) in subunit I that is not present in the related cytochrome c oxidases. The current work reports the 3.6-Å-resolution X-ray structure of the cytochrome aa3 -600 menaquinol oxidase from Bacillus subtilis containing 1 equivalent of menaquinone. The structure shows that TM0 forms part of a cleft to accommodate the menaquinol-7 substrate. Crystals which have been soaked with the quinol-analog inhibitor HQNO (N-oxo-2-heptyl-4-hydroxyquinoline) or 3-iodo-HQNO reveal a single binding site where the inhibitor forms hydrogen bonds to amino acid residues shown previously by spectroscopic methods to interact with the semiquinone state of menaquinone, a catalytic intermediate."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1915013117"xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Liu B."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Li J.'"xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Zhu J."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Ding Z."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Zhou A."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Gennis R.B."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/author"Yi S.M."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/pages"872-876"xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/title"Structure of the cytochrome aa3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site."xsd:string
http://purl.uniprot.org/citations/31888984http://purl.uniprot.org/core/volume"117"xsd:string
http://purl.uniprot.org/citations/31888984http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31888984
http://purl.uniprot.org/citations/31888984http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31888984
http://purl.uniprot.org/uniprot/#_P34956-mappedCitation-31888984http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31888984
http://purl.uniprot.org/uniprot/#_P34957-mappedCitation-31888984http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31888984
http://purl.uniprot.org/uniprot/#_P34958-mappedCitation-31888984http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31888984