http://purl.uniprot.org/citations/31888984 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/31888984 | http://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/31888984 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1915013117"xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Liu B."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Li J."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Li J.'"xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Liu L."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Xu J."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Zhu J."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Ding Z."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Zhou A."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Gennis R.B."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/author | "Yi S.M."xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
http://purl.uniprot.org/citations/31888984 | http://purl.uniprot.org/core/pages | "872-876"xsd:string |
http://purl.uniprot.org/citations/31888984 | http://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/31888984 | http://purl.uniprot.org/core/volume | "117"xsd:string |
http://purl.uniprot.org/citations/31888984 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31888984 |
http://purl.uniprot.org/citations/31888984 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31888984 |
http://purl.uniprot.org/uniprot/#_P34956-mappedCitation-31888984 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31888984 |
http://purl.uniprot.org/uniprot/#_P34957-mappedCitation-31888984 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31888984 |
http://purl.uniprot.org/uniprot/#_P34958-mappedCitation-31888984 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31888984 |