RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/25274631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25274631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25274631http://www.w3.org/2000/01/rdf-schema#comment"Two critical cysteine residues in the copper-A site (Cu(A)) on subunit II (CoxB) of bacterial cytochrome c oxidase lie on the periplasmic side of the cytoplasmic membrane. As the periplasm is an oxidizing environment as compared with the reducing cytoplasm, the prediction was that a disulfide bond formed between these cysteines must be eliminated by reduction prior to copper insertion. We show here that a periplasmic thioredoxin (TlpA) acts as a specific reductant not only for the Cu(2+) transfer chaperone ScoI but also for CoxB. The dual role of TlpA was documented best with high-resolution crystal structures of the kinetically trapped TlpA-ScoI and TlpA-CoxB mixed disulfide intermediates. They uncovered surprisingly disparate contact sites on TlpA for each of the two protein substrates. The equilibrium of CoxB reduction by TlpA revealed a thermodynamically favorable reaction, with a less negative redox potential of CoxB (E'0 = -231 mV) as compared with that of TlpA (E'0 = -256 mV). The reduction of CoxB by TlpA via disulfide exchange proved to be very fast, with a rate constant of 8.4 × 10(4) M(-1) s(-1) that is similar to that found previously for ScoI reduction. Hence, TlpA is a physiologically relevant reductase for both ScoI and CoxB. Although the requirement of ScoI for assembly of the Cu(A)-CoxB complex may be bypassed in vivo by high environmental Cu(2+) concentrations, TlpA is essential in this process because only reduced CoxB can bind copper ions."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M114.607127"xsd:string
http://purl.uniprot.org/citations/25274631http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.607127"xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Capitani G."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Capitani G."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Hennecke H."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Hennecke H."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Glockshuber R."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Glockshuber R."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Scharer M.A."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Scharer M.A."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Quade N."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Quade N."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Abicht H.K."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Abicht H.K."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Mohorko E."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Mohorko E."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Ledermann R."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/author"Ledermann R."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/25274631http://purl.uniprot.org/core/name"J Biol Chem"xsd:string