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Linking NrfD/PsrC-like architecture to energy conservation

2026-05Artigo científico Acesso aberto
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dc.contributor.authorManteigas, Gonçalo
dc.contributor.authorCatarino, Teresa
dc.contributor.authorVicente, João B.
dc.contributor.authorDuarte, Américo G.
dc.contributor.authorPereira, Inês A.C.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblWiley-Blackwell
dc.date.accessioned2026-05-15T13:16:01Z
dc.date.available2026-05-15T13:16:01Z
dc.date.issued2026-05
dc.descriptionPublisher Copyright: © 2026 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
dc.description.abstractThe QrcABCD quinone reductase complex is an electrogenic complex present in sulfate-reducing bacteria of the Desulfobacterota phylum. It operates as a cytochrome c3:menaquinone oxidoreductase involved in electron transfer from periplasmic hydrogen or formate oxidation to the menaquinone (MK) pool. Two proteins in this complex, QrcC and QrcD, form a redox dimer (QrcCD) responsible for MK reduction coupled to proton uptake from the cytoplasm. QrcD belongs to the NrfD/PsrC family, and homologs are found in many bacterial redox complexes in different bioenergetic contexts. In this work a homologous overexpression system for QrcABCD was established in Nitratidesulfovibrio vulgaris Hildenborough and used to produce variants with changes in key amino acids proposed to be involved in energy conservation. Growth studies of the modified strains combined with activity assays with isolated protein variants reconstituted in proteoliposomes revealed the essential role of key amino acids involved in the MK-binding site on the P-side of the membrane, and as part of a proposed proton uptake channel from the cytoplasm to the MK-binding site. The results support the proposed model for energy conservation where, upon formate or hydrogen oxidation, QrcABCD is involved in a redox-loop mechanism with another membrane complex, generating pmf by proton and electron uptake from different sides of the membrane, without active proton pumping.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent13
dc.format.extent2671639
dc.identifier.doi10.1002/pro.70557
dc.identifier.issn0961-8368
dc.identifier.otherPURE: 162298423
dc.identifier.otherPURE UUID: 129ac8de-acc0-4de4-a024-29e93ce55122
dc.identifier.otherScopus: 105035265382
dc.identifier.otherPubMed: 41949213
dc.identifier.otherPubMedCentral: PMC13059093
dc.identifier.otherWOS: 001734864900001
dc.identifier.otherORCID: /0000-0003-3855-5231/work/214827036
dc.identifier.urihttp://hdl.handle.net/10362/203136
dc.identifier.urlhttps://www.scopus.com/pages/publications/105035265382
dc.identifier.urlhttps://www.webofscience.com/wos/woscc/full-record/WOS:001734864900001
dc.language.isoeng
dc.peerreviewedyes
dc.subjectAnaerobic respiration
dc.subjectEnergy conservation
dc.subjectMembrane complex
dc.subjectNrfD/PsrC family
dc.subjectRedox loop
dc.subjectSulfate reduction
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectSDG 7 - Affordable and Clean Energy
dc.titleLinking NrfD/PsrC-like architecture to energy conservationen
dc.title.subtitleFunctional residues in the quinone reactive QrcABCD complex of sulfate-reducing bacteriaen
dc.typejournal article
degois.publication.firstPage1
degois.publication.issue5
degois.publication.lastPage13
degois.publication.titleProtein Science
degois.publication.volume35
dspace.entity.typePublication
rcaap.rightsopenAccess

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