Site-directed mutagenesis of five conserved residues of subunit I of the cytochrome cbb(3) oxidase in Rhodobacter capsulatus

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dc.authorid0000-0001-5901-6750en_US
dc.authorid0000-0001-6262-2866en_US
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorGürel, Ekrem
dc.contributor.authorWatmough, Nicholas J.
dc.contributor.authorMandacı, Sevnur
dc.date.accessioned2021-06-23T19:19:53Z
dc.date.available2021-06-23T19:19:53Z
dc.date.issued2007
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractCytochrome ebb.; oxidase is a member of the heme-copper oxidase superfamily that catalyses the reduction of molecular oxygen to the water and conserves the liberated energy in the form of a proton gradient. Comparison of the amino acid sequences of subunit I from different classes of heme-copper oxidases showed that transmembrane helix VIII and the loop between transmembrane helices IX and X contain five highly conserved polar residues; Ser333, Ser340, Thr350, Asn390 and Thr394. To determine the relationship between these conserved amino acids and the activity and assembly of the cbb(3); oxidase in Rhodobacter capsulatus, each of these five conserved amino acids was substituted for alanine by site-directed mutagenesis. The effects of these mutations on catalytic activity were determined using a NADI plate assay and by measurements of the rate of oxygen consumption. The consequence of these mutations for the structural integrity of the cbb(3) oxidase was determined by SDS-PAGE analysis of chromatophore membranes followed by TNBZ staining. The results indicate that the Asn390Ala mutation led to a complete loss of enzyme activity and that the Ser333Ala mutation decreased the activity significantly. The remaining mutants cause a partial loss of catalytic activity. All of the mutant enzymes, except Asn390Ala, were apparently correctly assembled and stable in the membrane of the R. capsulatus.en_US
dc.identifier.endpage707en_US
dc.identifier.issn1225-8687
dc.identifier.issue5en_US
dc.identifier.pmid17927903en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage697en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12491/6020
dc.identifier.urihttps://doi.org/10.5483/BMBRep.2007.40.5.697
dc.identifier.volume40en_US
dc.identifier.wosWOS:000249823600013en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorÖztürk, Mehmet
dc.institutionauthorGürel, Ekrem
dc.language.isoenen_US
dc.publisherSpringer Singapore Pte Ltden_US
dc.relation.ispartofJournal Of Biochemistry And Molecular Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCytochrome cbb(3)-type Oxidase Activityen_US
dc.subjectRespiration and Site-directed Mutagenesisen_US
dc.subjectRhodobacter Capsulatusen_US
dc.titleSite-directed mutagenesis of five conserved residues of subunit I of the cytochrome cbb(3) oxidase in Rhodobacter capsulatusen_US
dc.typeArticleen_US

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