Two conserved non-canonical histidines are essential for activity of the cbb (3)-type oxidase in Rhodobacter capsulatus

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dc.authorid0000-0001-6906-5257
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorMandacı, Sevnur
dc.date.accessioned2021-06-23T19:19:58Z
dc.date.available2021-06-23T19:19:58Z
dc.date.issued2007
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractCytochrome cbb (3) oxidase, a member of the heme-copper oxidase superfamily, catalyses the reduction of oxygen to water and generates a proton gradient. Cytochrome c oxidases are characterized by a catalytic subunit (subunit I) containing two hemes and one copper ion ligated by six invariant histidine residues, which are diagnostic of heme-copper oxidases in all type of the heme-copper oxidase superfamily. Alignments of the amino acid sequences of subunit I (FixN or CcoN) of the cbb (3)-type oxidases show that catalytic subunit also contains six non-canonical histidine residues that are conserved in all CcoN subunits of the cbb (3) oxidase, but not the catalytic subunits of other members of heme-copper oxidases superfamily. The function of these six CcoN-specific conserved histidines of cbb (3)-type oxidase in R. capsulatus is unknown. To analyze the contribution of the two invariant histidines of CcoN, H300 and H394, in activity and assembly of the Rhodobacter capsulatus cbb (3)-type oxidase, they were substituted for valine and alanine, respectively by site-directed mutagenesis. H300V and H394A mutations were analyzed with respect to their activity and assembly. It was found that H394A mutation led to a defect in the assembly of both CcoP and CcoO in the membrane, which results in almost complete loss of activity and that although the H300V mutant is normally assembled in the membrane and retain their stability, its catalytic activity is significantly reduced when compared with wild-type oxidase.en_US
dc.identifier.doi10.1007/s11033-006-9031-9
dc.identifier.endpage172en_US
dc.identifier.issn0301-4851
dc.identifier.issn1573-4978
dc.identifier.issue3en_US
dc.identifier.pmid17143652en_US
dc.identifier.scopus2-s2.0-34547165994en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage165en_US
dc.identifier.urihttps://doi.org/10.1007/s11033-006-9031-9
dc.identifier.urihttps://hdl.handle.net/20.500.12491/6035
dc.identifier.volume34en_US
dc.identifier.wosWOS:000248382800005en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorÖztürk, Mehmet
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofMolecular Biology Reportsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCytochrome cbb (3-)type Oxidase Activityen_US
dc.subjectRespirationen_US
dc.subjectRhodobacter Capsulatus and Site-Directed Mutagenesisen_US
dc.titleTwo conserved non-canonical histidines are essential for activity of the cbb (3)-type oxidase in Rhodobacter capsulatusen_US
dc.typeArticleen_US

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