Mutagenesis of tyrosine residues within helix VII in subunit I of the cytochrome cbb (3) oxidase from Rhodobacter capsulatus

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dc.authorid0000-0001-5901-6750en_US
dc.authorid0000-0001-6906-5257
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorWatmough, Nicholas J.
dc.date.accessioned2021-06-23T19:28:06Z
dc.date.available2021-06-23T19:28:06Z
dc.date.issued2011
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractThe cbb (3)-type oxidases are members of the heme-copper oxidase superfamily, distant by sequence comparisons, but sharing common functional characteristics. The cbb (3) oxidases are missing an active-site tyrosine residue that is absolutely conserved in all A and B-type heme-copper oxidases. This tyrosine is known to play a critical role in the catalytic mechanisms of A and B-type oxidases. The absence of this tyrosine in the cbb (3) oxidases raises the possibility that the cbb (3) oxidases utilize a different catalytic mechanism from that of the other members of the superfamily, or have this conserved residue in different helices. Recently sequence comparisons indicate that, a tyrosine residues that might be analogous to the active-site tyrosine in other oxidases are present in the cbb (3) oxidases but these tyrosines originates from a different transmembrane helix within the protein. In this research, three conserved tyrosine residues, Y294, Y308 and Y318, in helix VII were substituted for phenylalanine. Y318F mutant in the Rhodobacter capsulatus oxidase resulted in a fully assembled enzyme with nativelike structure and activity, but Y294F mutant is not assembled and have a catalytic activity. On the other hand, Y308F mutant is fully assembled enzyme with nativelike structure, but lacking catalytic activity. This result indicates that Y308 should be crucial in catalytic activity of the cbb (3) oxidase of R. capsulatus. These findings support the assumption that all of the heme-copper oxidases utilize the same catalytic mechanism and provide a residue originates from different places within the primary sequence for different members of the same superfamily.en_US
dc.identifier.doi10.1007/s11033-010-0437-z
dc.identifier.endpage3326en_US
dc.identifier.issn0301-4851
dc.identifier.issue5en_US
dc.identifier.pmid21107730en_US
dc.identifier.scopus2-s2.0-80052501914en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage3319en_US
dc.identifier.urihttps://doi.org/10.1007/s11033-010-0437-z
dc.identifier.urihttps://hdl.handle.net/20.500.12491/6952
dc.identifier.volume38en_US
dc.identifier.wosWOS:000290102100060en_US
dc.identifier.wosqualityQ2en_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 Oxidaseen_US
dc.subjectProton Pumping Channelsen_US
dc.subjectTyrosine-histidine Cross-linken_US
dc.subjectSite-directed Mutagenesisen_US
dc.titleMutagenesis of tyrosine residues within helix VII in subunit I of the cytochrome cbb (3) oxidase from Rhodobacter capsulatusen_US
dc.typeArticleen_US

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