Proton input channel of cytochrome cbb(3) type oxidase in Rhodobacter capsulatus

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dc.authorid0000-0002-4095-6619en_US
dc.authorid0000-0001-6906-5257
dc.contributor.authorYıldız, Gülgez Gökçe
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorDaldal, Fevzi
dc.date.accessioned2021-06-23T19:27:43Z
dc.date.available2021-06-23T19:27:43Z
dc.date.issued2011
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.descriptionEuropean Biotechnology Congress -- SEP 28-OCT 01, 2011 -- Istanbul, TURKEYen_US
dc.description.abstractCytochrome cbb3 is a distinct member of the superfamily of respiratory heme-copper oxidases responsible for catalyzing the reduction of oxygen to water. As in all A-family, B-family, and C-family this reaction drives proton pumping across the membrane. Mutagenesis studies on family A have identified two conserved proton input channels: D and K. The residues in the A-family that are located in the proton channels are not conserved in the C-family. Since the C-type oxygen reductases have been shown to pump protons, presence of proton-conducting channels is obvious in this family that play analogous roles to the D-channel and/or K-channel. In this work, sequences were aligned to identify functionally important residues which may form the proton channels in the C-family. The functional importance of the residues was tested by site-directed mutagenesis using the cbb3 oxidase from Rhodobacter capsulatus. Several residues proposed to be part of the putative K-channel had significantly reduced catalytic activity upon mutations: T272A, Y280F/Y281F, T319M, N346V, and Y374F. The results support the proposal that in the C-family only one channel, analogous to the K-channel in the A-type oxygen reductases, functions for the delivery of both catalytic and pumped protons.en_US
dc.description.sponsorshipEuropean Biotechnol Themat Network Assocen_US
dc.identifier.doi10.1016/j.copbio.2011.05.238
dc.identifier.endpageS80en_US
dc.identifier.issn0958-1669
dc.identifier.startpageS80en_US
dc.identifier.urihttps://doi.org/10.1016/j.copbio.2011.05.238
dc.identifier.urihttps://hdl.handle.net/20.500.12491/6879
dc.identifier.volume22en_US
dc.identifier.wosWOS:000295310800232en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.institutionauthorYıldız, Gülgez Gökçe
dc.institutionauthorÖztürk, Mehmet
dc.language.isoenen_US
dc.publisherCurrent Biology Ltden_US
dc.relation.ispartofCurrent Opinion In Biotechnologyen_US
dc.relation.publicationcategoryKonferans Öğesi - Uluslararası - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectRhodobacter Capsulatusen_US
dc.titleProton input channel of cytochrome cbb(3) type oxidase in Rhodobacter capsulatusen_US
dc.typeConference Objecten_US

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