The K-C channel in the cbb(3)-type respiratory oxygen reductase from rhodobacter capsulatus Is required for both chemical and pumped protons

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dc.authorid0000-0002-4095-6619en_US
dc.contributor.authorYıldız, Gülgez Gökçe
dc.contributor.authorGennis, Robert B.
dc.contributor.authorDaldal, Fevzi
dc.contributor.authorÖztürk, Mehmet
dc.date.accessioned2021-06-23T19:36:01Z
dc.date.available2021-06-23T19:36:01Z
dc.date.issued2014
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractThe heme-copper superfamily of proton-pumping respiratory oxygen reductases are classified into three families (A, B, and C families) based on structural and phylogenetic analyses. Most studies have focused on the A family, which includes the eukaryotic mitochondrial cytochrome c oxidase as well as many bacterial homologues. Members of the C family, also called the cbb(3)-type oxygen reductases, are found only in prokaryotes and are of particular interest because of their presence in a number of human pathogens. All of the heme-copper oxygen reductases require proton-conducting channels to convey chemical protons to the active site for water formation and to convey pumped protons across the membrane. Previous work indicated that there is only one proton-conducting input channel (the K-C channel) present in the cbb(3)-type oxygen reductases, which, if correct, must be utilized by both chemical protons and pumped protons. In this work, the effects of mutations in the KC channel of the cbb(3)-type oxygen reductase from Rhodobacter capsulatus were investigated by expressing the mutants in a strain lacking other respiratory oxygen reductases. Proton pumping was evaluated by using intact cells, and catalytic oxygen reductase activity was measured in isolated membranes. Two mutations, N346M and Y374F, severely reduced catalytic activity, presumably by blocking the chemical protons required at the active site. One mutation, T272A, resulted in a substantially lower proton-pumping stoichiometry but did not inhibit oxygen reductase activity. These are the first experimental data in support of the postulate that pumped protons are taken up from the bacterial cytoplasm through the K-C channel.en_US
dc.identifier.doi10.1128/JB.00005-14
dc.identifier.endpage1832en_US
dc.identifier.issn0021-9193
dc.identifier.issn1098-5530
dc.identifier.issue10en_US
dc.identifier.pmid24563037en_US
dc.identifier.scopus2-s2.0-84898888263en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1825en_US
dc.identifier.urihttps://doi.org/10.1128/JB.00005-14
dc.identifier.urihttps://hdl.handle.net/20.500.12491/7915
dc.identifier.volume196en_US
dc.identifier.wosWOS:000334674700005en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorYıldız, Gülgez Gökçe
dc.institutionauthorÖztürk, Mehmet
dc.language.isoenen_US
dc.publisherAmer Soc Microbiologyen_US
dc.relation.ispartofJournal Of Bacteriologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleThe K-C channel in the cbb(3)-type respiratory oxygen reductase from rhodobacter capsulatus Is required for both chemical and pumped protonsen_US
dc.typeArticleen_US

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