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Atypical features of thermus thermophilus succinate:quinone reductase

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Show simple item record Kolaj-Robin, Olga Noor, Mohamed R. O'Kane, Sarah R Baymann, Frauke Soulimane, Tewfik 2013-02-11T11:22:17Z 2013-02-11T11:22:17Z 2013
dc.description peer-reviewed en_US
dc.description.abstract The Thermus thermophilus succinate:quinone reductase (SQR), serving as the respiratory complex II, has been homologously produced under the control of a constitutive promoter and subsequently purified. The detailed biochemical characterization of the resulting wild type (wt-rcII) and His-tagged (rcII-His8-SdhB and rcII-SdhB-His6) complex II variants showed the same properties as the native enzyme with respect to the subunit composition, redox cofactor content and sensitivity to the inhibitors malonate, oxaloacetate, 3-nitropropionic acid and nonyl-4-hydroxyquinoline-N-oxide (NQNO). The position of the His-tag determined whether the enzyme retained its native trimeric conformation or whether it was present in a monomeric form. Only the trimer exhibited positive cooperativity at high temperatures. The EPR signal of the [2Fe-2S] cluster was sensitive to the presence of substrate and showed an increased rhombicity in the presence of succinate in the native and in all recombinant forms of the enzyme. The detailed analysis of the shape of this signal as a function of pH, substrate concentration and in the presence of various inhibitors and quinones is presented, leading to a model for the molecular mechanism that underlies the influence of succinate on the rhombicity of the EPR signal of the proximal ironsulfur cluster. en_US
dc.language.iso eng en_US
dc.publisher Public Library of Science en_US
dc.relation.ispartofseries PLoS One;8(1), e53559
dc.subject quinone reductase en_US
dc.subject SQR en_US
dc.title Atypical features of thermus thermophilus succinate:quinone reductase en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.contributor.sponsor SFI en_US
dc.contributor.sponsor IRCSET en_US
dc.contributor.sponsor French National Center for Scientific Research en_US
dc.relation.projectid BICF685 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1431868

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