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• W52582688 abstract "Copper is essential for the correct assembly and function of the cytochrome c oxidase(CcO), thus for the efficient cellular respiration in both eukaryotes and prokaryotes. CcOassembly in the inner mitochondrial membrane space is a multi complicated procedure,depended on a number of co-factors and their synergic action. These co-factors are proteinscommissioned with the correct folding of the enzyme subunits and thetransport/incorporation of heme moieties and Cu ions to them.While the proteins involved in this multistep procedure are rather known, themechanisms of metal ion delivery and incorporation within the two active centers of CcO,CuA and CuB, still remain uncharted. The CuA center is a binuclear copper center, whosepart in the respiratory chain is spoted in electron transport from the active cytochrome c tothe catalytic CuB center of CcO. Efficient CuA assembly is crucial for the catalytic action ofthe entire enzyme. Several proteins have been characterized as essential factors for thetransport of Cu ions to the CuA center; however their exact molecular mechanism of actionstill remains obscure.In prokaryotes, two protein families have been suggested to be involved in the CuAassembly.The first includes proteins that bind Cu1+ ions through a potential conserved motifH(M)x10Mx21HxM (hypothetical proteins, Hyp1), while the second includes proteins of theSco family, whose exact role in CuA assembly as thioredoxins or copper chaperones iswidely debated.In this work, it is propesed that a new periplasmic protein (TtHyp1 or PCuAC)selectively inserts Cu1+ ions in the Cox2 subunit of the ba3-CcO of Thermus thermophilusresulting the formation of the physiological binuclear TtCuA center, as well as that the Scoprotein of the organism (TtSco1) is not able to transfer metal ions to the CuA center; insteadit acts rather like a thio-disulfide reductase adjusting the proper redox state of the CuAcysteine residues. Proteins PCuAC, TtSco1 and TtCuA were over-expressed, purified andsubjected to biochemical characterization, while their Cu binding capability and their interse interactions were studied through NMR and UV spectroscopy. In addition, PCuAC wasstructurally characterized through NMR in its apo and Cu(I) form. The role of Sco proteinswas further investigated through genome based analysis and the expression andbiochemical characterization of a new protein, PpSco1/cytc from Pseudomonas putida, aunique bacterial protein consisted on two domains, a Sco1 and a cytc domain,presumptively connecting the role of Sco proteins with the suggested theory of thioredoxinaction.A novelty in this work was the methodological aspect of the multiple cloning of thetarget genes with a new cloning technology (Gateway) combined with site specificrecombination into multiple expression plasmid vectors and the development of a highthroughput technique for parallel expression/purification tests.The infra work provides new insights to the CuA center assembly molecularmechanism of the prokaryotic CcO, supporting a new model for the particular procedureand also subscripts for the decipherment of the complicated role of Sco proteins." @default.
• W52582688 created "2016-06-24" @default.
• W52582688 creator A5042146287 @default.
• W52582688 date "2008-09-22" @default.
• W52582688 modified "2023-09-27" @default.
• W52582688 title "Έκφραση και χαρακτηρισμός ανασυνδυασμένων πρωτεϊνών μεταφοράς χαλκού για τη μελέτη της συνεργικής τους δράσης κατά το τελευταίο στάδιο της αναπνευστικής αλυσίδας του μιτοχονδρίου" @default.
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