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• W2028755044 endingPage "86" @default.
• W2028755044 startingPage "75" @default.
• W2028755044 abstract "CP12 is a small chloroplastic protein involved in the Calvin cycle that was shown to bind copper, a metal ion that is involved in the transition of CP12 from a reduced to an oxidized state. In order to describe CP12's copper-binding properties, copper-IMAC experiments and site-directed mutagenesis based on computational modelling, were coupled with top-down MS [electrospray-ionization MS and MS/MS (tandem MS)]. Immobilized-copper-ion-affinity-chromatographic experiments allowed the primary characterization of the effects of mutation on copper binding. Top-down MS/MS experiments carried out under non-denaturing conditions on wild-type and mutant CP12-Cu(2+) complexes then allowed fragment ions specifically binding the copper ion to be determined. Comparison of MS/MS datasets defined three regions involved in metal ion binding: residues Asp(16)-Asp(23), Asp(38)-Lys(50) and Asp(70)-Glu(76), with the two first regions containing selected residues for mutation. These data confirmed that copper ligands involved glutamic acid and aspartic residues, a situation that contrasts with that obtaining for typical protein copper chelators. We propose that copper might play a role in the regulation of the biological activity of CP12." @default.
• W2028755044 created "2016-06-24" @default.
• W2028755044 creator A5006684316 @default.
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• W2028755044 creator A5079905766 @default.
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• W2028755044 date "2009-03-13" @default.
• W2028755044 modified "2023-10-16" @default.
• W2028755044 title "Mapping of a copper-binding site on the small CP12 chloroplastic protein of <i>Chlamydomonas reinhardtii</i> using top-down mass spectrometry and site-directed mutagenesis" @default.
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• W2028755044 doi "https://doi.org/10.1042/bj20082004" @default.
• W2028755044 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19099541" @default.
• W2028755044 hasPublicationYear "2009" @default.
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