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Nickel(II) binding to Cap43 protein fragments

Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Kowalik-Jankowska, Teresa and Costa, Max and Kozlowski, Henryk (2004) Nickel(II) binding to Cap43 protein fragments. Journal of Inorganic Biochemistry, Vol. 98 (6), p. 931-939. ISSN 0162-0134. Article.

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DOI: 10.1016/j.jinorgbio.2004.03.005


Cap43 protein has been tested for metal binding domains. The protein, specifically induced by nickel compounds in cultured human cells, had a new mono-histidinic motif consisting of 10 amino acids repeated three times in the C-terminus.
The 20-Ac-TRSRSHTSEG–TRSRSHTSEG (Thr341–Arg–Ser–Arg–Ser–His 346–Thr–Ser–Glu–Gly–Thr–Arg–Ser–Arg–Ser–His356 –Thr–Ser–Glu–Gly360 – peptide 1) and the 30–Ac-TRSRSHTSEG–TRSRSHTSEG–TRSRSHTSEG (Thr341 –Arg–Ser–Arg–Ser–His346 –Thr–Ser–Glu–Gly–Thr–Arg–Ser–Arg–Ser–His356 –Thr–Ser–Glu–Gly–Thr–Arg–Ser–Arg–Ser–His366 –Thr–Ser–Glu–Gly 370 – peptide 2) amino acids sequence has been analyzed as a site for Ni(II) binding.
A combined pH-metric and spectroscopic (UV–visible, CD, NMR) studies of Ni(II) binding to both fragments were performed. The 20-amino acid peptide can bind one and two metal ions while the 30-amino acid fragment one, two and three metal ions. At physiological pH, depending on the metal to ligand molar ratio, peptide 1 forms the Ni 2L species while peptide 2 the NiL, Ni2L and Ni3 L complexes where each metal ion is coordinated to the imidazole nitrogen atom of the histidine residue of the 10-amino acid fragment. Octahedral complexes at pH 8–9 and planar 4N complexes with (N Im , 3N ) bonding mode at pH above 9, are formed.
This work supports the existence of an interesting binding site at the COOH-terminal domain of the Cap43 protein.

Item Type:Article
ID Code:4813
Uncontrolled Keywords:Stability constants, spectroscopic study, Nickel(II) complexes, Cap43 fragments
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
Publisher:Elsevier Science
Deposited On:12 Nov 2010 12:38

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