Interactions of Zn(II) ions with three His-containing peptide models of histone H2A

 
This item is provided by the institution :
University of Ioannina
Repository :
Repository of UOI Olympias
see the original item page
in the repository's web site and access all digital files if the item*
share



2004 (EN)
Interactions of Zn(II) ions with three His-containing peptide models of histone H2A (EN)

Mylonas, M. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Mylonas, M. (EN)

The interactions of Zn(II) ions with the blocked hexapeptide models -TESHHK-, -TASHHK- and -TEAHHK- of the -ESHH- motif of the C-terminal of histone H2A were studied by using potentiometric and H-1-NMR techniques. The first step of these studies was to compare the pK(a) values of the two His residues inside each hexapeptide calculated by potentiometric or H-1-NMR titrations. Hereafter, the potentiometric titrations in the pH range 5-11 suggest the formation of several monomeric Zn(II) complexes. It was found that all hexapeptides bind to Zn(II) ions initially through both imidazole nitrogens in weakly acidic and neutral solutions forming slightly distorted octahedral complexes. At higher pH values, the combination of potentiometric titrations and one and two dimensional NMR suggested no amide coordination in the coordination sphere of Zn(II) ions. Obviously, these studies support that the -ESHH- sequence of histone H2A is a potential binding site for Zn(II) ions similarly with the Cu(II) and Ni(II) ions, presented in previous papers. (EN)

nuclear magnetic-resonance (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Bioinorg Chem Appl (EN)

English

2004

<Go to ISI>://000224303000009



*Institutions are responsible for keeping their URLs functional (digital file, item page in repository site)