Hpn and Hpn-like are Helicobacter pylori cytoplasmic proteins involved in the homeostasis of nickel; this metal is required for the enzymes urease and Ni-Fe hydrogenase, essential for the bacterium colonization in the human stomach. While almost half of Hpn sequence consists of polyhistydyl repeats, Hpn-like protein is rich in glutamine residues. In order to shed light on the role of the consecutive His and Gln residues in metal-ion binding, the present investigation is focused on the N-terminal domain of Hpn-like protein. Cu(II) and Ni(II) complexes of peptide models were studied by means of different thermodynamic and spectroscopic techniques, as well as through molecular modeling computations.
Poly-His and poly-Gln sequences in bacterial proteins: tempting sites for metal ions to interact with
GUERRINI, Remo;REMELLI, Maurizio;
2013
Abstract
Hpn and Hpn-like are Helicobacter pylori cytoplasmic proteins involved in the homeostasis of nickel; this metal is required for the enzymes urease and Ni-Fe hydrogenase, essential for the bacterium colonization in the human stomach. While almost half of Hpn sequence consists of polyhistydyl repeats, Hpn-like protein is rich in glutamine residues. In order to shed light on the role of the consecutive His and Gln residues in metal-ion binding, the present investigation is focused on the N-terminal domain of Hpn-like protein. Cu(II) and Ni(II) complexes of peptide models were studied by means of different thermodynamic and spectroscopic techniques, as well as through molecular modeling computations.I documenti in SFERA sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.