title: Metal binding ability of cysteine-rich peptide domain of ZIP13 Zn2+ ions transporter.
abstract: The coordination modes and thermodynamic stabilities of the complexes of the cysteine-rich N-terminal domain fragment of the ZIP13 zinc transporter (MPGCPCPGCG-NH(2)) with Zn(2+), Cd(2+), Bi(3+), and Ni(2+) have been studied by potentiometric, mass spectrometric, NMR, CD, and UV-vis spectroscopic methods. All of the studied metals had similar binding modes, with the three thiol sulfurs of cysteine residues involved in metal ion coordination. The stability of the complexes formed in solution changes in the series Bi(3+) ≫ Cd(2+) > Zn(2+) > Ni(2+), the strongest being for bismuth and the weakest for nickel. The N-terminal fragment of the human metalothionein-3 (MDPETCPCP-NH(2)) and unique histidine- and cysteine-rich domain of the C-terminus of Helicobacter pyroli HspA protein (Ac-ACCHDHKKH-NH(2)) have been chosen for the comparison studies. It confirmed indirectly which groups were the anchoring ones of ZIP13 domain. Experimental data from all of the used techniques and comparisons allowed us to propose possible coordination modes for all of the studied ZIP13 complexes.
authors.affiliation: Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
authors.forename: Slawomir
authors.initials: S
authors.lastname: Potocki
authors.forename: Magdalena
authors.initials: M
authors.lastname: Rowinska-Zyrek
authors.forename: Daniela
authors.initials: D
authors.lastname: Valensin
authors.forename: Karolina
authors.initials: K
authors.lastname: Krzywoszynska
authors.forename: Danuta
authors.initials: D
authors.lastname: Witkowska
authors.forename: Marek
authors.initials: M
authors.lastname: Luczkowski
authors.forename: Henryk
authors.initials: H
authors.lastname: Kozlowski
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D001729:Bismuth / Q000737:chemistry; D002104:Cadmium / Q000737:chemistry; D027682:Cation Transport Proteins / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry; D016480:Helicobacter pylori / Q000737:chemistry; D006801:Humans; D007477:Ions / Q000737:chemistry; D009532:Nickel / Q000737:chemistry; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification; D013816:Thermodynamics; D015032:Zinc / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D006360:Heat-Shock Proteins; C113725:HspA protein, bacteria; D007477:Ions; D009942:Organometallic Compounds; D010455:Peptides; C521172:SLC39A13 protein, human; D002104:Cadmium; D009532:Nickel; D015032:Zinc; D003545:Cysteine; D001729:Bismuth