Ni²⁺ chemistry in pathogens--a possible target for eradication.
The survival of all urease and/or hydrogenase containing pathogens depends on the proper homeostasis of nickel. In the scope of this perspectives paper, details of Ni(2+) metabolism of Helicobacter pylori, a widespread stomach-ulcer causing bacterium, are described. Nickel binding proteins and thermodynamics of such metal complexes are discussed in detail and special focus is given to potential nickel binding sequences in this metal's chaperones and regulators. A list of potential Ni(2+) binding sites in various pathogens is presented, which points out numerous examples of nickel interactions that still need to be understood.
Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland. magdalena.rowinska-zyrek@chem.uni.wroc.pl.
Magdalena
M
Rowinska-Zyrek
Jolanta
J
Zakrzewska-Czerwinska
Anna
A
Zawilak-Pawlik
Henryk
H
Kozlowski
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D016480:Helicobacter pylori / Q000187:drug effects; D006639:Histidine / Q000737:chemistry; D006706:Homeostasis; D008670:Metals / Q000737:chemistry; D018832:Molecular Chaperones / Q000737:chemistry; D008969:Molecular Sequence Data; D009532:Nickel / Q000737:chemistry*; D011485:Protein Binding; D013276:Stomach Ulcer / Q000188:drug therapy; D013816:Thermodynamics; D014510:Urease / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008670:Metals; D018832:Molecular Chaperones; D006639:Histidine; D009532:Nickel; D014510:Urease