title: Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example.
abstract: Increasing interest is focused on the role of zinc in biological systems. A rapidly growing family of DNA-binding proteins contains "zinc-fingers", where zinc is bound to cysteine or histidine residues. On the other hand zinc is able to displace calcium from its binding sites and in this way it may modify calcium-mediated cellular processes. In the present report dissociation rates of Zn2(+)- and Ca2(+)-complexes with 5-F-BAPTA, a widely used NMR-active calcium indicator, have been measured by two-dimensional 19F NMR exchange spectroscopic methods. The results show that the lifetime of the Zn2(+)-complex is more than five times longer than that of the Ca2(+)-complex. The longer lifetime, when combined with a higher thermodynamical stability of the Zn2+-complex, may explain why, in some cellular processes, Zn2+ can compete with Ca2+ in spite of a presumably high [Ca2+]/[Zn2+] free ion concentration ratio.
authors.affiliation: Institute of Biochemistry I., Semmelweis University School of Medicine, Budapest, Hungary.
authors.forename: P
authors.initials: P
authors.lastname: Csermely
authors.forename: P
authors.initials: P
authors.lastname: Sándor
authors.forename: L
authors.initials: L
authors.lastname: Radics
authors.forename: J
authors.initials: J
authors.lastname: Somogyi
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004355:Drug Stability; D004533:Egtazic Acid / Q000031:analogs & derivatives; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008667:Metalloproteins / Q000378:metabolism; D008962:Models, Theoretical; D011485:Protein Binding; D015032:Zinc / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D008667:Metalloproteins; D004533:Egtazic Acid; C039877:5,5'-difluoro-1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid; D015032:Zinc; D002118:Calcium