| First Author | Leiva-Presa A | Year | 2004 |
| Journal | Eur J Biochem | Volume | 271 |
| Issue | 23-24 | Pages | 4872-80 |
| PubMed ID | 15606775 | Mgi Jnum | J:98028 |
| Mgi Id | MGI:3576972 | Doi | 10.1111/j.1432-1033.2004.04456.x |
| Citation | Leiva-Presa A, et al. (2004) Mercury(II) binding to metallothioneins. Variables governing the formation and structural features of the mammalian Hg-MT species. Eur J Biochem 271(23-24):4872-80 |
| abstractText | With the aim of extending our knowledge on the reaction pathways of Zn-metallothionein (MT) and apo-MT species in the presence of Hg(II), we monitored the titration of Zn7-MT, Zn4-alphaMT and Zn3-betaMT proteins, at pH 7 and 3, with either HgCl2 or Hg(ClO4)2 by CD and UV-vis spectroscopy. Detailed analysis of the optical data revealed that standard variables, such as the pH of the solution, the binding ability of the counter-ion (chloride or perchlorate), and the time elapsed between subsequent additions of Hg(II) to the protein, play a determinant role in the stoichiometry, stereochemistry and degree of folding of the Hg-MT species. Despite the fact that the effect of these variables is unquestionable, it is difficult to generalize. Overall, it can be concluded that the reaction conditions [pH, time elapsed between subsequent additions of Hg(II) to the protein] affect the structural properties more substantially than the stoichiometry of the Hg-MT species, and that the role of the counter-ion becomes particularly apparent on the structure of overloaded Hg-MT. |
