Mercury(II) binding to metallothioneins: Variables governing the formation and structural features of the mammalian Hg-MT species

Àngels Leiva-Presa, Mercè Capdevila, Pilar Gonàles-Duarte

Research output: Contribution to journalArticleResearchpeer-review

24 Citations (Scopus)

Abstract

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-αMT and Zn3-βMT 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.
Original languageEnglish
Pages (from-to)4872-4880
JournalEuropean Journal of Biochemistry
Volume271
Issue number23-24
DOIs
Publication statusPublished - 1 Dec 2004

Keywords

  • α-metallothionein
  • β-metallothionein
  • Mercury(II) binding
  • Mercury-metallothionein
  • Metallothionein

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