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• W1926029227 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 Zn 7 ‐MT, Zn 4 ‐αMT and Zn 3 ‐βMT proteins, at pH 7 and 3, with either HgCl 2 or Hg(ClO 4 ) 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." @default.
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• W1926029227 date "2004-12-01" @default.
• W1926029227 modified "2023-10-18" @default.
• W1926029227 title "Mercury(II) binding to metallothioneins. Variables governing the formation and structural features of the mammalian Hg-MT species" @default.
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• W1926029227 doi "https://doi.org/10.1111/j.1432-1033.2004.04456.x" @default.
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