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With the aim of extending our knowledge on the reactionpathways of Zn-metallothionein (MT) and apo-MT speciesin the presence of Hg(II), we monitored the titration ofZn7-MT, Zn4-aMT and Zn3-bMT proteins, at pH 7 and 3,with either HgCl2or Hg(ClO4)2by CD and UV-vis spectr-oscopy. Detailed analysis of the optical data revealed thatstandard variables, such as the pH of the solution, thebinding ability of the counter-ion (chloride or perchlorate),and the time elapsedbetween subsequent additions ofHg(II)to the protein, play a determinant role in the stoichiometry,stereochemistry anddegree of folding of theHg-MT species.Despite the fact that the effect of these variables is unques-tionable, it is difficult to...
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Mercury(II) binding to metallothioneins Variables governing the formation and structural features of the mammalian Hg-MT species
