||In our previous studies on modeling methyl transfer protein, Ada protein, we found that zinc complexes of tri(2-thiophenyl)phosphine (PS3), (A), have similar methyl transfer behavior as its biological counter part.|
In order to probe the role of zinc in methylation process, we used tin and cadmium in model study to compare their chemistry relative to that of zinc. We found that all three metal complexes have similar chemistry and assume similar dimeric anion structure. For example, [Cd(PS3)]22-(1) and [Cd(SiPS3)]22-(2) have been successfully characterized crystallographically to possess the same structure as zinc dimer (A). However , in attempt to crystallize the tin analogue, the accidental oxidation product [SnIV(OH)2(SiPS3)]2, (5), was obtained. Its crystal structure gave clue to the mechanism of oxidation of the original tin dimer.
The reactions with alkylating reagent of (1) have been compared with those of zinc dimer (A), and we found that the metal (Zn or Cd) center causes the dimers to produce different degree of methylation products toward different alkylating reagents. For the reactions with CH3I, the different degree of methylation between Cd and Zn dimers shows that the presence of zinc center has higher methylation selectivity and weaker reactivity.