Methylation of (2-methylethanethiol-bis-3,5-dimethylpyrazolyl)methane zinc complexes and coordination of the resulting thioether: relevance to zinc-containing alkyl transfer enzymes

Abstract

Methylation of the coordinated thiolate in pseudotetrahedral Zn complexes of the form [(L3S)ZnX] by a variety of alkylating agents appears to occur via a nondissociative route and the resulting thioether can remain coordinated to the metal center as it does in zinc dependent alkyl transfer enzymes such as the DNA repair protein, Ada, from Escherichia coli.