Abstract
Four new thioimidazolylborate-zinc functionalized thiolate complexes have been synthesized. Their structure determinations reveal intramolecular X–H⋯S (X
=
O/N) hydrogen-bonding interactions. The influence of these hydrogen bonding on the methylation of the thiolate ligands is evident from the fact that the rate of methylation for these complexes is reduced ca. 2 orders of magnitude when compared to that of their non-hydrogen bonding-containing analogue.
A series of new thioimidazolylborate zinc thiolate complexes Tti
xyl
ZnSR (
2)–(
5) (where R
=
C
6H
4-
o-OH, C
6H
4-
o-CH
2OH, C
6H
4-
o-NH
2, and C
6H
4-
p-OH, respectively) have been synthesized and characterized as structural and functional models of the active site of the
Ada repair protein. Structural determination of complexes
2–
4 reveals intramolecular N/O–H⋯S hydrogen-bonding interactions. The influence of these hydrogen bonding interactions on the methylation of the thiolate ligands is evident from the fact that the rate of methylation for these complexes is reduced ca. 2 orders of magnitude compared to that found in the case of the non-hydrogen bonding-containing complex, Tti
xyl
ZnSC
6H
5 (
1).