| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1312858 | Inorganica Chimica Acta | 2006 | 8 Pages |
A series of new thioimidazolylborate zinc thiolate complexes TtixylZnSR (2)–(5) (where R = C6H4-o-OH, C6H4-o-CH2OH, C6H4-o-NH2, and C6H4-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, TtixylZnSC6H5 (1).
Graphical abstractFour 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.Figure optionsDownload full-size imageDownload as PowerPoint slide
