The importance of the ligand environment in determining chemistry at metal sites is well understood. As a result, the vast majority of ligand designs in enzyme modelling chemistry are aimed at tuning metal chemistry through rational selection of coordinating groups. In Nature, however, it is known that the microenvironment of the active site can also influence the function of metalloproteins through non-covalent interactions such as H-bonding. In order to elucidate this aspect of enzyme catalysis we have been exploring the effects of H-bond donors on substrate binding, and chemical properties relevant to hydrolysis and redox chemistry at the metal site(s). Metal complexes of ligands with a range of H-bonding groups displaying internal H-bonds with other metal-bound ligands will be presented. The chemical effects exerted by these groups will be discussed, as will potential applications. The magnitudes of some beneficial effects caused by the H-bonding microenvironments will be compared with those ‘traditionally’ obtained by manipulating the primary coordination sphere.
|Number of pages||1|
|Journal||ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY|
|Publication status||Published - 22 Aug 2004|