Book Description
Metalloenzymes make up approximately one third of all enzymes and catalyze a diverse range of reactions. Such enzymes include matrix metalloproteinases, carbonic anhydride, and the mononuclear non-heme iron(II) enzymes; all of which have been modeled using small molecular complexes to understand the structure and function. Symmetrical tripodal pseudopeptides were previously synthesized to model these enzymes, but they produced undesired complex polymers. Therefore, tert-butyl THB, a ligand with three tert-butyl histamines, was synthesized to produce a 1:1 metal/ligand binding mode. The tert-butyl THB ligand was confirmed by ESI-MS+ and NMR. In parallel, in order to accurately model more diverse active sites, such as those that contain two-histidines and one cysteine, two cysteines and one histidine, or two histidines and one carboxylate group, asymmetric ligands were synthesized which used the actual amino acid contained in the enzyme active site. These asymmetric ligands were partially synthesized and characterized, but require further development.
