G. Parkin, The bioinorganic chemistry of zinc: synthetic analogues of zinc enzymes that feature tripodal ligands, CHEM COMMUN, (20), 2000, pp. 1971-1985
Zinc, as a constituent of more than 300 enzymes, plays essential roles in b
iological systems. The active sites of these enzymes feature a zinc center
attached to the protein backbone by three or four amino acid residues, the
nature of which influences the specific function of the enzyme. In order to
understand why different zinc enzymes utilize different amino acid residue
s at the active site, it is necessary to understand how, and why, the chemi
stry of zinc is modulated by its coordination environment. Answers to these
questions are being provided by a study of synthetic analogues of zinc enz
ymes, i.e. small molecules that resemble the enzyme active sites. This arti
cle provides an account of those studies that have specifically used tripod
al ligands to mimic the active site protein residues in an effort to ascert
ain the bioinorganic chemistry of zinc.