Copper(II) complexes of tetrapeptides containing cysteinyl and histidinyl residues

It is becoming increasingly apparent that the coordination chemistry of oligopeptides with Cys-X-Y-Cys and His-X-Y-Cys sequences (X, Y = variable amino acid residues) is an important theme in transition metal and bioinorganic chemistry(1,2). The Cys-X-Y-Cys sequence is often encountered in the metal binding site of several metalloproteins, such as iron–sulfur proteins, e.g. rubredoxins(3) and ferrodoxins(4), high potential iron–sulfur proteins(5), metallothioneins(6), zinc proteins(7) etc. The amino acid sequence His-X-Y-Cys is also of bioinorganic importance since it has been found in the active site of copper(8), iron–sulfur(9) and zinc(10) proteins. We are currently seeking to develop the area of transition metal/Cys-X-Y-Cys and His-X-Y-Cys peptide interactions(11,12); our goals are: (i) to elucidate the role of these sequences in the biological activity and mechanism of action of the above metallobiomolecules, and (ii) to find possible new and more effective agents for the elimination of heavy metals from the human organism or from contaminated waste waters. Here we report the preparation and preliminary characterization of copper(II) complexes of tetrapeptide ligands containing the Cys-X-Y-Cys and His-X-Y-Cys sequences. This revised version was published online in June 2006 with corrections to the Cover Date.