Reaction of Fe3(CO)12 with octreotide--chemical, electrochemical and biological investigations.

In search for peptidic [FeFe] hydrogenase mimics, the cyclic disulfide Sandostatin (R) (octreotide) was allowed to react with Fe-3(CO)(12). An octreotide-Fe-2(CO)(6) complex was isolated and characterized spectroscopically as well as by elemental and thermochemical analysis. The complex catalyzes the electrochemical reduction of H+ to H-2. It is suggested by radioligand binding assays that the complex retains much of the binding affinity for the somatostatin hsst(1-5) receptors of octreotide.