Reaction of Fe3(CO)12 with octreotide-chemical, electrochemical and biological investigations
By Apfel, Ulf-Peter; Rudolph, Manfred; Apfel, Christina; Robl, Christian; Langenegger, Daniel; Hoyer, Daniel; Jaun, Bernhard; Ebert, Marc-Olivier; Alpermann, Theodor; Seebach, Dieter & Weigand, Wolfgang
Published in Dalton Trans.
The Royal Society of Chemistry
2010
Abstract
In search for peptidic [FeFe] hydrogenase mimics, the cyclic disulfide Sandostatin[registered sign] (octreotide) was allowed to react with Fe3(CO)12. An octreotide-Fe2(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 H2. It is suggested by radioligand binding assays that the complex retains much of the binding affinity for the somatostatin hsst1-5 receptors of octreotide.