Noncovalent Insertion Of Ferrocenes Into The Protein Shell Of Apo-ferritin

摘要

Apo-ferritin was used for the incorporation of functionalized ferrocene derivatives and the resulting composites were studied by means of single-crystal X-ray diffraction and electrochemical analysis, revealing a different incorporation behaviour of the ferrocenes governed by the functional group present.rnThe combination of naturally occuring proteins with artificial guest molecules has been investigated using a variety of approaches. These include the covalent binding of an artificial cofactor to the protein backbone, the anchoring using a natural host molecule or the noncovalent insertion of guests into a suitable protein cavity. The resulting composites allow the combination of features previously assigned to either low-molecular weight organic molecules or supramolecular protein moieties, thus creating systems helping to understand the interaction between proteins and organic molecules or potentially finding new applications in catalytic reactions.