Many enzymes contain a metal ion as the catalytic center, which is commonly denoted as the active site. In the active site, the metal ion is attached to the functional groups of several specific amino acids, for instance to imidazole groups of histidine residues. In biomimetics we try to make low-molecular weight complexes as models for the active site of a specific enzyme, with the aim to gain insight in the structure of the enzyme, or in order to mimic the function of the enzyme.

In a project focussing on the enzyme hydrogenase, dinuclear iron-nickel coordination compounds are designed, prepared and characterized. These complexes serve as model compounds in obtaining insight in the relation between the structure of the active site of hydrogenase and its function (hydrogen activation). The aim is to develop novel complexes that can be used as catalysts for the electrocatalytic production of dihydrogen from protons.

In another project, we try to mimic linear molecular motors such as myosin to produce unidirectional motion of single molecules. Whereas in natural systems ATP hydrolysis is the source of energy that promote the motion, we use light to trigger hopping of ruthenium complexes on model membranes, and biased Brownian motion to achieve unidirectionality.

More information on the possible research topics in biomimetics can be found in the 'related projects' tab.