Our research projects
Artificial activation of enzymes
The groups main focus is on [FeFe] hydrogenases (HydA), for which we recently developed a method by which synthetic analogues of the metalorganic cofactor can be introduced either directly in the apo-form of the enzyme or into the maturation machinery. We are now taking advantage of this method to study the mechanism and maturation process of the enzyme, as well as developing technological devices were HydA replaces platinum for electro- and photochemical hydrogen gas production.
In a second project line we are studying the di-metal (-tyrosyl-radical) sites found in Class I ribonucleotide reductases (RNR), in order to unravel the factors governing the metal selectivity of its different subclasses denoted Ia (Fe/Fe), Ib (Mn/Mn) and Ic (Mn/Fe) respectively. The work includes studies of mutants, maturase proteins and potential metal-chaperone proteins.
In parallel we design and prepare artificial enzymes by employing synthetic peptides and scaffold proteins. Particular interest is placed on hydrogenase mimics because of their enormous potential in the field of artificial photosynthesis and the production of a “solar fuel”.