Expression and Purification of Recombinant Metalloproteins

Although many metalloproteins are essential for life they are very often only found in minute amounts.  In order to provide sufficient quantities for characterization or for use as commercial products, metalloproteins are often expressed in heterologous systems. In our laboratory we have state-of-art facilities for cloning, expression (e.g. by high cell density fed-batch fermentation) and purification of recombinant metallo­proteins. We have developed high-yield bacterial expression systems and purification (HPLC) strategies for a number of important metalloproteins, e.g. tryptophan hydroxylase, iron-sulfur proteins, cytochrome c4, plastocyanin and blue copper nitrite reductase. Current focus is on development of expression systems for new metalloproteins and strategies for production of isotope-depleted and isotope-enriched/labelled metallo­proteins.

If you have any questions or comments on this research programme please contact Hans E. Mølager Christensen;