dr. Peter-Leon Hagedoorn

T: +31 15 27 82334
E: P.L.Hagedoorn@remove-this.tudelft.nl


Room C2.
Van der Maasweg 9
2629 HZ Delft
The Netherlands

 

Read more about Peter-Leon here.

Metallo-proteins

Life requires some 20 odd elements, and many biocatalysts mandatorily need metal ions for their biological activity. Since present-day life is the product of evolution one can legitimately ask the question: why does a cell go for a particular chemistry. In this framework we are interested in structure-mechanism relations of metalloproteins, in particular metalloenzymes, as biological coordination complexes in a variety of environments. We go after high space-time resolution in the characterization of atomic structural changes on a pre-steady state scale. We have a preference for redox-active transition ions with their spectroscopically interesting colors and magnetic properties. To illustrate this quest the picture zooms in into the structure of a hyperthermophilic ferritin where hard Lewis acid side groups collaborate with a radical-forming tyrosine to catalytically oxidize essential iron ions en route to storage in an intra-protein cavity. We also employ and modify metalloproteins with a view to putative industrial or medical applications. The ferritin is for example usable in water purification.

Generic enzyme assays

Enzymes are superior catalysts of chemical reactions. In order to measure the performance of an enzyme, usually, changes in substrate or product concentrations are measured. This means that, in principle, for every enzyme and every substrate/product a different assay has to be developed. This is currently a bottleneck in high-throughput approaches to systematically engineer industrially useful biocatalysts.

Calorimetry offers a way to bypass the need to measure substrate/product levels, but instead measure the heat that is being developed (or consumed) during a chemical reaction. Current state-of-the-art microcalorimeters are able to accurately measure the small heat changes during enzyme catalysed reactions. However, the proper analysis to obtain accurate kinetic parameters (Vmax, Km, KI) for any enzyme still requires development.

 

© 2017 TU Delft

Metamenu