Crystallographic studies of natural, mutant and artificial metalloenzymes and metalloproteins

We want to use high-resolution crystallography to continue or do new fundamental research on: 1) the oxygen-sensitivity of metalloenzymes and metalloproteins; 2)
maturation proteins involved in the biosynthesis of metal sites in hydrogenases and nitrogenase; 3) SAM radical enzymes; 4) the biological assembly of iron-sulfur
clusters; 5) the role of quinolinate synthase in NAD biosynthesis; 6) transduction of signals like oxygen and NO by Fe-S cluster-dependent transcriptional regulators.
Our main goal is to understand the structure-function relationships of these proteins and to decipher their mechanisms. More distant goals include the design and
production of improved enzymes, facilitating their use for biotechnological applications.