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 improve our understanding of structure-function relationships such as those determining oxygen sensitivity and oxygen-tolerance of Fe-S clustercontaining proteins, those involved in the catalysis of important biochemical reactions and those involved in Fe-S cluster-dependent signal transduction. More distant goals include the design and production of improved and/or artificial metalloenzymes, facilitating their use for biotechnological applications.