Bioinorganic chemistry and spectroscopy
In my group we aim to elucidate the role of metal ions in biological systems. Examples include the function of metalloenzymes, how metal ions induce aggregation of proteins (relevant to e.g. Alzheimer's disease), or the binding of heavy metals to proteins (toxicity). We apply a variety of spectroscopic techniques and quantum chemistry methods to uncover structure and dynamics of metal sites in biomolecules - mainly proteins. This includes development and use of specialized techniques: perturbed angular correlation (PAC) of gamma rays and beta-NMR, which is a billion times more sensitive than conventional NMR spectroscopy. Part of the work is carried out at the large international facilities TRIUMF and CERN.
Recent publications include:
M. Stachura, S. Chakraborty, A. Gottberg, L. Ruckthong, Pecoraro V.L., Hemmingsen L. Direct observations of nanosecond exchange dynamics at a protein metal site J. Am. Chem. Soc., 2017, 139: 79-82
J.T. Pedersen, S.W. Chen, C.B. Borg, S. Ness, J.M. Bahl, N.H.H. Heegaard, C.M. Dobson, L. Hemmingsen, N. Cremades, K. Teilum Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing J. Am. Chem. Soc., 2016, 138, 3966-3969
Szunyogh D., Zsolokai H., Thulstrup P.W., Larsen F.H., Gyurcsik B., Christensen N.J., Stachura M., Hemmingsen L*., and Jancso A.* Specificity of the metalloregulator CueR for Monovalent metal ions: Possible functional role of a coordinated thiol? Angew. Chem. Int. Ed., 2015, 54, 15756–15761