Events

"Heterobimetallic protein cofactors:  Natures tool for small-molecule activation"

Hannah Shafaat, Max Planck Institute for Energy Conversion

Nature has devised complex protein systems to perform challenging chemical reactions, including energy storage and respiration.  A majority of these proteins contain metal ions, and a substantial subset relies on multiple metal centers in their active sites.  In this way, cofactors are finely tuned for a particular purpose.  We have carried out extensive spectroscopic investigation of two heterobimetallic proteins that carry out distinct catalytic reactions, from proton reduction to substrate oxidation.1-3  Complementary experiments on model compounds and application of high-level calculations provide insight into structure and catalytic mechanisms.4,5  These results will be discussed in the context of understanding Natures design principles for creating highly active metalloenzymes.

Selected References:
(1)    Shafaat, H.; Rdiger, O.; Ogata, H.; Lubitz, W. BBA - Reviews on Bioenergetics 2013, in press.  DOI:  10.1016/j.bbabio.2013.01.015.
(2)    Griese, J.; Roos, K.; Cox, N.; Shafaat, H. S.; Branca, R. M. M.; Lehtioe, J.; Graslund, A.; Lubitz, W.; Siegbahn, P. E. M.; Hoegbom, M. Submitted to Nature Chemical Biology 2013.
(3)    Shafaat, H. S.; Cox, N. J. Am. Chem. Soc. 2013, in preparation.
(4)    Shafaat, H. S.; Weber, K.; Petrenko, T.; Neese, F.; Lubitz, W. Inorg. Chem. 2012, 51, 11787.
(5)    Weber, K.; Krmer, T.; Shafaat, H. S.; Weyhermuller, T.; Bill, E.; van Gastel, M.; Neese, F.; Lubitz, W. J. Am. Chem. Soc. 2012, 134, 20745.

Hosted by Jonathan Owen

Monday, February 25, 2013 at 4:00pm
Room 209 Havemeyer