Dresden 2009 – scientific programme
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BP: Fachverband Biologische Physik
BP 7: Poster I
BP 7.30: Poster
Monday, March 23, 2009, 17:45–20:00, P3
Oxygenation interactions of the metalloprotein hemocyanin in aqueous solution revealed by core-level spectroscopy — •Daniel Panzer1, Christian Beck2, Jochen Maul1, Nora Bergmann3, Gerhard Schönhense1, Heinz Decker2, and Emad Aziz4 — 1Institut für Physik, Staudinger Weg 7, Johannes Gutenberg-Universität, D-55099 Mainz — 2Institut für Molekulare Biophysik, Welderweg 26, Johannes Gutenberg-Universität, D-55099 Mainz — 3Max-Delbrück-Center for Molecular Medicine, D-13125 Berlin-Buch — 4BESSY GmbH, Albert-Einstein-Strasse 15, D-12489 Berlin
Active metal sites play a key role in the biochemistry of oxygen and particularly in oxygen transport. Hemocyanin (Hc) is a widespread respiratory protein in arthropods and molluscs comprehending multiple copper active sites. Observing the binding, interaction and subsequent reactivity of dioxygen at these hemocyanin copper centres is thus essential for understanding its comprehensive chemical and biological functionality.
Here, we use core-level spectroscopy to measure the copper X-ray absorption structure of hemocyanin in aqueous solution and therewith very similar to physiological conditions. We identify the deoxygenated and the oxygenated state of the native Hc molecule by probing the local electronic structure of the oxygen-active metal centres. Our findings demonstrate an X-ray approach to observe the biochemical activity in an intact metalloprotein molecule and open perspectives for X-ray spectroscopy of complex biomolecules under in vivo conditions.
Funded by the DFG (DE 414/12-1 and SCHO 341/7).