Dresden 2011 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 8: Posters: Protein Structure \& Dynamics
BP 8.2: Poster
Montag, 14. März 2011, 17:15–20:00, P3
L-edge X-Ray Spectroscopy Revealing Structure and Dynamics of Metalloprotein Active Centers — •Kathrin Maria Lange1, Ronny Golnak1, Sebastien Bonhommeau2, and Emad Flear Aziz1,3 — 1Helmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str. 15, 12489 Berlin — 2Institut des Sciences Moléculaires, UMR 5255 CNRS, 351 cours de la Libération, 33405 Talence Cedex, France — 3Freie Universität Berlin, FB Physik, Arnimallee 14, D-14195 Berlin, Germany
Reactions catalyzed by metalloproteins occur at their active centre, accordingly determining its electronic structure allows drawing conclusions about the protein function. We revealed for the first time the electronic structure of metalloproteins in physiological media using L-edge X-ray absorption spectroscopy on the iron active centre.1 By comparing the electronic structure of haemoglobin and catalase, the origin of the high enzymatic activity of catalase could be revealed.2 Furthermore the preferential ligation of myoglobin was investigated recently.3 The electronic structure of its iron active centre upon binding to O2, CO, CN and NO were compared to the reduced form and metmyoglobin. For the interpretation of the data muliplet calculations were used.
1 E F Aziz et al., Phys. Rev. Let. 102, 68103 (2009)
2 N Bergmann et al., Phys. Chem. Chem. Phys. Vol. 12, 18, 4827-4832 (2010)
3 K M Lange et al., in preparation (2010)