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BP: Fachverband Biologische Physik

BP 8: Posters: Protein Structure \& Dynamics

BP 8.2: Poster

Monday, March 14, 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 Aziz^1,3 — 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)