Regensburg 2010 – scientific programme
Parts | Days | Selection | Search | Downloads | Help
CPP: Fachverband Chemische Physik und Polymerphysik
CPP 28: Poster: Biopolymers and Biomaterials
CPP 28.12: Poster
Wednesday, March 24, 2010, 17:30–19:00, Poster C
Xenon-Binding Studies of the Thermophilic Enzyme HisF from Thermotoga maritima Using NMR-Spectroscopy — •Christoph Liebold1, Felix List1, Hans Robert Kalbitzer1, Reinhard Sterner1, and Eike Brunner2 — 1Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040, Germany — 2Department of chemistry and food chemistry, Dresden University of Technology, 01062,Germany
The hydrophobic noble gas xenon is known to interact with hydrophobic cavities of macromolecules. Important functional entities of enzymes such as substrate tunnels or the active site often exhibit hydrophobic properties. Therefore, Xe can serve as a probe to explore these entities. [1] Moreover, Xe-binding sites are thought to be centres of increased flexibility, thus providing the possibility of conformational changes required for the function of the enzyme. We evaluated the influence of Xe-binding upon the enzyme HisF from the thermophilic bacterium Thermotoga maritima using 1H-15N HSQC spectra and detected xenon-induced conformational changes mainly for hydrophobic residues located around preexisting cavities within the molecule.This behavior indicates that xenon indeed binds into the aforementioned cavities. Biological implications of our observations are discussed and compared with the results of substrate-binding experiments.
[1] Rubin, S. M.; Spence M. M.; Goodson B. M.; Wemmer D. E. Pines A. Proc. Natl. Acad. Sci. U.S.A, 2000, 97, 9472-9475