TU Berlin

Physikalische Chemie / Biophysikalische ChemieIngo Zebger

Inhalt des Dokuments

zur Navigation

Dr. Ingo Zebger


M.Sc. in Chemistry (Diplom-Chemiker)
M.Sc. in Science communication and marketing

Wissenschaftlicher Werdegang
since 08/2003
Senior staff scientist, Institute of Chemistry – PC 14, Technical University of Berlin, Germany (Prof. P.Hildebrandt’s group)
Research Assistant Professor, Department of Physical Chemistry, University of Århus, Denmark (Prof. P.R. Ogilby’s group)
Postdoctoral fellowship, Department of Physical Chemistry, University of Essen, Germany (Prof. H.W. Siesler’s group)
Research associate, Department of Mechanical and Chemical Engineering, Hochschule Krefeld (Niederrhein University of Applied Sciences), Germany (Prof. N. Nowack’s group)
Research associate (PhD thesis), Department of Physical Chemistry, University of Essen, Germany (Prof. H.W. Siesler’s group)


FTIR spectroscopic investigations are a powerful tool to carry out structure/function studies in proteins.
Especially in spectral regions of multiple band overlaps, (IR) Difference spectroscopy is suitable to follow specific changes in the structure and orientation of the protein backbone, as well as, the prosthetic group(s) under various external perturbation, such as potential variations or the irradiation with light of specific wavelength. This is done relative to a reference state in the static or time-resolved regime.

By monitoring IR-difference bands of specific secondary structural element, we can follow the response of the protein backbone relative to electron transfer dynamics of the prosthetic group e.g. in heme proteins immobilized onto SAM-coated Au-surfaces. Complementary information about the latter are obtained by SERRS and Electrochemistry

Oxygen tolerant [NiFe]-hydrogenases of Ralstonia species are of potential for bio-technological energy storage and conversion.
IR-spectroscopy is applied in combination with EPR and UV/Vis, Resonance Raman spectroscopy to unravel/elucidate the underlying reaction mechanism and the structural reason for this oxygen tolerance in comparison with anaerobic standard hydrogenases and to carry out initial functional studies for hydrogenase-based bioelectronic devices.
In this context IR-spectroscopy monitors the catalytic process and allows to identify the involved redox states via the spectral pattern of the CO/CN--ligands attached to the catalytic center.


FTIR measurements in the bulk (Transmission or Attenuated Total Reflectance mode)

Surface Enhanced Infrared Absorption Spectroscopy





Schnellnavigation zur Seite über Nummerneingabe