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Projekt 13 PD Dr. Erik Schleicher/Prof. Stefan Weber

Characterization of light-active multi-cofactor proteins with photoreceptor ability or photorepair activity

The main focus of the project is to characterize selective members of the new class of FeS-BCP proteins using time-resolved electron paramagnetic resonance (EPR) and transient absorption (TA) spectroscopy in combination with an examination of the redox states of the individual cofactors. These methods have proven useful in unravelling electron-transfer pathways, mapping of electronic structures and probing protein-cofactor interactions in other blue-light-active flavoproteins including photolyases and cryptochromes.

The specific aims of this proposal are as follows:

  • Protein production
  • Unraveling the function of the FeS cluster in CryB and PhrB
  • Unraveling the function of the lumazine cofactor
  • Characterisation of electron-transfer pathways in FeS-BCP proteins
     

 

Cry-Pro Sublass2-1.png

Figure 1: Comparison of the crystal structures of (6-4) photolyase PhrB (PDB ID code 4DJA, left) and CryB (PDB ID code 3ZXS, right). The essential FAD cofactor is shown in yellow. The additional [4Fe-4S] cluster, the ribolumazine and the putative electron transfer chain are depicted in orange, red and green, respectively.

 

Contact

PD Dr. Erik Schleicher

Institute of Physical Chemistry

Albertstr. 21

79104 Freiburg

Phone: +49 (0) 761 203-6204

Fax: +49 (0) 761 203-6222

email: erik.schleicher@physchem.uni-freiburg.de

http://www.radicals.uni-freiburg.de/ak/mitarbeiterinnen/schleicher

 

Prof. Dr. Stefan Weber

Institute of Physical Chemistry

Albertstr. 21

79104 Freiburg

Phone: +49 (0) 761 203-6214

Fax:+49 (0) 761 203-6222

email: stefan.weber@physchem.uni-freiburg.de

http://www.radicals.uni-freiburg.de/ak/weber

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