Dr. Sven Stripp

I did my Ph.D. with Thomas Happe at Ruhr-Universität Bochum. In 2010, I joined the group of Joachim Heberle to focus on vibrational spectroscopy. As a biospectroscopist, my research includes both chemical and physical approaches and is motivated by biological questions. I am married and have two hilarious children. 

Department of Physics

Institute of Experimental Physics

Experimental Molecular Biophysics

Researcher

Address
Arnimallee 14
Room 1.1.39
14195 Berlin
Telephone
+49 30 838 55069
Email
sven.stripp@zedat.fu-berlin.de

2010 – today   Freie Universität Berlin, Postdoctoral scientist   

2007 – 2010    Ruhr-Universität Bochum, Dissertation in Biology

2001 – 2007    Ruhr-Universität Bochum, Studies of Chemistry and Biology

CV as PDF

I develop and apply spectroscopic and electrochemical techniques to probe proteins under biologically relevant conditions. My key interests involve gas-processing metalloenzymes like hydrogenases, CO- and formate dehydrogenases, nitrogenases, as well as cytochrome-c oxidase and photosystem II. I try to understand the catalytic mechanisms of H2, O2, and CO/CO2 turnover as well as in vivo cofactor synthesis. 

Methode

Setup for in situ ATR FTIR spectroscopy under gas, light, and potential control.
  • The molecular proceedings of biological hydrogen turnover. Acc. Chem. Res. 2018; 51 (8): 1755 – 1763. doi.org/10.1021/acs.accounts.8b00109
  • Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases. Nat. comm. 2018; 9: 4726. doi.org/10.1038/s41467-018-07140-x
  • Protonation and Reduction Dynamics at the Hydrogen-forming Cofactor of [FeFe]-Hydrogenases. Phys. Chem. Chem. Phys. 2018; 20: 3128–3140. doi.org/10.1039/C7CP04757F
  • Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry. J. Am. Chem. Soc. 2017; 139: 12157−12160. doi.org/10.1021/jacs.7b07548
  • Proton-Coupled Reduction of the Catalytic [4Fe-4S] Cluster in [FeFe]-Hydrogenases. Angew. Chemie Int. Ed. 2017; 56 (52): 16503–16506. doi.org/10.1002/anie.201709910