2018 - today    Postdoctoral scientist in Physics at the Freie Universität Berlin

2013 - 2018      Ph.D. in Physics at the Freie Universität Berlin

2013                Diploma in Physics at the Freie Universität Berlin

Curriculum vitae

In general, I am interested in gas-processing metalloenzymes and the molecular proceedings of catalysis. I focus on all type of hydrogenases as well as cytochrome c oxidase. By controlling experimental conditions (e.g. electron and proton accessibility and/or exposure to reactive gases) it is possible to stabilize reaction intermediates that can be then characterized by steady state spectroscopy. To follow catalysis in real time I apply time-resolved techniques as e.g. Quantum Cascade Laser spectroscopy to validate the involvement of selected intermediates in catalysis.

• [FeFe]-Hydrogenases: recent developments and future perspectives. Wittkamp, F.; Senger, M.; Stripp, S. T.; Apfel, U. P., Chemical communications 2018, 54 (47), 5934-5942.
• Protonation/reduction dynamics at the [4Fe-4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases. Senger, M.; Mebs, S.; Duan, J.; Shulenina, O.; Laun, K.; Kertess, L.; Wittkamp, F.; Apfel, U. P.; Happe, T.; Winkler, M.; Haumann, M.; Stripp, S. T., Phys Chem Chem Phys 2018, 20 (5), 3128-3140.
• Hydrogen and oxygen trapping at the H-cluster of [FeFe]-hydrogenase revealed by site-selective spectroscopy and QM/MM calculations. Mebs, S.; Kositzki, R.; Duan, J.; Kertess, L.; Senger, M.; Wittkamp, F.; Apfel, U. P.; Happe, T.; Stripp, S. T.; Winkler, M.; Haumann, M., Biochimica et biophysica acta 2018, 1859 (1), 28-41.
• Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases. Winkler, M.; Senger, M.; Duan, J.; Esselborn, J.; Wittkamp, F.; Hofmann, E.; Apfel, U. P.; Stripp, S. T.; Happe, T., Nat Commun 2017, 8, 16115.
• Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis. Senger, M.; Stripp, S. T.; Soboh, B.,The Journal of biological chemistry 2017, 292 (28), 11670-11681.
• Proton-Coupled Reduction of the Catalytic [4Fe-4S] Cluster in [FeFe]-Hydrogenases. Senger, M.; Laun, K.; Wittkamp, F.; Duan, J.; Haumann, M.; Happe, T.; Winkler, M.; Apfel, U. P.; Stripp, S. T., Angewandte Chemie 2017, 56 (52), 16503-16506.
• Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry. Mebs, S.; Senger, M.; Duan, J.; Wittkamp, F.; Apfel, U. P.; Happe, T.; Winkler, M.; Stripp, S. T.; Haumann, M., J Am Chem Soc 2017, 139 (35), 12157-12160.
• Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics. Senger, M.; Mebs, S.; Duan, J.; Wittkamp, F.; Apfel, U. P.; Heberle, J.; Haumann, M.; Stripp, S. T., Proceedings of the National Academy of Sciences of the United States of America 2016, 113 (30), 8454-9.