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You are here: FRIAS Fellows Fellows 2021/22 Prof. Dr. Stefan Weber

Prof. Dr. Stefan Weber

University of Freiburg
Physical Chemistry
Internal Senior Fellow
October 2014 - September 2015

Phone +49 761 203-6214

CV

Stefan Weber studied Chemistry at the University of Stuttgart, Germany, and received his diploma  in 1989. From 1990–1994 he worked as a PhD student at the Institute of Physical Chemistry of the Department of Chemistry, University of Stuttgart, where he completed his PhD (Prof. Dr. Gerd Kothe) in 1994. After a postdoctoral training at the Department of Chemistry at the University of Chicago with Professor James R Norris, Jr., Stefan Weber joined the Physics Department of the Free University of Berlin in 1997 to start his independent scientific career. In 2003 he received his habilitation in Experimental Physics.

In 2006 and 2007 he received several offers for full professorships of Magnetic Resonance at the University of East Anglia at Norwich, UK, the Manchester Interdisciplinary Biocentre of the University of Manchester, UK, and Queen Mary University of London, UK. He rejected these these offers in favor of a call from the University of Freiburg to become a full professor of Physical Chemistry in 2008.

Stefan Weber received a Feodor-Lynen fellowship of the Alexander von Humbolt Foundation (Bonn, Germany) for a two-years postdoctoral research stay in the US. In 2010 he was awarded the renowned Morino Lectureship for the promotion of Molecular Spectroscopy of the Morino Foundation in Japan.

Prof. Weber is author or co-autor of more than 80 publications. He has recently edited a book on “Flavins and Flavoproteins”.

His research interests cover magnetic resonance studies (electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR)) of blue-light active flavoproteins, metalloproteins, and functional materials. He currently develops novel magnetic-resonance detection schemes for sensitivity enhancement of EPR.

 

Selected Publications

  • Variable electron transfer pathways in an amphibian cryptochrome. Tryptophan versus tyrosine-based radical pair; Till Biskup, Bernd Paulus, Asako Okafuji, Kenichi Hitomi, Elizabeth D. Getzoff, Stefan Weber, Erik Schleicher; Journal of Biological Chemistry 288 (2013) 9249–9260.
  • Magnetically sensitive light-induced reactions in cryptochrome are consistent with its proposed role as a magnetocrecepto; Kiminori Maeda, Alexander J. Robinson, Kevin B. Henbest, Hannah J. Hogben, Till Biskup, Margaret Ahmad, Erik Schleicher, Stefan Weber, Christiane R. Timmel, Peter J. Hore; Proceedings of the National Academy of Sciences of the United States of America 109 (2012) 4774–4779.
  • Evidence for interstitial carbon in nitrogenase FeMo cofactor; Thomas Spatzal, Müge Aksoyoglu, Limei Zhang, Susana L.A. Andrade, Erik Schleicher, Stefan Weber, Douglas C. Rees, Oliver Einsle; Science 334 (2011) 940.
  • Unexpected electron transfer in a cryptochrome identified by time-resolved EPR spectroscopy; Till Biskup, Kenichi Hitomi, Elizabeth D. Getzoff, Sebastian Krapf, Thorsten Koslowski, Erik Schleicher, Stefan Weber; Angewandte Chemie International Edition 50 (2011) 12647–12651.
  • Direct observation of a photoinduced radical pair in a cryptochrome blue-light recepto; Till Biskup, Erik Schleicher, Asako Okafuji, Gerhard Link, Kenichi Hitomi, Elizabeth D. Getzoff, Stefan Weber; Angewandte Chemie International Edition 48 (2009) 404–407.

 

FRIAS Research Project

Designed quantum transport in complex materials

Within the FRIAS priority program, we plan to investigate radical-pair based magnetoreceptor molecules of the type proposed to be utilized by migratory birds for navigation along the Earth’s magnetic field. Cryptochrome, a flavin-based photoreceptor and a candidate protein for the birds’ magnetic sense, provides an electron-transfer cascade for efficient and fast light-induced electron transfer over rather long distances. We will examine spin-multiplicity evolution in electron transfer and its consequences for the primary photochemistry of various members of the cryptochrome protein family, for which electron-transfer diversity has been reported despite high structural conservation. Combined with theoretical studies (together with Andreas Buchleitner) we will try to unravel common mechanistic schemes and how these can be exploited to increase the efficiency of light-to-energy conversion devices (together with Eicke R. Weber).