Göttingen Graduate Center for Neurosciences, Biophysics, and Molecular Biosciences

Bennati, Marina, Prof. Dr.


  • 1995 - PhD (Physics) University of Stuttgart
  • 1996 - 1999 DFG Postdoctoral fellow, MIT Cambridge (USA)
  • 1999 - 2001 MIT sponsored research staff associate
  • 2002 - 2006 Lecturer and research scientist, University of Frankfurt
  • Since 2007 Independent research group leader, Electron Paramagnetic Resonance Spectroscopy, MPI for Biophysical Chemistry, Göttingen
  • Since 2011 Joint Professorship University of Göttingen (Department of Chemistry) & MPI for Multidisciplinary Sciences
  • 2012 - 2019 Chair of DFG priority program 1601 ‘New Frontiers in Sensitivity for EPR Spectroscopy: from Biological Cells to Nano Materials’



Homepage Department/Research Group

https://www.mpinat.mpg.de/bennati/



Major research interest

EPR Spectroscopy for Biomolecular Structure

Our research focuses on the investigation of paramagnetic centers in biological systems with electron paramagnetic resonance (EPR) spectroscopy. In biological processes, paramagnetic centers are encountered as metal ions or clusters, amino acid radicals cofactors in electron transfer or catalytic reactions or can be inserted in diamagnetic proteins in form of spin labels. The recent advent of high-field EPR in combination with pulsed techniques, has substantially increased the available sensitivity and resolution, allowing us to explore biological systems close to their physiological conditions.

Local structure at atomic resolution can be achieved by detecting the interaction of electron spins with surrounding magnetic nuclei in electron nuclear double resonance (ENDOR). This method permits one to determine the distance as well as the orientation of nuclear spins with respect to a paramagnetic center. The figure illustrates nuclei that were detected in a 95 GHz ENDOR experiment to elucidate the structure of the active site in a p21ras-Mn-GDP complex.

GGNB Bennati Figure 1Adapted from Bennati et al. (2006) Biochemistry 45: 42


Distances and orientations in protein complexes by high-field pulse EPR
Pulse EPR spectroscopy can be used to detect the interaction between two unpaired electron spins. These techniques enable long-range distance measurements on the order of 2 up to 8 nm and can give information on the assembly of protein complexes or tertiary structures in large proteins or enzymes at concentrations as low as 10 - 20 μM. Experiments performed at high magnetic fields contain also information about the relative orientations of two paramagnetic centers.

GGNB Bennati Figure 2The RNR-R2 dimer from mouse. Structure of the tyrosyl biradical determined in high-field PELDOR, as defined by the projection angles θij between the g-tensor principal axes and the dipolar distance vector r at each radical site. Adapted from V. Denysenkov et al. (2008) Angewandte Chemie 147: 1224


Studies of enzymatic mechanisms: Ribonucleotide reductase
RNRs catalyse the reduction of nucleotide into deoxynucleotide in all living cells, the rate-determining step in DNA biosynthesis. The class I enzymes are composed of two subunits, R1 and R2. The R2 subunit contains the essential diferric cluster-tyrosyl radical cofactor and R1 is the site of conversion of nucleoside diphosphates to 2’-deoxynucleoside diphosphates. In collaboration with the group of J. Stubbe (MIT) we are investigating the mechanism of the long-range electron transfer between R2 and R1 using EPR long-range distance measurements in the active enzyme by freeze quenching the intermediate states. We have measured the distance between the Y•s in R2 as well as the cross distance between R1 and R2 (Figure 3).

GGNB Bennati Figure 3Predicted diagonal and linear distances by the docking model (black) and measured diagonal distances obtained by PELDOR (blue) projected onto the docking model of E. coli Ribonucleotide Reductase. Adapted from M. R. Seyedsayamdost, M. Bennati et al. (2007) J. Am. Chem. Soc. 129: 15748


Selected recent publications


  • Levien M, Yang L, van der Ham A, Reinhard M, John M, Purea A, Ganz J, Marquardsen T, Tkach I, Orlando T, Bennati M (2024) Overhauser enhanced liquid state nuclear magnetic resonance pectroscopy in one and two dimensions. Nat Commun 15, 5904. doi: 10.1038/s41467-024-50265-5

  • Hecker F, Fries L, Hiller M, Chiesa M, Bennati M (2023) 17O Hyperfine Spectroscopy Reveals Hydration Structure of Nitroxide Radicals in Aqueous Solutions. Angew. Chem. Int. Ed. 62 (4), e202213700. doi: 10.1002/anie.202213700

  • Meyer A, Kehl A, Cui C, Reichardt F A K, Hecker F, Funk L-M, Ghosh M K, Pan K T, Urlaub H, Tittmann K, Stubbe J, Bennati M (2022) 19F Electron-nuclear double resonance reveals interaction between redox-active tyrosines across the α/β interface of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 144, S. 11270 – 11282. doi: 10.1021/jacs.2c02906

  • Pokern Y, Eltzner B, Huckemann SF, Beeken C, Stubbe J, Tkach I, Bennati M, Hiller M (2021) Statistical Analysis of ENDOR Spectra. Proc. Natl. Acad. Sci. USA 118 (27), e2023615118. doi: 10.1073/pnas.2023615118

  • Orlando T, Dervisoglu R, Levien M, Tkach I, Prisner TF, Andreas L, Denysenkov V, Bennati M (2018) Dynamic nuclear polarization of 13C nuclei in the liquid state over a 10 Tesla field range. Angewandte Chemie International Edition, 57, 1-6

  • Liu G, Levien M, Karschin N, Parigi G, Luchinat C, Bennati M (2017) One-thousand-fold enhancement of high field liquid nuclear magnetic resonance signals at room temperature. Nature Chemistry 9:676. doi:10.1038/nchem.2723