The stable tyrosyl radical in ribonucleotide reductase was used to characterize the dimer structure at low temperature. Using Pulsed Electron Double Resonance (PELDOR) at high frequency (180 GHz) and high field (6.4 T), not only the distance but also the relative orientation between the two radicals in the dimer could be determined. The position of the tyrosyl radicals in the monomer were taken from the crystal structure. The self-developed PELDOR measurement setup in Frankfurt has the highest frequency worldwide.
- Denysenkov, V. P., Prisner, T. F., Stubbe, J.& Bennati, M. High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase. Proc. Nat. Acad. Sci. 103, 13386-13390 (2006)
- Denysenkov, V. P., Biglino, D., Lubitz, W., Prisner, T. F. & Bennati, M. Structure of the tyrosyl biradical in mouse R2 ribonucleotide reductase from high-field PELDOR. Angew. Chem. Int. Edit. 47, 1224-1227 (2008)
- Bennati, M.& Prisner, T. F. New developments in high field electron paramagnetic resonance with applications in structural biology. Rep. Prog. Phys. 68, 411-448 (2005)