EPR Spectroscopy on Volume Limited Protein Single Crystals at X-band
Technology research and method development for studying protein single crystals of nanoliter volumes (0.2 mm3) at X-band using advanced resonators and state-of-the-art digital detection.
Electron Paramagnetic Resonance (EPR) experiments on single crystals are the ultimate method to study paramagnetic states and obtain the full magnetic tensor interactions reflecting the electronic structure of the active site. Ultimately the catalytic activity of hydrogenase enzymes can be understood by relating the information of the magnetic principal axes to the known protein structure. However, the application of single-crystal EPR is severely limited by the small crystals sizes that are usually available (sub-nanoliter to nanoliter volumes). We propose the following work packages to make single crystal EPR feasible.
This work package makes use of the key enabling technologies in order to study, for the first time, protein single crystals of [FeFe]-Hydrogenase enzymes.
Key Enabling Technologies
The Key Enabling Technologies outlined in this fellowship have the potential to increase the sensitivity of EPR by a factor of 30 through the application of highly innovative concepts based on micro-resonators.
Links of Interest
EPR Research Group - Led by Dr. Alexander Schnegg, the EPR Research Group aims to develop and utilise state-of-the-art EPR spectrometers ranging from GHz to Thz frequencies.
Dept. Biophysical Chemistry - Led by Prof. Wolfgang Lubitz, the Department of Biophysical Chemistry looks to understand the chemical reaction of biological hydrogenase in order to create bio-inspired molecular catalysts.