We are seeking for a PhD candidate to work on the characterization by advanced Electron Paramagnetic Resonance methodology of mononuclear molybdenum active sites in selected metalloenzymes (see accompagnying file). In this project, we aim at providing new insights into how the protein environment tunes the reactivity of mononuclear molybdenum enzymes as well as clues for the rationale design of bio-inspired Mo-based artificial catalysts optimized towards the reduction of CO2.
For this purpose, a state-of-the-art experimental approach based on multi-frequency EPR spectroscopy, including pulsed hyperfine spectroscopy will be used to characterize the magnetic properties and the local nuclear environment of key Mo(V) intermediates. Uniform or specific isotope enrichment strategies of natural or engineered enzymes, or of their substrates or inhibitors will be developed to provide a deep understanding of the active site reactivity. The data will be interpreted by computer-assisted theoretical modeling relying on structure-based DFT calculations and/or QM/MM hybrid approaches.
The student will be hosted in the Bioenergetics and Protein Engineering (BIP)lab in Marseille for a 3-year PhD contract from Aix-Marseille to begin in October 2018. The BIP lab has a strong expertise in spectroscopic and theoretical studies of metallo-enzymes It hosts one of the major French EPR facilities of the national EPR network.
KeyWords: PhD fellowship, EPR spectroscopy, Physical chemistry
Expires on Wednesday June 6th, 2018