Metal ions and paramagnetic proteins

People working with me on this project at CRMN: T. Le Marchand (IR CNRS), W. Papawassiliou (post-doc), A. J. Pell (Pr ENS Lyon).

Collaborators: Pr.. R. Pierattelli, I. C. Felli, E. Ravera, G. Parigi, C. Luchinat (CERM, Univ. Florence, IT), Pr. L. Emsley (EPFL, CH).

Metal ions are critical in a variety of biological processes, from catalysis to transport and signalling in numerous biochemical pathways. About one third of the proteins purified to date contain at least a metal ion as a cofactor. Despite the importance of these systems, structural data are often difficult to obtain, leaving key aspects of their metal ion coordination, oxidation states, and electronic properties unresolved.
Solid-state NMR, especially under fast MAS conditions, has emerged as a powerful method for probing metal ions directly. In our lab, we leverage high-speed MAS to enhance resolution and sensitivity in paramagnetic NMR, allowing us to observe nuclei near metal centers previously undetectable. This approach provides direct electronic and structural information about the active sites, with an unprecedented level of detail regarding bond lengths and angles, key for developing effective catalysts and understanding enzyme function.
The pioneering work accomplished so far opens new avenues in MAS-NMR for studying larger, more complex metal-containing biomolecules, bridging chemistry and structural biology and advancing our knowledge of metalloenzymes and other essential metalloproteins.

See: Knight et al. Acc. Chem. Res. 2013, 46, 2108; Bertarello et al. Inorg. Chem. 2017, 56, 6624; Bertarello et al. J Am Chem Soc 2020, 142, 16757; Bonaccorsi et al. 2020, 142, 19660.