paramagnetic effects in metalloproteins - Cu Zn superoxide dismutase

The main objective of our work is to enable researchers in chemistry and biology to use nuclear magnetic resonance as a routine tool in order to obtain a structural and dynamic characterisation of chemical or biological systems of primary importance, from new materials to complex biological systems, such as metalloproteins and large biological assemblies of high molecular weigh.
Through the design of a set of innovative and powerful solid-state NMR tools, we overcome the current barriers to progress in the understanding of these systems, and shed light onto their local and global structures, dynamics, reactivity, and substrate recognition.

Bio-molecular solid-state NMR.
Our objective is to provide unique insight into structure and function for the understanding of central biochemical and genetic processes which cannot be accessed at atomic resolution by any other experimental technique in order to control complex biomolecular systems, modify their behaviour and design improved ligands, that could be lead compounds for the development of new drugs. Recent examples include the study of protein-protein interactions in the bacterial replisome, the investigation of the molecular basis of replication in Measles virus, and the development of new methods for structure and dynamics of membrane proteins.

Paramagnetic solid-state NMR.
The aim of our research in this area is to develop solid-state NMR into a robust tool for the structure characterisation of complex samples containing paramagnetic metal centres, such as battery materials, supported catalysts or metalloproteins. Recent examples include the characterisation of a series of novel cathode materials, of the local environments of dilute activator ions in the solid-state lighting phosphor, and the full structural and dynamical determination of a microcrystalline copper metalloenzyme.

Recent highlights

  • A method for sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectra of 5–30 kDa proteins, applicable to poorly soluble, and noncrystalline systems.
  • An approach for the study of structure and electrical properties of lithium iron manganese phosphates, key to building batteries with enhanced energy storage capacity.
  • The determination of the molecular structure of a large metalloenzyme and of its local dynamics.

Contact: Dr. Guido PINTACUDA, Group Leader –