Team Interactions Protein-Metal
Metals play a fundamental role in biology, in particular because they are essential to the functioning of many proteins. But they can also be toxic because of their intrinsic properties or for some of them like actinides, 90Sr, or 60Co because they are radioactive. We seek to decipher the mechanisms of these relationships between living organisms and metals at different scales to better understand the toxicity processes for humans and the environment and how to deal with them.
Our research objectives concern five main themes :
- The response of environmental bacteria to metals and radionuclides.
- Toxicity of radionuclides on human models.
- Properties of metal sites in proteins and identification of proteins targeted by radionuclides.
- Engineering of affine and specific proteins chelating radionuclides and lanthanides in perspectives of biodetection or bioremediation.
- Structure-property relationships of proteins involved in catalysis or cellular bioenergetics.
We address these questions using a multidisciplinary approach of molecular ecology, microbiology, molecular biology, biochemistry and biophysics and large scientific instruments such as the Ailes and Mars lines of the SOLEIL Synchrotron or platforms dedicated to the manipulation of actinides (Atalante, CEA-Marcoule), thanks to collaborations with chemists, bioinformaticians or cell biologists.
The elements of interest are natural radionuclides (NOR, in the form of U, Th and decay products), fission products (90Sr, 137Cs, minor actinides, Pu), 60Co, as well as new sources of pollutants potentially released during the dismantling of nuclear facilities or within fusion reactors (tritiated particles).
Recently, we have extended our work to the biological role of rare earths elements (REE) in certain bacteria.
Team manager
Catherine Berthomieu
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Key words
Metalloproteins structure-fonction ; Nuclear toxicology ; Biosensors ; Bioremediation ; Metal stress ; Radionuclides