Séminaire CulturChem | Wadih Ghattas "Artificial enzymes beyond powerful catalytic tools"
-
Le 28 fév. 2022
-
11:00 - 12:30
-
Séminaire
-
Sorbonne Université campus Pierre et Marie Curie
Bâtiment Esclangon amphi Astier
(Masque obligatoire)
-
Ollivier Cyril
-
01 44 27 38 50
Wadih Ghattas (Université Paris-Sud Orsay)
présentera un séminaire dans le cadre des conférences CulturChem
intitulé
"Artificial enzymes beyond powerful catalytic tools"
Abstract. In the context of environmentally friendly green chemistry, enzymes can be used instead of chemical catalysts but their high substrate specificity limits their utility. Additionally, their scope of catalysis is limited to the panel of biochemical reactions while chemists have developed a larger variety of reactions. To overcome these hurdles artificial enzymes have been developed by incorporating chemical catalysts inside proteins. On the one hand, chemical catalysts bestow artificial enzymes with a wide scope of catalysis, on the other protein residues provide a chiral environment and eco-compatibility. Artificial enzymes are now considered a major development addressing the increasing societal and governmental pressure that demand greener chemistry. The talk will feature a prominent example of the development of artificial Diels-Alderases as well as thepotential applications of such biorthogonal artificial enzymes. Indeed, we demonstrated that such artificial enzymes function in living cells thus opening new horizons of applications in therapy and diagnostics.
The chemical and the biological components of artificial metalloenzymes can be separately fine-tuned to optimize the catalysis. Such chemo-genetic optimizations are a unique feature of artificial enzymes and have led to highly efficient examples. Recently while designing the active site of an artificial enzyme, we witnessed how the protein fold can adapt to different metals and how single mutations distant from the active site can affect metal coordination. Studying artificial enzymes is proving to be useful to further improving our understanding of metal coordination in metalloproteins in general.