ARCANE Seminar - November 24

PROGRAMME

14:00 | Stefano Ciurli (University of Bologna)
“Urease, a Nickel Enzyme: From Catalytic Mechanism to Inhibition”

Urease is a nickel-dependent enzyme that catalyzes the hydrolysis of urea into ammonia and carbamate. While this reaction plays important physiological roles in many microorganisms, urease activity is also a major virulence factor in several human pathogens, making the enzyme an attractive therapeutic target. Its remarkable catalytic efficiency relies on a dinuclear nickel active site, where metal coordination, substrate binding, proton transfer, and protein dynamics are intimately coupled.

In this seminar, I will discuss how structural, spectroscopic, and biochemical studies have contributed to our understanding of the molecular mechanism of urease catalysis, with particular emphasis on the role of the nickel ions in substrate activation and turnover. I will then focus on the inhibition of urease and on how different classes of inhibitors interact with the metal-containing active site and interfere with its catalytic machinery.

Understanding these interactions at the molecular level provides the basis for moving from inhibition to inhibitor design. The comparison of catalytic and inhibited states reveals how coordination geometry, metal–ligand interactions, and the architecture of the active-site cavity determine inhibitor binding and efficacy. Urease therefore provides an illustrative example of how mechanistic bioinorganic chemistry can contribute to the identification and exploitation of metalloenzymes as therapeutic targets.

15:00 | Wajdi Jaouad (LCBM)
“Biochemical and functional characterizations of antimicrobial peptides from human gut microbiome”

15:20 | Coffee Break

15:40 | Yung-Sing Wong (DPM)
“Greener Drug Design: BET inhibitors with Anti-inflammatory Activity”

16:10 | Andrés Palencia (IAB)
“Structural Studies on Protein-RNA Complexes and Applications For the Development of Next-Generation Anti-microbials”