Integrated Calendar

TBA..

Artificial metalloenzymes (ArMs) have attracted increasing attention in the past two
decades as attractive alternatives to either homogeneous catalysts or enzymes.
Artificial metalloenzymes result from anchoring a catalytically competent abiotic metal
cofactor within a host protein, Figure. The resulting ArMs combine attractive features
of both homogeneous- and bio-catalysts. Importantly, they enable access to new-tonature
reactions in a cellular environment.
Relying on a supramolecular anchoring of an organometallic cofactor in various
protein scaffolds, we have optimized the performance of ArMs for sixteen different
reactions, Figure.
Following a general introduction to the underlying principles of ArMs, this talk will
highlight our recent progress in engineering and evolving such hybrid catalysts for
olefin metathesis, C–H activation, hydroamination, and allylic substitution. A
particular emphasis will be set on performing catalysis in a cellular environment.

Proteasomes are the major regulators of protein half-life, as such play critical roles in a wide range of physiological processes. There are a few proteasome complexes all share the 20S catalytic module. The 20S proteasome and the 19S regulatory complex assemble the 26S proteasome, the major machine in protein degradation. Under osmotic stress, the 26S proteasome forms the proteasome granules (PG) based on the liquid-liquid phase separation (LLPS) principle. I will describe an alternative pathway of protein degradation mediated by the 20S proteasome. Live imaging of the 20S and 19S complexes revealed unexpected intracellular dynamics of the 20S and 26S proteasomes under different conditions and uncovered certain aspects of PG regulation.