Sílvia Osuna

This study identifies a conserved histidine residue critical for fluoroacetate dehalogenase activity on difluoroacetate and shows substitutions enhance its catalytic efficiency.

This study investigates how functional and conformational substates change during enzyme evolution using single-molecule kinetic assays and simulations, showing coordinated shifts in substate equilibria that optimize catalytic efficiency.

This study enhances the reversible photocontrol of a photoxenase by engineering conformational shifts, achieving a light-regulation factor of ~100 with near-quantitative reversibility.

This study shows that distal mutations improve enzyme catalysis by enhancing substrate binding and product release, working with active-site mutations to increase overall activity.

This study designs and synthesizes six new photoswitchable unnatural amino acids (psUAAs) for enzyme engineering, showing enhanced interaction potential and diverse photochemical behaviors.

The paper describes how two distinct enzymes evolved from a common ancestor through different mutational paths, leading to divergent molecular and phenotypic outcomes.