New Publication from Gascon Lab:

We are excited to announce our latest publication, “Quantifying and Engineering Electric Fields in Liver Alcohol Dehydrogenase,” now available in press.

In this work, we use QM/MM simulations to investigate how active-site mutations and metal substitutions modulate the electric field inside the enzyme liver alcohol dehydrogenase (LADH). By directly computing electric fields projected along a bound carbonyl vibrational probe, we reproduce experimentally observed trends from Vibrational Stark Effect (VSE) spectroscopy and provide molecular-level insight into how electrostatic perturbations influence catalysis.

Our results establish a quantitative computational framework linking atomistic electrostatic modeling with experimentally measurable electric-field observables, helping advance the rational engineering of enzyme electrostatics for catalysis.

New research from the Gascon Lab, in collaboration with Warren Beck (Michigan State University), has been accepted for publication in The Journal of Physical Chemistry B.

This work investigates the molecular mechanism of photoactivation in the orange carotenoid protein using a combination of spectroscopy and molecular simulations. The results suggest that ultrafast, excited-state conformational motions of the carotenoid chromophore—specifically bicycle-pedal–type distortions—initiate the transition toward the active state by driving a coupled dynamical response of the protein.

These findings provide a detailed mechanistic picture of how light energy is converted into structural change in a biological photoreceptor and establish a direct link between excited-state dynamics and functional protein response.