Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

TLDR

Many biological processes depend on detecting and responding to light, often mediated by a structural change in a protein triggered by photon‑induced chromophore isomerization. The authors used time‑resolved serial femtosecond crystallography with free‑electron‑laser x‑ray pulses spanning 100 fs to 3 ms to capture the dynamics. This enabled real‑time observation of the trans‑cis isomerization of the chromophore in photoactive yellow protein and the accompanying protein structural changes. Pande et al., Science, this issue p.

Abstract

Visualizing a response to light Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein. Science , this issue p. 725