Experimental Data for: Internal Vibrational Energy Redistribution Precedes Energy Dissipation into the Solvent upon Photoexcitation of Heme Proteins

This project explores the fundamental mechanisms of energy dissipation in photoexcited heme proteins, with a focus on myoglobin and cytochrome c. This is the collected and simulated data used for the paper: "Internal Vibrational Energy Redistribution Precedes Energy Dissipation into the Solvent upon Photoexcitation of Heme Proteins" and is meant to give access to the data for other researchers to enable comparison and further research into this topic. Understanding how proteins manage excess energy is essential for uncovering biological processes such as allosteric communication, radiation protection, and enzyme activity regulation.

Using optical pump–THz probe (OPTP) spectroscopy, this study provides a time-resolved view of how vibrational energy, following photoexcitation at the Soret band, redistributes internally within the protein structure before dissipating into the surrounding aqueous solvent. The measurements reveal distinct time constants (~6–10 ps) that characterize energy flow into water, depending on the protein and solvent (H₂O vs D₂O), highlighting a significant isotope effect.

To interpret the experimental findings, the research integrates a computational thermal diffusion model that simulates energy propagation from the heme center outward. The model successfully reproduces the observed dynamics, supporting a diffusive, rather than ballistic, mode of energy transport through the protein matrix.

Overall, the project delivers key insights into protein–solvent thermal coupling, validates hierarchical vibrational relaxation pathways, and demonstrates the strength of OPTP spectroscopy as a tool for probing ultrafast biomolecular dynamics in a minimally invasive manner.