Ultrafast X-ray Spectroscopy of Haem Proteins

Authors

DOI:

https://doi.org/10.2533/chimia.2022.538

Keywords:

Haem proteins, Ultrafast dynamics, X-ray Absorption Spectroscopy, X-ray Emission Spectroscopy, Protein excited state dynamics

Abstract

In this article we revisit our recent picosecond and femtosecond X-ray absorption spectroscopy (XAS) and X-ray emission spectroscopy (XES) experiments, probing the ultrafast electronic and geometric evolution of photoexcited haem proteins, namely ferrous Nitrosyl Myoglobin (MbNO) and ferric Cytochrome c (Cyt c). We show through these two examples, combined with results from ultrafast optical spectroscopy, the universal behavior of the excited state dynamics of ferric and ferrous complexes. Regardless of the type of ligand, its dissociation or lack thereof, or the metal oxidation state, the photoexcited system relaxes through a cascade of excited spin states leading to formation of a high spin state, which in the case of the haem is a domed porphyrin.

Downloads

Published

2022-06-29

How to Cite

[1]
C. Bacellar, M. Chergui, Chimia 2022, 76, 538, DOI: 10.2533/chimia.2022.538.