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research article

Ultrafast X-ray Spectroscopy of Haem Proteins

Bacellar, Camila  
•
Chergui, Majed  
June 1, 2022
Chimia

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 be-havior of the excited state dynamics of ferric and ferrous haems. 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 results in doming of porphyrin.

  • Details
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Type
research article
DOI
10.2533/chimia.2022.538
Web of Science ID

WOS:000823036600003

Author(s)
Bacellar, Camila  
Chergui, Majed  
Date Issued

2022-06-01

Publisher

SWISS CHEMICAL SOC

Published in
Chimia
Volume

76

Issue

6

Start page

538

End page

545

Subjects

Chemistry, Multidisciplinary

•

Chemistry

•

heam proteins

•

ultrafast dynamics

•

x-ray absorption spectroscopy

•

x-ray emission spectroscopy

•

protein excited state dynamics

•

resolved resonance raman

•

nitric-oxide

•

carbon-monoxide

•

geminate recombination

•

transient absorption

•

structural dynamics

•

molecular-dynamics

•

hydrogen-sulfide

•

excited-state

•

cytochrome-c

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LSU  
Available on Infoscience
August 1, 2022
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/189601
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