1. Ultrafast X-ray Spectroscopy of Haem Proteins
- Author
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Camila Bacellar and Majed Chergui
- Subjects
carbon-monoxide ,molecular-dynamics ,resolved resonance raman ,nitric-oxide ,transient absorption ,x-ray emission spectroscopy ,General Medicine ,General Chemistry ,x-ray absorption spectroscopy ,structural dynamics ,heam proteins ,cytochrome-c ,protein excited state dynamics ,ultrafast dynamics ,hydrogen-sulfide ,geminate recombination ,excited-state - 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.
- Published
- 2022
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