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Excited-state molecular structures captured by X-ray transient absorption spectroscopy: a decade and beyond
Abstract
Transient molecular structures along chemical reaction pathways are important for predicting molecular reactivity, understanding reaction mechanisms, as well as controlling reaction pathways. During the past decade, X-ray transient absorption spectroscopy (XTA, or LITR-XAS, laser-initiated X-ray absorption spectroscopy), analogous to the commonly used optical transient absorption spectroscopy, has been developed. XTA uses a laser pulse to trigger a fundamental chemical process, and an X-ray pulse(s) to probe transient structures as a function of the time delay between the pump and probe pulses. Using X-ray pulses with high photon flux from synchrotron sources, transient electronic and molecular structures of metal complexes have been studied in disordered media from homogeneous solutions to heterogeneous solution–solid interfaces. Several examples from the studies at the Advanced Photon Source in Argonne National Laboratory are summarized, including excited-state metalloporphyrins, metal-to-ligand charge transfer (MLCT) states of transition metal complexes, and charge transfer states of metal complexes at the interface with semiconductor nanoparticles. Recent developments of the method are briefly described followed by a future prospective of XTA. It is envisioned that concurrent developments in X-ray free-electron lasers and synchrotron X-ray facilities as well as other table-top laser-driven femtosecond X-ray sources will make many breakthroughs and realise dreams of visualizing molecular movies and snapshots, which ultimately enable chemical reaction pathways to be controlled.
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“The final refined model included 97.26% of residues in the favoured region of the Ramachandran plot with 0.25% outliers as calculated by MolProbity56.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [56]
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“Structure quality was assessed using Molprobity56 before deposition in the PDB82,83”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [56]
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“The final coordinates were validated using MolProbity56.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [56]
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Metadata
- Authors
- Chen, L. X., Zhang, X., Lockard, J. V., Stickrath, A. B., Attenkofer, K., Jennings, G., & Liu, D.-J.
- Affiliations
- Northwestern University (US)
- Argonne National Laboratory (US)
- Venue
- Acta Crystallographica Section A Foundations of Crystallography
- Published
- 2010-02-18
- Volume
- 66
- Issue
- 2
- Pages
- 240-251
- ISSN
- 0108-7673 (ISSN-L)
- OpenAlex
- W2093910216
- Cited by
- 88
- References
- 111
- Citations by year
- 2026: 1 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 2 · 2019: 5 · 2018: 6 · 2017: 10 · 2016: 9 · 2015: 11 · 2014: 8 · 2013: 11 · 2012: 4
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Acta Crystallographica Section A Foundations of Crystallography (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Physics and Astronomy › Radiation › X-ray Spectroscopy and Fluorescence Analysis
- Physical Sciences › Physics and Astronomy › Radiation › Advanced X-ray Imaging Techniques
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Keywords
- excited-state molecular structure, metalloporphyrins, metal-to-ligand charge transfer, transition metal complexes, reaction mechanism, femtosecond X-ray sources, X-ray free-electron laser, solid-solution interface
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