ArticleProceedings of the National Academy of Sciences of the United States of America2022
Vibrational couplings between protein and cofactor in bacterial phytochrome Agp1 revealed by 2D-IR spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- FTIR Spectroscopy of Red and Far-Red-Light Sensing Phytochromes In vitro.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Ultrafast, remote-controlled protonation reaction enables structural changes in a phytochrome.Science advances · 2025Article
- Resonant Vibrational Enhancement of Downhill Energy Transfer in theThe journal of physical chemistry letters · 2024Article
- Analogies and Differences in the Photoactivation Mechanism of Bathy and Canonical Bacteriophytochromes Revealed by Multiscale Modeling.The journal of physical chemistry letters · 2024Article
- Biomolecular infrared spectroscopy: making time for dynamics.Chemical science · 2024Review
- Molecular Dynamics of Artificially Pair-Decoupled Systems: An Accurate Tool for Investigating the Importance of Intramolecular Couplings.Journal of chemical theory and computation · 2023Article
- Vibrational Spectroscopy of Phytochromes.Biomolecules · 2023Review
- Two-dimensional infrared-Raman spectroscopy as a probe of water's tetrahedrality.Nature communications · 2023Article
- The molecular mechanism of light-induced bond formation and breakage in the cyanobacteriochrome TePixJ.Physical chemistry chemical physics : PCCP · 2023Article
- Vibrational couplings between protein and cofactor in bacterial phytochrome Agp1 revealed by 2D-IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
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Abstract
Phytochromes are ubiquitous photoreceptor proteins that undergo a significant refolding of secondary structure in response to initial photoisomerization of the chromophoric group. This process is important for the signal transduction through the protein and thus its regulatory function in different organisms. Here, we employ two-dimensional infrared absorption (2D-IR) spectroscopy, an ultrafast spectroscopic technique that is sensitive to vibrational couplings, to study the photoreaction of bacterial phytochrome Agp1. By calculating difference spectra with respect to the photoactivation, we are able to isolate sharp difference cross-peaks that report on local changes in vibrational couplings between different sites of the chromophore and the protein. These results indicate inter alia that a dipole coupling between the chromophore and the so-called tongue region plays a role in stabilizing the protein in the light-activated state.
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