Power Density Titration of Reversible Photoisomerization of a Fluorescent 
Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown 
by Quantitative Millisecond Serial Synchrotron X-ray Crystallography

Baxter, J. M.; Hutchison, C. D. M.; Fadini, A.; Maghlaoui, K.; Cordon-Preciado, V.; Morgan, R. M. L.; Agthe, M.; Horrell, S.; Tellkamp, F.; Mehrabi, P.; Pfeifer, Y.; Müller-Werkmeister, H. M.; von Stetten, D.; Pearson, A. R.; van Thor, J. J.

doi:10.1021/jacs.3c12883

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学術論文

Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography

MPS-Authors

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Tellkamp, F.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Mehrabi, P.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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https://doi.org/10.1021/jacs.3c12883
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baxter-et-al-2024-power-density-titration-of-reversible-photoisomerization-of-a-fluorescent-protein-chromophore-in-the.pdf
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ja3c12883_si_001.pdf
(付録資料), 793KB

引用

Baxter, J. M., Hutchison, C. D. M., Fadini, A., Maghlaoui, K., Cordon-Preciado, V., Morgan, R. M. L., Agthe, M., Horrell, S., Tellkamp, F., Mehrabi, P., Pfeifer, Y., Müller-Werkmeister, H. M., von Stetten, D., Pearson, A. R., & van Thor, J. J. (2024). Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography. Journal of the American Chemical Society, 146(24), 16394-16403. doi:10.1021/jacs.3c12883.

引用: https://hdl.handle.net/21.11116/0000-000F-6DFB-D

要旨

We present millisecond quantitative serial X-ray crystallography at 1.7 Å resolution demonstrating precise optical control of reversible population transfer from Trans–Cis and Cis–Trans photoisomerization of a reversibly switchable fluorescent protein, rsKiiro. Quantitative results from the analysis of electron density differences, extrapolated structure factors, and occupancy refinements are shown to correspond to optical measurements of photoinduced population transfer and have sensitivity to a few percent in concentration differences. Millisecond time-resolved concentration differences are precisely and reversibly controlled through intense continuous wave laser illuminations at 405 and 473 nm for the Trans-to-Cis and Cis-to-Trans reactions, respectively, while the X-ray crystallographic measurement and laser illumination of the metastable Trans chromophore conformation causes partial thermally driven reconversion across a 91.5 kJ/mol thermal barrier from which a temperature jump between 112 and 128 K is extracted.