Optical control of ultrafast structural dynamics in a fluorescent protein
Hutchison, C. D. M., Baxter, J. M., Fitzpatrick, A., Dorlhiac, G., Fadini, A., Perrett, S., Maghlaoui, K., Lefèvre, S. B., Cordon-Preciado, V., Ferreira, J. L., Chukhutsina, V. U., Garratt, D., Barnard, J., Galinis, G., Glencross, F., Morgan, R. M., Stockton, S., Taylor, B., Yuan, L., . . . van Thor, J. J. (2023). Optical control of ultrafast structural dynamics in a fluorescent protein. Nature Chemistry, Early online. https://doi.org/10.1038/s41557-023-01275-1
Published inNature Chemistry
© The Author(s) 2023
The photoisomerization reaction of a fluorescent protein chromophore occurs on the ultrafast timescale. The structural dynamics that result from femtosecond optical excitation have contributions from vibrational and electronic processes and from reaction dynamics that involve the crossing through a conical intersection. The creation and progression of the ultrafast structural dynamics strongly depends on optical and molecular parameters. When using X-ray crystallography as a probe of ultrafast dynamics, the origin of the observed nuclear motions is not known. Now, high-resolution pump–probe X-ray crystallography reveals complex sub-ångström, ultrafast motions and hydrogen-bonding rearrangements in the active site of a fluorescent protein. However, we demonstrate that the measured motions are not part of the photoisomerization reaction but instead arise from impulsively driven coherent vibrational processes in the electronic ground state. A coherent-control experiment using a two-colour and two-pulse optical excitation strongly amplifies the X-ray crystallographic difference density, while it fully depletes the photoisomerization process. A coherent control mechanism was tested and confirmed the wave packets assignment. ...
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Related funder(s)European Commission
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Additional information about fundingJ.J.v.T. acknowledges support by the Engineering and Physical Sciences Research Council (EPSRC; EP/M000192/1), the Biotechnology and Biological Sciences Research Council (BBSRC; BB/P00752X/1) and travel grant assistance from the UK XFEL HUB. G. Groenhof and D.M. acknowledge funding from the BioExcel CoE project funded by the European Union contracts H2020-INFRAEDI-02-2018-823830 and H2020-EINFRA-2015-1-675728, and the CSC-IT centre in Espoo for access to computing resources. This work is supported in part by NIH grant GM118044 (to S.G.B.). S.I. acknowledges support by Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from the Japan Agency for Medical Research and Development (AMED; grant no. JP21am0101070) and support by JSPS KAKENHI (JP19H05777). E.N. acknowledges support by JSPS KAKENHI (JP19H05781). V.U.C. was supported by an EMBO long-term fellowship (EMBO ALTF 244-2017) and has received funding from the European Union Horizon 2020 research and innovation programme under Marie Sklodowska-Curie grant agreement no. 839389. ...
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