@article {27329,
	title = {Ultrafast proton-coupled isomerization in the phototransformation of phytochrome},
	journal = {Nature Chemistry},
	volume = {14},
	number = {7},
	year = {2022},
	note = {Export Date: 06 April 2024; Cited By: 11},
	month = {2022},
	pages = {823 - 830},
	abstract = {The biological function of phytochromes is triggered by an ultrafast photoisomerization of the tetrapyrrole chromophore biliverdin between two rings denoted C and D. The mechanism by which this process induces extended structural changes of the protein is unclear. Here we report ultrafast proton-coupled photoisomerization upon excitation of the parent state (Pfr) of bacteriophytochrome Agp2. Transient deprotonation of the chromophore{\textquoteright}s pyrrole ring D or ring C into a hydrogen-bonded water cluster, revealed by a broad continuum infrared band, is triggered by electronic excitation, coherent oscillations and the sudden electric-field change in the excited state. Subsequently, a dominant fraction of the excited population relaxes back to the Pfr state, while ~35\% follows the forward reaction to the photoproduct. A combination of quantum mechanics/molecular mechanics calculations and ultrafast visible and infrared spectroscopies demonstrates how proton-coupled dynamics in the excited state of Pfr leads to a restructured hydrogen-bond environment of early Lumi-F, which is interpreted as a trigger for downstream protein structural changes. [Figure not available: see fulltext.]. {\textcopyright} 2022, The Author(s).},
	url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85130154686\&doi=10.1038\%2fs41557-022-00944-x\&partnerID=40\&md5=bb99275888487c75b68825eac1a6a9dd},
	author = {Yang, Y. and Stensitzki, T. and Sauthof, L. and Schmidt, A. and Piwowarski, P. and Velazquez Escobar, F. and Michael, N. and Nguyen, A.D. and Szczepek, M. and Br{\"u}nig, F.N. and Netz, R.R. and Mroginski, M.A. and Adam, S. and Bartl, F. and Schapiro, I. and Hildebrandt, P. and Scheerer, P. and Heyne, K.}
}
