Citation:
Y. Yang, Stensitzki, T. , Sauthof, L. , Schmidt, A. , Piwowarski, P. , F. Escobar, Velazquez , Michael, N. , Nguyen, A.D. , Szczepek, M. , Brünig, F.N. , Netz, R.R. , Mroginski, M.A. , Adam, S. , Bartl, F. , Schapiro, I. , Hildebrandt, P. , Scheerer, P. , and Heyne, K.. 2022.
“Ultrafast Proton-Coupled Isomerization In The Phototransformation Of Phytochrome”. Nature Chemistry, 14, Pp. 823 - 830.
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85130154686&doi=10.1038%2fs41557-022-00944-x&partnerID=40&md5=bb99275888487c75b68825eac1a6a9dd.
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’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.]. © 2022, The Author(s).Notes:
Export Date: 06 April 2024; Cited By: 11