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Open Gain Access To, Short Article 1 Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt am Main, Max-von-Laue Strae 7, 60438 Frankfurt, Germany 2 Institute of Biophysics, Goethe University Frankfurt am Main, Max-von-Laue Strae 1, 60438 Frankfurt, Germany 3 Department of Chemistry, Philipps-Universitt Marburg, Hans-Meerwein-Strae 4, 35032 Marburg, Germany 4 Center for Synthetic Microbiology, Philipps-Universitt Marburg, Hans-Meerwein-Strae 6, 35032 Marburg, Germany * Authors to whom correspondence need to be dealt with.

Knotless phytochromes are among the 3 primary subgroups classified by their unique lack of the PAS domain in their photosensory core module, which remains in contrast to the canonical PAS-GAF-PHY variety. In spite of extensive research study on the ultrafast photodynamics of phytochromes, little is understood about the main kinetics in knotless phytochromes.

Our results show that the excited state lifetime of Pr * (200 ps) is comparable to bacteriophytochromes, but a lot longer than in many canonical phytochromes. We appoint the sluggish Pr * kinetics to relaxation processes of the chromophore-binding pocket that controls the bilin chromophore's isomerization step.  View Details  starts with a quicker excited state relaxation than in canonical phytochromes, but, regardless of the differences in the particular domain architectures, continues via similar ground state intermediate steps up to Meta-F.

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e., offered area and flexibility) within the binding pocket, while the general reaction steps following the photoexcitation are probably conserved amongst the red/far-red phytochromes.

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