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Time-resolved fluorescence traces at room temperature of native LHC II - Download Scientific Diagram

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Open Gain Access To, 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 should be dealt with.

Knotless phytochromes are among the 3 main 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 array. Despite intensive research on the ultrafast photodynamics of phytochromes, little is known about the main kinetics in knotless phytochromes.

Our results show that the ecstatic state lifetime of Pr * (200 ps) is similar to bacteriophytochromes, however a lot longer than in a lot of canonical phytochromes. We designate the slow Pr * kinetics to relaxation procedures of the chromophore-binding pocket that manages the bilin chromophore's isomerization action. The Pfr photoconversion dynamics starts with a quicker thrilled state relaxation than in canonical phytochromes, but, in spite of the differences in the respective domain architectures, continues through similar ground state intermediate actions up to Meta-F.

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e., readily available space and versatility) within the binding pocket, while the general response steps following the photoexcitation are probably conserved amongst the red/far-red phytochromes.

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