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Anabaena Sensory Rhodopsin : effect of mutations on the ultrafast photo-isomerization dynamics

Abstract : ASR, is a photoreceptor protein that binds the protonated Schiff base of retinal in two ground state conformations. The particular protein consists a model system where the effect of the protein environment on the isomerization dynamics of the two isomers can be investigated. In this thesis an extended study on point mutated proteins is presented where the variable is the protein environment. The results show significant differences between the two isomers excited state lifetimes with the shorter or longer lifetimes commented in terms of Sl/S2 electronic mixing. Supplementary, the experimental development of a Transient absorption spectrometer (T.A) and a Two-dimensional electronic spectroscopy setup (2DES) operating in the NIR and UV-Vis spectral range respectively are described. The 2DES spectrometer is based on translating wedges made out of birefringent material producing two collinear phase-locked pulses with sub-I Ofs duration. The interferometric precision on controlling the delay between the two pump pulses allows to perform 2DES measurements on systems absorbing in the 360-430 nm range allowing to resolve the excitation process spectrally.
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Submitted on : Tuesday, September 3, 2019 - 4:46:23 PM
Last modification on : Wednesday, September 4, 2019 - 3:42:22 PM
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  • HAL Id : tel-02277567, version 1



Damianos Agathangelou. Anabaena Sensory Rhodopsin : effect of mutations on the ultrafast photo-isomerization dynamics. Theoretical and/or physical chemistry. Université de Strasbourg, 2019. English. ⟨NNT : 2019STRAE001⟩. ⟨tel-02277567⟩



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