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• W2103421890 abstract "Proteorhodopsin (pR) is a membrane-embedded proton pump from the microbial rhodopsin family. Light absorption by its retinal chromophore initiates a photocycle, driven by trans/cis isomerization on the femtosecond to picosecond time scales. Here, we report a study on the photoisomerization dynamics of the retinal chromophore of pR, using dispersed ultrafast pump-dump-probe spectroscopy. The application of a pump pulse initiates the photocycle, and with an appropriately tuned dump pulse applied at a time delay after the dump, the molecules in the initial stages of the photochemical process can be de-excited and driven back to the ground state. In this way, we were able to resolve an intermediate on the electronic ground state that represents chromophores that are unsuccessful in isomerization. In particular, the fractions of molecules that undergo slow isomerization (20 ps) have a high probability to enter this state rather than the isomerized K-state. On the ground state reaction surface, return to the stable ground state conformation via a structural or vibrational relaxation occurs in 2-3 ps. Inclusion of this intermediate in the kinetic scheme led to more consistent spectra of the retinal-excited state, and to a more accurate estimation of the quantum yield of isomerization (Phi = 0.4 at pH 6)." @default.
• W2103421890 created "2016-06-24" @default.
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• W2103421890 date "2009-11-23" @default.
• W2103421890 modified "2023-10-18" @default.
• W2103421890 title "Reaction Pathways of Photoexcited Retinal in Proteorhodopsin Studied by Pump−Dump−Probe Spectroscopy" @default.
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• W2103421890 doi "https://doi.org/10.1021/jp9065289" @default.
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• W2103421890 hasPublicationYear "2009" @default.
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