Comparing photoinduced vibrational coherences in bacteriorhodopsin and in native and locked retinal protonated Schiff bases

Bixue Hou; Noga Friedman; Michael Ottolenghi; Mordechai Sheves; Sanford Ruhman

doi:10.1016/j.cplett.2003.10.038

Comparing photoinduced vibrational coherences in bacteriorhodopsin and in native and locked retinal protonated Schiff bases

Bixue Hou, Noga Friedman, Michael Ottolenghi, Mordechai Sheves, Sanford Ruhman^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

Low frequency excited state vibrational coherences induced by impulsive photoexcitation in bacteriorhodopsin are detected via femtosecond pump-probe spectroscopy, and compared with similar data in retinal protonated Schiff bases of native and locked retinals. At delays above ∼100 fs a single vibration below 200 fs dominates the detected spectral modulations. Its frequency of ∼120 in retinal protonated Schiff base is virtually unchanged by locking the C₁₃=C₁₄ bond in the trans or cis configurations, but is increased to 170 cm^-1 within the protein environment. The implications of this result on the part played by the protein in directing the reactivity of the retinal within bacteriorhodopsin is discussed.

Original language	English
Pages (from-to)	549-555
Number of pages	7
Journal	Chemical Physics Letters
Volume	381
Issue number	5-6
DOIs	https://doi.org/10.1016/j.cplett.2003.10.038
State	Published - 21 Nov 2003

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10.1016/j.cplett.2003.10.038

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abstract = "Low frequency excited state vibrational coherences induced by impulsive photoexcitation in bacteriorhodopsin are detected via femtosecond pump-probe spectroscopy, and compared with similar data in retinal protonated Schiff bases of native and locked retinals. At delays above ∼100 fs a single vibration below 200 fs dominates the detected spectral modulations. Its frequency of ∼120 in retinal protonated Schiff base is virtually unchanged by locking the C13=C14 bond in the trans or cis configurations, but is increased to 170 cm-1 within the protein environment. The implications of this result on the part played by the protein in directing the reactivity of the retinal within bacteriorhodopsin is discussed.",

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AU - Hou, Bixue

AU - Friedman, Noga

AU - Ottolenghi, Michael

AU - Sheves, Mordechai

AU - Ruhman, Sanford

PY - 2003/11/21

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N2 - Low frequency excited state vibrational coherences induced by impulsive photoexcitation in bacteriorhodopsin are detected via femtosecond pump-probe spectroscopy, and compared with similar data in retinal protonated Schiff bases of native and locked retinals. At delays above ∼100 fs a single vibration below 200 fs dominates the detected spectral modulations. Its frequency of ∼120 in retinal protonated Schiff base is virtually unchanged by locking the C13=C14 bond in the trans or cis configurations, but is increased to 170 cm-1 within the protein environment. The implications of this result on the part played by the protein in directing the reactivity of the retinal within bacteriorhodopsin is discussed.

AB - Low frequency excited state vibrational coherences induced by impulsive photoexcitation in bacteriorhodopsin are detected via femtosecond pump-probe spectroscopy, and compared with similar data in retinal protonated Schiff bases of native and locked retinals. At delays above ∼100 fs a single vibration below 200 fs dominates the detected spectral modulations. Its frequency of ∼120 in retinal protonated Schiff base is virtually unchanged by locking the C13=C14 bond in the trans or cis configurations, but is increased to 170 cm-1 within the protein environment. The implications of this result on the part played by the protein in directing the reactivity of the retinal within bacteriorhodopsin is discussed.

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Comparing photoinduced vibrational coherences in bacteriorhodopsin and in native and locked retinal protonated Schiff bases

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