Comparing photochemistry of n- and tert-butylamine all-trans retinal protonated Schiff-base: Effects of C{double bond, long}N configurational inhomogeneity

Jingyi Zhu; Oshrat Bismuth; Itay Gdor; Amir Wand; Noga Friedman; Mordechai Sheves; Sanford Ruhman

doi:10.1016/j.cplett.2009.08.040

Comparing photochemistry of n- and tert-butylamine all-trans retinal protonated Schiff-base: Effects of C{double bond, long}N configurational inhomogeneity

Jingyi Zhu
, Oshrat Bismuth
, Itay Gdor
, Amir Wand
, Noga Friedman
, Mordechai Sheves
, Sanford Ruhman^*

^*Corresponding author for this work

Institute of Chemistry

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

7 Scopus citations

Abstract

Photochemistry of all-trans tert-butylamine retinal protonated Schiff-base (TB-RPSB) is investigated by femtosecond pump-hyperspectral probe spectroscopy. Unlike the n-butyl analogue (NB-RPSB) no shifting of the transient spectral bands is observed upon tuning the excitation pulses from 395 to 475 nm. The 15 nm shift observed for NB-RPSB in similar experiments was assigned to unspecified ground state structural inhomogeneity. Present results indicate that is most likely due to the coexistence of C₁₅{double bond, long}N double bond isomers in NB-RPSB. Elimination of this inhomogeneity in TB-RPSB makes it a more appropriate model for appreciating protein effects on RPSB photochemistry in retinal proteins.

Original language	English
Pages (from-to)	229-233
Number of pages	5
Journal	Chemical Physics Letters
Volume	479
Issue number	4-6
DOIs	https://doi.org/10.1016/j.cplett.2009.08.040
State	Published - 17 Sep 2009

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10.1016/j.cplett.2009.08.040

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title = "Comparing photochemistry of n- and tert-butylamine all-trans retinal protonated Schiff-base: Effects of C\{double bond, long\}N configurational inhomogeneity",

abstract = "Photochemistry of all-trans tert-butylamine retinal protonated Schiff-base (TB-RPSB) is investigated by femtosecond pump-hyperspectral probe spectroscopy. Unlike the n-butyl analogue (NB-RPSB) no shifting of the transient spectral bands is observed upon tuning the excitation pulses from 395 to 475 nm. The 15 nm shift observed for NB-RPSB in similar experiments was assigned to unspecified ground state structural inhomogeneity. Present results indicate that is most likely due to the coexistence of C15\{double bond, long\}N double bond isomers in NB-RPSB. Elimination of this inhomogeneity in TB-RPSB makes it a more appropriate model for appreciating protein effects on RPSB photochemistry in retinal proteins.",

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T1 - Comparing photochemistry of n- and tert-butylamine all-trans retinal protonated Schiff-base

T2 - Effects of C{double bond, long}N configurational inhomogeneity

AU - Zhu, Jingyi

AU - Bismuth, Oshrat

AU - Gdor, Itay

AU - Wand, Amir

AU - Friedman, Noga

AU - Sheves, Mordechai

AU - Ruhman, Sanford

PY - 2009/9/17

Y1 - 2009/9/17

N2 - Photochemistry of all-trans tert-butylamine retinal protonated Schiff-base (TB-RPSB) is investigated by femtosecond pump-hyperspectral probe spectroscopy. Unlike the n-butyl analogue (NB-RPSB) no shifting of the transient spectral bands is observed upon tuning the excitation pulses from 395 to 475 nm. The 15 nm shift observed for NB-RPSB in similar experiments was assigned to unspecified ground state structural inhomogeneity. Present results indicate that is most likely due to the coexistence of C15{double bond, long}N double bond isomers in NB-RPSB. Elimination of this inhomogeneity in TB-RPSB makes it a more appropriate model for appreciating protein effects on RPSB photochemistry in retinal proteins.

AB - Photochemistry of all-trans tert-butylamine retinal protonated Schiff-base (TB-RPSB) is investigated by femtosecond pump-hyperspectral probe spectroscopy. Unlike the n-butyl analogue (NB-RPSB) no shifting of the transient spectral bands is observed upon tuning the excitation pulses from 395 to 475 nm. The 15 nm shift observed for NB-RPSB in similar experiments was assigned to unspecified ground state structural inhomogeneity. Present results indicate that is most likely due to the coexistence of C15{double bond, long}N double bond isomers in NB-RPSB. Elimination of this inhomogeneity in TB-RPSB makes it a more appropriate model for appreciating protein effects on RPSB photochemistry in retinal proteins.

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Comparing photochemistry of n- and tert-butylamine all-trans retinal protonated Schiff-base: Effects of C{double bond, long}N configurational inhomogeneity

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