Ultrafast excited-state dynamics of tryptophan in water observed by transient absorption spectroscopy

Sharma, Divya; Léonard, Jérémie; Haacke, S.

doi:10.1016/j.cplett.2010.02.057

Cited by 19 publications

(31 citation statements)

References 27 publications

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“…1, this feature reflects the shape of the static absorption of the sample and is due to ground state bleaching (GSB). Similar measurements were already reported by Haacke and co-workers [53], with identical dynamics, who probed a wider spectral window ranging from 300 to 700 nm.…”

Section: Methodssupporting

confidence: 81%

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Ultraviolet transient absorption, transient grating and photon echo studies of aqueous tryptophan

et al. 2013

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a b s t r a c tWe compare UV transient grating (TG) experiments of aqueous tryptophan with transient absorption (TA) and fluorescence up-conversion measurements. The TG and TA signals show a bi-exponential rise with sub-ps and ps time constants, which are consistent with the fluorescence studies. Using experimental data, we provide an equation for the homodyne-detected TG signal, taking into account the sub-100 fs internal conversion of tryptophan after excitation. In addition, we measure a sub-100 fs homogeneous electronic dephasing time for tryptophan in water by the photon echo (PE) technique. These measurements provide a consistent picture of excited state dynamics of aqueous tryptophan that may serve as a basis for coherent 2D-UV spectroscopy of biosystems.

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Section: Methodssupporting

confidence: 81%

“…A Singular value decomposition (SVD) analysis confirms a very similar spectral evolution. In their study, Haacke and co-workers reported similar time scales for the s 2 -s 3 components [53].…”

Section: Transient Absorption Experimentsmentioning

confidence: 79%

Ultraviolet transient absorption, transient grating and photon echo studies of aqueous tryptophan

et al. 2013

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“…The lifetime of the W* state in tryptophan, as reported here, is consistent with previous reports of the nanosecond fluorescence lifetime of tryptophan. 42 , 45 , 68 , 69 …”

Section: Discussionmentioning

confidence: 99%

Structure and Function of Tryptophan–Tyrosine Dyads in Biomimetic β Hairpins

et al. 2019

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Tyrosine–tryptophan (YW) dyads are ubiquitous structural motifs in enzymes and play roles in proton-coupled electron transfer (PCET) and, possibly, protection from oxidative stress. Here, we describe the function of YW dyads in de novo designed 18-mer, β hairpins. In Peptide M, a YW dyad is formed between W14 and Y5. A UV hypochromic effect and an excitonic Cotton signal are observed, in addition to singlet, excited state (W*) and fluorescence emission spectral shifts. In a second Peptide, Peptide MW, a Y5–W13 dyad is formed diagonally across the strand and distorts the backbone. On a picosecond timescale, the W* excited-state decay kinetics are similar in all peptides but are accelerated relative to amino acids in solution. In Peptide MW, the W* spectrum is consistent with increased conformational flexibility. In Peptide M and MW, the electron paramagnetic resonance spectra obtained after UV photolysis are characteristic of tyrosine and tryptophan radicals at 160 K. Notably, at pH 9, the radical photolysis yield is decreased in Peptide M and MW, compared to that in a tyrosine and tryptophan mixture. This protective effect is not observed at pH 11 and is not observed in peptides containing a tryptophan–histidine dyad or tryptophan alone. The YW dyad protective effect is attributed to an increase in the radical recombination rate. This increase in rate can be facilitated by hydrogen-bonding interactions, which lower the barrier for the PCET reaction at pH 9. These results suggest that the YW dyad structural motif promotes radical quenching under conditions of reactive oxygen stress.

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“…85 For zwitterionic Trp in water, the protonated amino group seems to be key side chain group for excited state deactivation involving intramolecular proton transfer from NH3 + to the indole chromophore. 124,125 ranging from 2.7 to 5.5 ns, the χ1=180° (a) rotamer with =0.5 ns. 126 Although these processes are responsible for the dramatic variation of the Trp lifetime, they do not explain the existence of multiple lifetimes for a single residue.…”

Section: Tryptophan Fluorescence: the Rotamer Modelmentioning

confidence: 99%

UV Photoinduced Dynamics of Conformer-Resolved Aromatic Peptides

2019

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A detailed understanding of radiative and nonradiative processes in peptides containing an aromatic chromophore requires the knowledge of the nature and energy level of low-lying excited states that could be coupled to the bright 1 * excited state. Isolated aromatic amino acids and short peptides provide benchmark cases to study, at the molecular level, the photoinduced processes that govern their excited state dynamics. Recent advances in gas phase laser spectroscopy of conformer-selected peptides have paved the way to a better, yet not fully complete, understanding of the influence of intramolecular interactions on the properties of aromatic chromophores. This review aims at providing an overview of the photophysics and photochemistry at play in neutral and charged aromatic chromophore containing peptides, with a particular emphasis on the charge (electron, proton) and energy transfer processes. A significant impact is exerted by the experimental progress in energy-and time-resolved spectroscopy of protonated species, which leads to a growing demand for theoretical supports to accurately describe their excited state properties.

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Ultrafast excited-state dynamics of tryptophan in water observed by transient absorption spectroscopy

Cited by 19 publications

References 27 publications

Ultraviolet transient absorption, transient grating and photon echo studies of aqueous tryptophan

Ultraviolet transient absorption, transient grating and photon echo studies of aqueous tryptophan

Structure and Function of Tryptophan–Tyrosine Dyads in Biomimetic β Hairpins

UV Photoinduced Dynamics of Conformer-Resolved Aromatic Peptides

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