Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore

A. Espagne; P. Changenet-Barret; S. Charier; J. B. Baudin; L. Jullien; P. Plaza; M. M. Martin

doi:10.1016/B978-044451656-5/50082-7

Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore

A. Espagne
, P. Changenet-Barret
, S. Charier
, J. B. Baudin
, L. Jullien
, P. Plaza
, M. M. Martin

PSL Research University

Résultats de recherche: Le chapitre dans un livre, un rapport, une anthologie ou une collection › Chapitre › Revue par des pairs

Résumé

In order to better understand the early photophysics of PYP, this chapter compares three model chromophores, the deprotonated trans-p-coumaxic acid (pCA2-) and its amide (pCM-) and phenyl thioester (pCT-) analogues, in aqueous solution. The excited-state relaxation dynamics is followed by subpicosecond transient absorption and gain spectroscopy. The excited-state deactivation pathway of PYP model chromophores is found to depend strongly on the substituent adjacent to the carbonyl group. The photoisomerization reaction of the deprotonated p-coumaric acid (pCA2-) and of its amide analogue (pCM-) in solution does not show any spectroscopically detectable intermediate, which is quite different from PYP. On the contrary, the phenyl thioester derivative pCT- exhibits a photo-physical behavior in solution surprisingly close to that of the protein during its initial deactivation step. This chapter highlights the determining role of the thioester bond in the primary molecular events in PYP.

langue originale	Anglais
titre	Femtochemistry and Femtobiology
Sous-titre	Ultrafast Events in Molecular Science VIth International Conference on Femtochemistry Maison de la Chimie, Paris, France July 6-10, 2003
Editeur	Elsevier
Pages	421-424
Nombre de pages	4
ISBN (Electronique)	9780444516565
Les DOIs	https://doi.org/10.1016/B978-044451656-5/50082-7
état	Publié - 1 janv. 2004
Modification externe	Oui

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Espagne, A., Changenet-Barret, P., Charier, S., Baudin, J. B., Jullien, L., Plaza, P., & Martin, M. M. (2004). Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore. Dans Femtochemistry and Femtobiology: Ultrafast Events in Molecular Science VIth International Conference on Femtochemistry Maison de la Chimie, Paris, France July 6-10, 2003 (p. 421-424). Elsevier. https://doi.org/10.1016/B978-044451656-5/50082-7

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abstract = "In order to better understand the early photophysics of PYP, this chapter compares three model chromophores, the deprotonated trans-p-coumaxic acid (pCA2-) and its amide (pCM-) and phenyl thioester (pCT-) analogues, in aqueous solution. The excited-state relaxation dynamics is followed by subpicosecond transient absorption and gain spectroscopy. The excited-state deactivation pathway of PYP model chromophores is found to depend strongly on the substituent adjacent to the carbonyl group. The photoisomerization reaction of the deprotonated p-coumaric acid (pCA2-) and of its amide analogue (pCM-) in solution does not show any spectroscopically detectable intermediate, which is quite different from PYP. On the contrary, the phenyl thioester derivative pCT- exhibits a photo-physical behavior in solution surprisingly close to that of the protein during its initial deactivation step. This chapter highlights the determining role of the thioester bond in the primary molecular events in PYP.",

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Espagne, A, Changenet-Barret, P, Charier, S, Baudin, JB, Jullien, L, Plaza, P & Martin, MM 2004, Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore. Dans Femtochemistry and Femtobiology: Ultrafast Events in Molecular Science VIth International Conference on Femtochemistry Maison de la Chimie, Paris, France July 6-10, 2003. Elsevier, p. 421-424. https://doi.org/10.1016/B978-044451656-5/50082-7

Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore. / Espagne, A.; Changenet-Barret, P.; Charier, S. et al.
Femtochemistry and Femtobiology: Ultrafast Events in Molecular Science VIth International Conference on Femtochemistry Maison de la Chimie, Paris, France July 6-10, 2003. Elsevier, 2004. p. 421-424.

Résultats de recherche: Le chapitre dans un livre, un rapport, une anthologie ou une collection › Chapitre › Revue par des pairs

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AU - Charier, S.

AU - Baudin, J. B.

AU - Jullien, L.

AU - Plaza, P.

AU - Martin, M. M.

PY - 2004/1/1

Y1 - 2004/1/1

N2 - In order to better understand the early photophysics of PYP, this chapter compares three model chromophores, the deprotonated trans-p-coumaxic acid (pCA2-) and its amide (pCM-) and phenyl thioester (pCT-) analogues, in aqueous solution. The excited-state relaxation dynamics is followed by subpicosecond transient absorption and gain spectroscopy. The excited-state deactivation pathway of PYP model chromophores is found to depend strongly on the substituent adjacent to the carbonyl group. The photoisomerization reaction of the deprotonated p-coumaric acid (pCA2-) and of its amide analogue (pCM-) in solution does not show any spectroscopically detectable intermediate, which is quite different from PYP. On the contrary, the phenyl thioester derivative pCT- exhibits a photo-physical behavior in solution surprisingly close to that of the protein during its initial deactivation step. This chapter highlights the determining role of the thioester bond in the primary molecular events in PYP.

AB - In order to better understand the early photophysics of PYP, this chapter compares three model chromophores, the deprotonated trans-p-coumaxic acid (pCA2-) and its amide (pCM-) and phenyl thioester (pCT-) analogues, in aqueous solution. The excited-state relaxation dynamics is followed by subpicosecond transient absorption and gain spectroscopy. The excited-state deactivation pathway of PYP model chromophores is found to depend strongly on the substituent adjacent to the carbonyl group. The photoisomerization reaction of the deprotonated p-coumaric acid (pCA2-) and of its amide analogue (pCM-) in solution does not show any spectroscopically detectable intermediate, which is quite different from PYP. On the contrary, the phenyl thioester derivative pCT- exhibits a photo-physical behavior in solution surprisingly close to that of the protein during its initial deactivation step. This chapter highlights the determining role of the thioester bond in the primary molecular events in PYP.

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Espagne A, Changenet-Barret P, Charier S, Baudin JB, Jullien L, Plaza P et al. Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore. Dans Femtochemistry and Femtobiology: Ultrafast Events in Molecular Science VIth International Conference on Femtochemistry Maison de la Chimie, Paris, France July 6-10, 2003. Elsevier. 2004. p. 421-424 doi: 10.1016/B978-044451656-5/50082-7

Chemical structure effect on the excited-state relaxation dynamics of the PYP chromophore

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