2012
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Method For Generating Cyan Fluorescent Proteins Which Have A Reduced Ph Sensitivity Patent Pasquier Helene; Merola Fabienne; Erard Marie; Espagne Agathe; Fredj Asma WO 2012/172095 A1, 2012. @patent{lens.org/080-732-449-078-090,
title = {Method For Generating Cyan Fluorescent Proteins Which Have A Reduced Ph Sensitivity},
author = {Pasquier Helene and Merola Fabienne and Erard Marie and Espagne Agathe and Fredj Asma},
url = {https://lens.org/080-732-449-078-090},
year = {2012},
date = {2012-12-20},
number = {WO 2012/172095 A1},
location = {World Intellectual Property Organization},
keywords = {},
pubstate = {published},
tppubtype = {patent}
}
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2011
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Cyan Fluorescent Protein Carries a Constitutive Mutation That Prevents Its Dimerization Article de journal A Espagne; M Erard; K Madiona; V Derrien; G Jonasson; B Levy; H Pasquier; R Melki; F Merola Biochemistry, 50 (4), p. 437-439, 2011, ISSN: 0006-2960. @article{RN29b,
title = {Cyan Fluorescent Protein Carries a Constitutive Mutation That Prevents Its Dimerization},
author = {A Espagne and M Erard and K Madiona and V Derrien and G Jonasson and B Levy and H Pasquier and R Melki and F Merola},
doi = {10.1021/bi1015875},
issn = {0006-2960},
year = {2011},
date = {2011-01-01},
journal = {Biochemistry},
volume = {50},
number = {4},
pages = {437-439},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
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Relationship between Homo-Oligomerization of a Mammalian Olfactory Receptor and Its Activation State Demonstrated by Bioluminescence Resonance Energy Transfer Article de journal F Wade; A Espagne; M A Persuy; J Vidic; R Monnerie; F Merola; E Pajot-Augy; G Sanz Journal of Biological Chemistry, 286 (17), p. 15252-15259, 2011, ISSN: 0021-9258. @article{RN34b,
title = {Relationship between Homo-Oligomerization of a Mammalian Olfactory Receptor and Its Activation State Demonstrated by Bioluminescence Resonance Energy Transfer},
author = {F Wade and A Espagne and M A Persuy and J Vidic and R Monnerie and F Merola and E {Pajot-Augy} and G Sanz},
doi = {10.1074/jbc.M110.184580},
issn = {0021-9258},
year = {2011},
date = {2011-01-01},
journal = {Journal of Biological Chemistry},
volume = {286},
number = {17},
pages = {15252-15259},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
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2010
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DNA Repair by Photolyase: A Novel Substrate with Low Background Absorption around 265 Nm for Transient Absorption Studies in the UV Article de journal V Thiagarajan; S Villette; A Espagne; A P M Eker; K Brettel; M Byrdin Biochemistry, 49 (2), p. 297-303, 2010, ISSN: 0006-2960. @article{RN30,
title = {DNA Repair by Photolyase: A Novel Substrate with Low Background Absorption around 265 Nm for Transient Absorption Studies in the UV},
author = {V Thiagarajan and S Villette and A Espagne and A P M Eker and K Brettel and M Byrdin},
doi = {10.1021/bi901562a},
issn = {0006-2960},
year = {2010},
date = {2010-01-01},
journal = {Biochemistry},
volume = {49},
number = {2},
pages = {297-303},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2009
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Use of Ruthenium Dyes for Subnanosecond Detector Fidelity Testing in Real Time Transient Absorption Article de journal M Byrdin; V Thiagarajan; S Villette; A Espagne; K Brettel Review of Scientific Instruments, 80 (4), p. 5, 2009, ISSN: 0034-6748. @article{RN32b,
title = {Use of Ruthenium Dyes for Subnanosecond Detector Fidelity Testing in Real Time Transient Absorption},
author = {M Byrdin and V Thiagarajan and S Villette and A Espagne and K Brettel},
doi = {10.1063/1.3117208},
issn = {0034-6748},
year = {2009},
date = {2009-01-01},
journal = {Review of Scientific Instruments},
volume = {80},
number = {4},
pages = {5},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
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Very Fast Product Release and Catalytic Turnover of DNA Photolyase Article de journal A Espagne; M Byrdin; A P M Eker; K Brettel Chembiochem, 10 (11), p. 1777-1780, 2009, ISSN: 1439-4227. @article{RN31b,
title = {Very Fast Product Release and Catalytic Turnover of DNA Photolyase},
author = {A Espagne and M Byrdin and A P M Eker and K Brettel},
doi = {10.1002/cbic.200900328},
issn = {1439-4227},
year = {2009},
date = {2009-01-01},
journal = {Chembiochem},
volume = {10},
number = {11},
pages = {1777-1780},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2008
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Polarized Transient Absorption to Resolve Electron Transfer between Tryptophans in DNA Photolyase Article de journal M Byrdin; S Villette; A Espagne; A P M Eker; K Brettel Journal of Physical Chemistry B, 112 (22), p. 6866-6871, 2008, ISSN: 1520-6106. @article{RN33b,
title = {Polarized Transient Absorption to Resolve Electron Transfer between Tryptophans in DNA Photolyase},
author = {M Byrdin and S Villette and A Espagne and A P M Eker and K Brettel},
doi = {10.1021/jp711435y},
issn = {1520-6106},
year = {2008},
date = {2008-01-01},
journal = {Journal of Physical Chemistry B},
volume = {112},
number = {22},
pages = {6866-6871},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Ultrafast photochemical processes: From the lab to natural photoactive systems Article de journal M M Martin; P Plaza; P Changenet-Barret; A Espagne; M Mahet; C Ley; F Lacombat Actualite Chimique, (320-321), p. 14–19, 2008. @article{Martin:2008,
title = {Ultrafast photochemical processes: From the lab to natural photoactive systems},
author = {M M Martin and P Plaza and P Changenet-Barret and A Espagne and M Mahet and C Ley and F Lacombat},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-48649089855&partnerID=40&md5=5dbe5748299ea91b50952e61834a11b9},
year = {2008},
date = {2008-01-01},
journal = {Actualite Chimique},
number = {320-321},
pages = {14--19},
abstract = {The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions. |
2007
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Photoinduced charge shift as the driving force for the excited-state relaxation of analogues of the Photoactive Yellow Protein chromophore in solution Article de journal A Espagne; P Changenet-Barret; J -B Baudin; P Plaza; M M Martin Journal of Photochemistry and Photobiology A: Chemistry, 185 (2-3), p. 245-252, 2007, ISSN: 1010-6030. @article{RN51,
title = {Photoinduced charge shift as the driving force for the excited-state relaxation of analogues of the Photoactive Yellow Protein chromophore in solution},
author = {A Espagne and P Changenet-Barret and J -B Baudin and P Plaza and M M Martin},
url = {<Go to ISI>://000243736600019},
doi = {10.1016/j.jphotochem.2006.06.016},
issn = {1010-6030},
year = {2007},
date = {2007-01-01},
journal = {Journal of Photochemistry and Photobiology A: Chemistry},
volume = {185},
number = {2-3},
pages = {245-252},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Ultrafast light-induced response of photoactive yellow protein chromophore analogues Article de journal A Espagne; D H Paik; P Changenet-Barret; P Plaza; M M Martin; A H Zewail Photochemical and Photobiological Sciences, 6 (7), p. 780–787, 2007. @article{Espagne:2007,
title = {Ultrafast light-induced response of photoactive yellow protein chromophore analogues},
author = {A Espagne and D H Paik and P Changenet-Barret and P Plaza and M M Martin and A H Zewail},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-34447134184&doi=10.1039%2fb700927e&partnerID=40&md5=f30b6c18d177d6acc83123a44276d1be},
doi = {10.1039/b700927e},
year = {2007},
date = {2007-01-01},
journal = {Photochemical and Photobiological Sciences},
volume = {6},
number = {7},
pages = {780--787},
abstract = {The fluorescence decays of several analogues of the photoactive yellow protein (PYP) chromophore in aqueous solution have been measured by femtosecond fluorescence up-conversion and the corresponding time-resolved fluorescence spectra have been reconstructed. The native chromophore of PYP is a thioester derivative of p-coumaric acid in its trans deprotonated form. Fluorescence kinetics are reported for a thioester phenyl analogue and for two analogues where the thioester group has been changed to amide and carboxylate groups. The kinetics are compared to those we previously reported for the analogues bearing ketone and ester groups. The fluorescence decays of the full series are found to lie in the 1-10 ps range depending on the electron-acceptor character of the substituent, in good agreement with the excited-state relaxation kinetics extracted from transient absorption measurements. Steady-state photolysis is also examined and found to depend strongly on the nature of the substituent. While it has been shown that the ultrafast light-induced response of the chromophore in PYP is controlled by the properties of the protein nanospace, the present results demonstrate that, in solution, the relaxation dynamics and pathway of the chromophore is controlled by its electron donor-acceptor structure: structures of stronger electron donor-acceptor character lead to faster decays and less photoisomerisation. © The Royal Society of Chemistry and Owner Societies.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The fluorescence decays of several analogues of the photoactive yellow protein (PYP) chromophore in aqueous solution have been measured by femtosecond fluorescence up-conversion and the corresponding time-resolved fluorescence spectra have been reconstructed. The native chromophore of PYP is a thioester derivative of p-coumaric acid in its trans deprotonated form. Fluorescence kinetics are reported for a thioester phenyl analogue and for two analogues where the thioester group has been changed to amide and carboxylate groups. The kinetics are compared to those we previously reported for the analogues bearing ketone and ester groups. The fluorescence decays of the full series are found to lie in the 1-10 ps range depending on the electron-acceptor character of the substituent, in good agreement with the excited-state relaxation kinetics extracted from transient absorption measurements. Steady-state photolysis is also examined and found to depend strongly on the nature of the substituent. While it has been shown that the ultrafast light-induced response of the chromophore in PYP is controlled by the properties of the protein nanospace, the present results demonstrate that, in solution, the relaxation dynamics and pathway of the chromophore is controlled by its electron donor-acceptor structure: structures of stronger electron donor-acceptor character lead to faster decays and less photoisomerisation. © The Royal Society of Chemistry and Owner Societies. |
Ultrafast Structural Dynamics of Water Induced by Dissipation of Vibrational Energy Article de journal S Ashihara; N Huse; A Espagne; E T J Nibbering; T Elsaesser Journal of Physical Chemistry A, 111 (5), p. 743-746, 2007, ISSN: 1089-5639. @article{RN53,
title = {Ultrafast Structural Dynamics of Water Induced by Dissipation of Vibrational Energy},
author = {S Ashihara and N Huse and A Espagne and E T J Nibbering and T Elsaesser},
doi = {10.1021/jp0676538},
issn = {1089-5639},
year = {2007},
date = {2007-01-01},
journal = {Journal of Physical Chemistry A},
volume = {111},
number = {5},
pages = {743-746},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2006
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Excited-state dynamics of the PYP chromophore in solution. Environment and structure effects Inproceedings A Espagne; P Changenet-Barret; J -B Baudin; P Plaza; M M Martin Jr, Castleman A W; Kimble, M L (Ed.): VIIth International Conference on Femtochemistry, p. 204-214, Elsevier, 2006. @inproceedings{RN101,
title = {Excited-state dynamics of the PYP chromophore in solution. Environment and structure effects},
author = {A Espagne and P Changenet-Barret and J -B Baudin and P Plaza and M M Martin},
editor = {A W Castleman Jr and M L Kimble},
year = {2006},
date = {2006-01-01},
booktitle = {VIIth International Conference on Femtochemistry},
pages = {204-214},
publisher = {Elsevier},
series = {Femtochemistry VII: Fundamental Ultrafast Processes in Chemistry, Physics and Biology},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}
|
Solvent effect on the excited-state dynamics of analogues of the photoactive Yellow Protein chromophore Article de journal A Espagne; P Changenet-Barret; P Plaza; M M Martin Journal of Physical Chemistry A, 110 (10), p. 3393–3404, 2006. @article{Espagne:2006a,
title = {Solvent effect on the excited-state dynamics of analogues of the photoactive Yellow Protein chromophore},
author = {A Espagne and P Changenet-Barret and P Plaza and M M Martin},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-33645500398&doi=10.1021%2fjp0563843&partnerID=40&md5=d174de26213df87496872cae2ddf21dd},
doi = {10.1021/jp0563843},
year = {2006},
date = {2006-01-01},
journal = {Journal of Physical Chemistry A},
volume = {110},
number = {10},
pages = {3393--3404},
abstract = {We previously reported that two analogues of the Photoactive Yellow Protein chromophore, trans-p-hydroxycinnamic acid (pCA2-) and its amide derivative (pCM-) in their deprotonated forms, undergo a transcis photoisomerization whereas the thioester derivative, trans-p-hydroxythiophenyl cinnamate (pCT-), does not. pCT- is also the only one to exhibit a short-lived intermediate on its excited-state deactivation pathway. We here further stress the existence of two different relaxation mechanisms for these molecules and examine the reaction coordinates involved. We looked at the effect of the solvent properties (viscosity, polarity, solvation dynamics) on their excited-state relaxation dynamics, probed by ultrafast transient absorption spectroscopy. Sensitivity to the solvent properties is found to be larger for pCT- than for pCA2- and pCM-. This difference is considered to reveal that either the relaxation pathway or the reaction coordinate is different for these two classes of analogues. It is also found to be correlated to the electron donor - acceptor character of the molecule. We attribute the excited-state deactivation of analogues bearing a weaker acceptor group, pCA2- and pCM-, to a stilbene-like photoisomerization mechanism with the concerted rotation of the ethylenic bond and one adjacent single bond. For pCT-, which contains a stronger acceptor group, we consider a photoisomerization mechanism mainly involving the single torsion of the ethylenic bond. The excited-state deactivation of pCT - would lead to the formation of a ground-state intermediate at the "perp" geometry, which would return to the initial trans conformation without net isomerization. © 2006 American Chemical Society.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
We previously reported that two analogues of the Photoactive Yellow Protein chromophore, trans-p-hydroxycinnamic acid (pCA2-) and its amide derivative (pCM-) in their deprotonated forms, undergo a transcis photoisomerization whereas the thioester derivative, trans-p-hydroxythiophenyl cinnamate (pCT-), does not. pCT- is also the only one to exhibit a short-lived intermediate on its excited-state deactivation pathway. We here further stress the existence of two different relaxation mechanisms for these molecules and examine the reaction coordinates involved. We looked at the effect of the solvent properties (viscosity, polarity, solvation dynamics) on their excited-state relaxation dynamics, probed by ultrafast transient absorption spectroscopy. Sensitivity to the solvent properties is found to be larger for pCT- than for pCA2- and pCM-. This difference is considered to reveal that either the relaxation pathway or the reaction coordinate is different for these two classes of analogues. It is also found to be correlated to the electron donor - acceptor character of the molecule. We attribute the excited-state deactivation of analogues bearing a weaker acceptor group, pCA2- and pCM-, to a stilbene-like photoisomerization mechanism with the concerted rotation of the ethylenic bond and one adjacent single bond. For pCT-, which contains a stronger acceptor group, we consider a photoisomerization mechanism mainly involving the single torsion of the ethylenic bond. The excited-state deactivation of pCT - would lead to the formation of a ground-state intermediate at the "perp" geometry, which would return to the initial trans conformation without net isomerization. © 2006 American Chemical Society. |
Ultrafast photoisomerization of photoactive yellow protein chromophore analogues in solution: Influence of the protonation state Article de journal A Espagne; D H Paik; P Changenet-Barret; M M Martin; A H Zewail ChemPhysChem, 7 (8), p. 1717–1726, 2006. @article{Espagne:2006b,
title = {Ultrafast photoisomerization of photoactive yellow protein chromophore analogues in solution: Influence of the protonation state},
author = {A Espagne and D H Paik and P Changenet-Barret and M M Martin and A H Zewail},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-33748194569&doi=10.1002%2fcphc.200600137&partnerID=40&md5=1e4642cd9b9e7e944526096c65c4fc00},
doi = {10.1002/cphc.200600137},
year = {2006},
date = {2006-01-01},
journal = {ChemPhysChem},
volume = {7},
number = {8},
pages = {1717--1726},
abstract = {We investigate solvent viscosity and polarity effects on the photoisomerization of the protonated and deprotonated forms of two analogues of the photoactive yellow protein (PYP) chromophore. These are trans-p- hydroxybenzylidene acetone and trans-p-hydroxyphenyl cinnamate, studied in solutions of different polarity and viscosity at room temperature, by means of femtosecond fluorescence up-conversion. The fluorescence lifetimes of the protonated forms are found to be barely sensitive to solvent viscosity, and to increase with increasing solvent polarity. In contrast, the fluorescence decays of the deprotonated forms are significantly slowed down in viscous media and accelerated in polar solvents. These results elucidate the dramatic influence of the protonation state of the PYP chromophore analogues on their photoinduced dynamics. The viscosity and polarity effects are, respectively, interpreted in terms of different isomerization coordinates and charge redistribution in S 1. A trans-to-cis isomerization mechanism involving mainly the ethylenic double-bond torsion and/or salvation is proposed for the anionic forms, whereas "concerted" intramolecular motions are proposed for the neutral forms. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
We investigate solvent viscosity and polarity effects on the photoisomerization of the protonated and deprotonated forms of two analogues of the photoactive yellow protein (PYP) chromophore. These are trans-p- hydroxybenzylidene acetone and trans-p-hydroxyphenyl cinnamate, studied in solutions of different polarity and viscosity at room temperature, by means of femtosecond fluorescence up-conversion. The fluorescence lifetimes of the protonated forms are found to be barely sensitive to solvent viscosity, and to increase with increasing solvent polarity. In contrast, the fluorescence decays of the deprotonated forms are significantly slowed down in viscous media and accelerated in polar solvents. These results elucidate the dramatic influence of the protonation state of the PYP chromophore analogues on their photoinduced dynamics. The viscosity and polarity effects are, respectively, interpreted in terms of different isomerization coordinates and charge redistribution in S 1. A trans-to-cis isomerization mechanism involving mainly the ethylenic double-bond torsion and/or salvation is proposed for the anionic forms, whereas "concerted" intramolecular motions are proposed for the neutral forms. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA. |
Vibrational Couplings and Ultrafast Relaxation of the O-Ħ Bending Mode in Liquid H2O Article de journal S Ashihara; N Huse; A Espagne; E T J Nibbering; T Elsaesser Chemical Physics Letters, 424 (1-3), p. 66-70, 2006, ISSN: 0009-2614. @article{RN54b,
title = {Vibrational Couplings and Ultrafast Relaxation of the O-{H} Bending Mode in Liquid H2O},
author = {S Ashihara and N Huse and A Espagne and E T J Nibbering and T Elsaesser},
doi = {10.1016/j.cplett.2006.04.051},
issn = {0009-2614},
year = {2006},
date = {2006-01-01},
journal = {Chemical Physics Letters},
volume = {424},
number = {1-3},
pages = {66-70},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
