Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues

J. Leonard; E. Portuondo-Campa; A. Cannizzo; F. van Mourik; G. van der Zwan; J. Tittor; S. Haacke; M. Chergui

doi:10.1073/pnas.0812877106

Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues

J. Leonard, E. Portuondo-Campa, A. Cannizzo, F. van Mourik, G. van der Zwan, J. Tittor, S. Haacke, M. Chergui

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Ultrafast transient absorption spectroscopy of wild-type bacteriorhodopsin (WT bR) and 2 tryptophan mutants (W86F and W182F) is performed with visible light excitation (pump) and UV probe. The aim is to investigate the photoinduced change in the charge distribution with 50-fs time resolution by probing the effects on the tryptophan absorption bands. A systematic, quantitative comparison of the transient absorption of the 3 samples is carried out. The main result is the absence in the W86F mutant of a transient induced absorption band observed at ≈300-310 nm in WT bR and W182F. A simple model describing the dipolar interaction of the retinal moiety with the 2 tryptophan residues of interest allows us to reproduce the dominant features of the transient signals observed in the 3 samples at ultrashort pump-probe delays. In particular, we show that Trp

Original language	English
Pages (from-to)	7718-23
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	106
Issue number	19
DOIs	https://doi.org/10.1073/pnas.0812877106
Publication status	Published - 2009

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Leonard, J., Portuondo-Campa, E., Cannizzo, A., van Mourik, F., van der Zwan, G., Tittor, J., Haacke, S., & Chergui, M. (2009). Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues. Proceedings of the National Academy of Sciences of the United States of America, 106(19), 7718-23. https://doi.org/10.1073/pnas.0812877106

@article{73b905664c124a8b94d3e732e7e19d3c,

title = "Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues",

abstract = "Ultrafast transient absorption spectroscopy of wild-type bacteriorhodopsin (WT bR) and 2 tryptophan mutants (W86F and W182F) is performed with visible light excitation (pump) and UV probe. The aim is to investigate the photoinduced change in the charge distribution with 50-fs time resolution by probing the effects on the tryptophan absorption bands. A systematic, quantitative comparison of the transient absorption of the 3 samples is carried out. The main result is the absence in the W86F mutant of a transient induced absorption band observed at ≈300-310 nm in WT bR and W182F. A simple model describing the dipolar interaction of the retinal moiety with the 2 tryptophan residues of interest allows us to reproduce the dominant features of the transient signals observed in the 3 samples at ultrashort pump-probe delays. In particular, we show that Trp",

author = "J. Leonard and E. Portuondo-Campa and A. Cannizzo and {van Mourik}, F. and {van der Zwan}, G. and J. Tittor and S. Haacke and M. Chergui",

year = "2009",

doi = "10.1073/pnas.0812877106",

language = "English",

volume = "106",

pages = "7718--23",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Acad Sciences",

number = "19",

}

Leonard, J, Portuondo-Campa, E, Cannizzo, A, van Mourik, F, van der Zwan, G, Tittor, J, Haacke, S & Chergui, M 2009, 'Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues', Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 19, pp. 7718-23. https://doi.org/10.1073/pnas.0812877106

Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues. / Leonard, J.; Portuondo-Campa, E.; Cannizzo, A. et al.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, No. 19, 2009, p. 7718-23.

Research output: Contribution to Journal › Article › Academic › peer-review

TY - JOUR

T1 - Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues

AU - Leonard, J.

AU - Portuondo-Campa, E.

AU - Cannizzo, A.

AU - van Mourik, F.

AU - van der Zwan, G.

AU - Tittor, J.

AU - Haacke, S.

AU - Chergui, M.

PY - 2009

Y1 - 2009

N2 - Ultrafast transient absorption spectroscopy of wild-type bacteriorhodopsin (WT bR) and 2 tryptophan mutants (W86F and W182F) is performed with visible light excitation (pump) and UV probe. The aim is to investigate the photoinduced change in the charge distribution with 50-fs time resolution by probing the effects on the tryptophan absorption bands. A systematic, quantitative comparison of the transient absorption of the 3 samples is carried out. The main result is the absence in the W86F mutant of a transient induced absorption band observed at ≈300-310 nm in WT bR and W182F. A simple model describing the dipolar interaction of the retinal moiety with the 2 tryptophan residues of interest allows us to reproduce the dominant features of the transient signals observed in the 3 samples at ultrashort pump-probe delays. In particular, we show that Trp

AB - Ultrafast transient absorption spectroscopy of wild-type bacteriorhodopsin (WT bR) and 2 tryptophan mutants (W86F and W182F) is performed with visible light excitation (pump) and UV probe. The aim is to investigate the photoinduced change in the charge distribution with 50-fs time resolution by probing the effects on the tryptophan absorption bands. A systematic, quantitative comparison of the transient absorption of the 3 samples is carried out. The main result is the absence in the W86F mutant of a transient induced absorption band observed at ≈300-310 nm in WT bR and W182F. A simple model describing the dipolar interaction of the retinal moiety with the 2 tryptophan residues of interest allows us to reproduce the dominant features of the transient signals observed in the 3 samples at ultrashort pump-probe delays. In particular, we show that Trp

U2 - 10.1073/pnas.0812877106

DO - 10.1073/pnas.0812877106

M3 - Article

VL - 106

SP - 7718

EP - 7723

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 19

ER -

Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues

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