ArticleProceedings of the National Academy of Sciences of the United States of America2009
Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Dynamic Equilibrium between the Fluorescent State of Tryptophan and Its Cation-Electron Ion Pair Governs Triplet State Population.Journal of the American Chemical Society · 2025Article
- Ultrafast terahertz Stark spectroscopy reveals the excited-state dipole moments of retinal in bacteriorhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ultraviolet Superradiance from Mega-Networks of Tryptophan in Biological Architectures.The journal of physical chemistry. B · 2024Article
- Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin.Nature communications · 2019Article
- Oxidative species-induced excitonic transport in tubulin aromatic networks: Potential implications for neurodegenerative disease.Journal of photochemistry and photobiology. B, Biology · 2017Article
- The feasibility of coherent energy transfer in microtubules.Journal of the Royal Society, Interface · 2014Article
- Full-Quantum chemical calculation of the absorption maximum of bacteriorhodopsin: a comprehensive analysis of the amino acid residues contributing to the opsin shift.Biophysics (Nagoya-shi, Japan) · 2012Article
- Carotenoid response to retinal excitation and photoisomerization dynamics in xanthorhodopsin.Chemical physics letters · 2011Article
- Two-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: a first principles study.Physical chemistry chemical physics : PCCP · 2011Article
- Aborted double bicycle-pedal isomerization with hydrogen bond breaking is the primary event of bacteriorhodopsin proton pumping.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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8 authors.
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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 approximately 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(86) undergoes a significant Stark shift induced by the transient retinal dipole moment. The corresponding transient signal can be isolated by direct subtraction of experimental data obtained for WT bR and W86F. It shows an instantaneous rise, followed by a decay over approximately 500 fs corresponding to the isomerization time. Interestingly, it does not decay back to zero, thus revealing a change in the local electrostatic environment that remains long after isomerization, in the K intermediate state of the protein cycle. The comparison of WT bR and W86F also leads to a revised interpretation of the overall transient UV absorption of bR.
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