Home > Publications database > Insights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption > print

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017 _ _ |a This version is available at http://www.pnas.org, http://dx.doi.org/10.1073/pnas.0506303103
024 7 _ |a pmid:16537491
|2 pmid
024 7 _ |a pmc:PMC1449653
|2 pmc
024 7 _ |a 10.1073/pnas.0506303103
|2 DOI
024 7 _ |a WOS:000236429300032
|2 WOS
024 7 _ |a 2128/2655
|2 Handle
037 _ _ |a PreJuSER-51340
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |a Schenkl, S.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Insights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption
260 _ _ |a Washington, DC
|b Academy
|c 2006
300 _ _ |a 4101 - 4106
336 7 _ |a Journal Article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
|2 DRIVER
440 _ 0 |a Proceedings of the National Academy of Sciences of the United States of America
|x 0027-8424
|0 5100
|y 11
|v 103
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a A visible-pump/UV-probe transient absorption is used to characterize the ultrafast dynamics of bacteriorhodopsin with 80-fs time resolution. We identify three spectral components in the 265- to 310-nm region, related to the all-trans retinal, tryptophan (Trp)-86 and the isomerized photoproduct, allowing us to map the dynamics from reactants to products, along with the response of Trp amino acids. The signal of the photoproduct appears with a time delay of approximately 250 fs and is characterized by a steep rise ( approximately 150 fs), followed by additional rise and decay components, with time scales characteristic of the J intermediate. The delayed onset and the steep rise point to an impulsive formation of a transition state on the way to isomerization. We argue that this impulsive formation results from a splitting of a wave packet of torsional modes on the potential surface at the branching between the all-trans and the cis forms. Parallel to these dynamics, the signal caused by Trp response rises in approximately 200 fs, because of the translocation of charge along the conjugate chain, and possible mechanisms are presented, which trigger isomerization.
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: chemistry
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: genetics
650 _ 2 |2 MeSH
|a Biophysical Phenomena
650 _ 2 |2 MeSH
|a Biophysics
650 _ 2 |2 MeSH
|a Halobacterium salinarum: chemistry
650 _ 2 |2 MeSH
|a Halobacterium salinarum: genetics
650 _ 2 |2 MeSH
|a Isomerism
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Mutagenesis, Site-Directed
650 _ 2 |2 MeSH
|a Spectrophotometry, Ultraviolet
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 2 |2 MeSH
|a Tryptophan: chemistry
650 _ 7 |0 53026-44-1
|2 NLM Chemicals
|a Bacteriorhodopsins
650 _ 7 |0 73-22-3
|2 NLM Chemicals
|a Tryptophan
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a ultrafast spectroscopy
653 2 0 |2 Author
|a retinal proteins
653 2 0 |2 Author
|a translocation of charge
653 2 0 |2 Author
|a structural dynamics
700 1 _ |a van Mourik, F.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Friedman, N.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Sheves, M.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Schlesinger, R.
|b 4
|u FZJ
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700 1 _ |a Haacke, S.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Chergui, M.
|b 6
|0 P:(DE-HGF)0
773 _ _ |a 10.1073/pnas.0506303103
|g Vol. 103, p. 4101 - 4106
|p 4101 - 4106
|q 103<4101 - 4106
|0 PERI:(DE-600)1461794-8
|t Proceedings of the National Academy of Sciences of the United States of America
|v 103
|y 2006
|x 0027-8424
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1449653
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