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000051340 084__ $$2WoS$$aMultidisciplinary Sciences
000051340 1001_ $$0P:(DE-HGF)0$$aSchenkl, S.$$b0
000051340 245__ $$aInsights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption
000051340 260__ $$aWashington, DC$$bAcademy$$c2006
000051340 300__ $$a4101 - 4106
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000051340 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v103$$x0027-8424$$y11
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000051340 520__ $$aA 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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000051340 650_2 $$2MeSH$$aBacteriorhodopsins: chemistry
000051340 650_2 $$2MeSH$$aBacteriorhodopsins: genetics
000051340 650_2 $$2MeSH$$aBiophysical Phenomena
000051340 650_2 $$2MeSH$$aBiophysics
000051340 650_2 $$2MeSH$$aHalobacterium salinarum: chemistry
000051340 650_2 $$2MeSH$$aHalobacterium salinarum: genetics
000051340 650_2 $$2MeSH$$aIsomerism
000051340 650_2 $$2MeSH$$aKinetics
000051340 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000051340 650_2 $$2MeSH$$aSpectrophotometry, Ultraviolet
000051340 650_2 $$2MeSH$$aThermodynamics
000051340 650_2 $$2MeSH$$aTryptophan: chemistry
000051340 650_7 $$053026-44-1$$2NLM Chemicals$$aBacteriorhodopsins
000051340 650_7 $$073-22-3$$2NLM Chemicals$$aTryptophan
000051340 650_7 $$2WoSType$$aJ
000051340 65320 $$2Author$$aultrafast spectroscopy
000051340 65320 $$2Author$$aretinal proteins
000051340 65320 $$2Author$$atranslocation of charge
000051340 65320 $$2Author$$astructural dynamics
000051340 7001_ $$0P:(DE-HGF)0$$avan Mourik, F.$$b1
000051340 7001_ $$0P:(DE-HGF)0$$aFriedman, N.$$b2
000051340 7001_ $$0P:(DE-HGF)0$$aSheves, M.$$b3
000051340 7001_ $$0P:(DE-Juel1)VDB1421$$aSchlesinger, R.$$b4$$uFZJ
000051340 7001_ $$0P:(DE-HGF)0$$aHaacke, S.$$b5
000051340 7001_ $$0P:(DE-HGF)0$$aChergui, M.$$b6
000051340 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.0506303103$$gVol. 103, p. 4101 - 4106$$p4101 - 4106$$q103<4101 - 4106$$tProceedings of the National Academy of Sciences of the United States of America$$v103$$x0027-8424$$y2006
000051340 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1449653
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