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000052270 084__ $$2WoS$$aBiophysics
000052270 1001_ $$0P:(DE-Juel1)VDB4616$$aEfremov, R.$$b0$$uFZJ
000052270 245__ $$aTime-resolved microscopy on a single crystal of bacteriorhodopsin reveals lattice induced differences in the photocycle kinetics
000052270 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2006
000052270 300__ $$a1441 - 1451
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000052270 440_0 $$0882$$aBiophysical Journal$$v91$$x0006-3495
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000052270 520__ $$aThe determination of the intermediate state structures of the bacteriorhodopsin photocycle has lead to an unprecedented level of understanding of the catalytic process exerted by a membrane protein. However, the crystallographic structures of the intermediate states are only relevant if the working cycle is not impaired by the crystal lattice. Therefore, we applied visible and Fourier transform infrared spectroscopy (FTIR) microspectroscopy with microsecond time resolution to compare the photoreaction of a single bacteriorhodopsin crystal to that of bacteriorhodopsin residing in the native purple membrane. The analysis of the FTIR difference spectra of the resolved intermediate states reveals great similarity in structural changes taking place in the crystal and in PM. However, the kinetics of the photocycle are significantly altered in the three-dimensional crystal as compared to PM. Strikingly, the L state decay is accelerated in the crystal, whereas the M decay is delayed. The physical origin of this deviation and the implications for trapping of intermediate states are discussed. As a methodological advance, time-resolved step-scan FTIR spectroscopy on a single protein crystal is demonstrated for the first time which may be used in the future to gauge the functionality of other crystallized proteins with the molecular resolution of vibrational spectroscopy.
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000052270 650_2 $$2MeSH$$aBacteriorhodopsins: chemistry
000052270 650_2 $$2MeSH$$aBacteriorhodopsins: radiation effects
000052270 650_2 $$2MeSH$$aBacteriorhodopsins: ultrastructure
000052270 650_2 $$2MeSH$$aCrystallography: methods
000052270 650_2 $$2MeSH$$aDose-Response Relationship, Radiation
000052270 650_2 $$2MeSH$$aKinetics
000052270 650_2 $$2MeSH$$aLight
000052270 650_2 $$2MeSH$$aPhotobiology: methods
000052270 650_2 $$2MeSH$$aPhotochemistry: methods
000052270 650_2 $$2MeSH$$aRadiation Dosage
000052270 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: methods
000052270 650_2 $$2MeSH$$aTime Factors
000052270 650_7 $$053026-44-1$$2NLM Chemicals$$aBacteriorhodopsins
000052270 650_7 $$2WoSType$$aJ
000052270 7001_ $$0P:(DE-Juel1)VDB482$$aGordeliy, V. I.$$b1$$uFZJ
000052270 7001_ $$0P:(DE-HGF)0$$aHeberle, J.$$b2
000052270 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b3$$uFZJ
000052270 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.106.083345$$gVol. 91, p. 1441 - 1451$$p1441 - 1451$$q91<1441 - 1451$$tBiophysical journal$$v91$$x0006-3495$$y2006
000052270 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1518640
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