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000046162 0247_ $$2DOI$$a10.1021/ja047023o
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000046162 084__ $$2WoS$$aChemistry, Multidisciplinary
000046162 1001_ $$0P:(DE-HGF)0$$aHabuchi, S.$$b0
000046162 245__ $$aEvidence for the isomerization and decarboxylation in the photoconversion of the red fluorescent protein DsRed
000046162 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2005
000046162 300__ $$a8977 - 8984
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000046162 440_0 $$08502$$aJournal of the American Chemical Society$$v127$$x0002-7863
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000046162 520__ $$aRecently, it has been shown that the red fluorescent protein DsRed undergoes photoconversion on intense irradiation, but the mechanism of the conversion has not yet been elucidated. Upon irradiation with a nanosecond-pulsed laser at 532 nm, the chromophore of DsRed absorbing at 559 nm and emitting at 583 nm (R form) converts into a super red (SR) form absorbing at 574 nm and emitting at 595 nm. This conversion leads to a significant change in the fluorescence quantum yield from 0.7 to 0.01. Here we demonstrate that the photoconversion is the result of structural changes of the chromophore and one amino acid. Absorption, fluorescence, and vibrational spectroscopy as well as mass spectrometry suggest that a cis-to-trans isomerization of the chromophore and decarboxylation of a glutamate (E215) take place upon irradiation to form SR. At the same time, another photoproduct (B) with an absorption maximum at 386 nm appears upon irradiation. This species is assigned as a protonated form of the DsRed chromophore. It might be a mixture of several protonated DsRed forms as there is at least two ways of formation. Furthermore, the photoconversion of DsRed is proven to occur through a consecutive two-photon absorption process. Our results demonstrate the importance of the chromophore conformation in the ground state on the brightness of the protein as well as the importance of the photon flux to control/avoid the photoconversion process.
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000046162 650_2 $$2MeSH$$aDecarboxylation
000046162 650_2 $$2MeSH$$aIsomerism
000046162 650_2 $$2MeSH$$aLasers
000046162 650_2 $$2MeSH$$aLuminescent Proteins: chemistry
000046162 650_2 $$2MeSH$$aLuminescent Proteins: radiation effects
000046162 650_2 $$2MeSH$$aMolecular Structure
000046162 650_2 $$2MeSH$$aPhotolysis
000046162 650_2 $$2MeSH$$aTime Factors
000046162 650_7 $$00$$2NLM Chemicals$$aLuminescent Proteins
000046162 650_7 $$00$$2NLM Chemicals$$afluorescent protein 583
000046162 650_7 $$2WoSType$$aJ
000046162 7001_ $$0P:(DE-HGF)0$$aCotlet, M.$$b1
000046162 7001_ $$0P:(DE-Juel1)131924$$aGensch, T.$$b2$$uFZJ
000046162 7001_ $$0P:(DE-Juel1)VDB37437$$aBednarz, T.$$b3$$uFZJ
000046162 7001_ $$0P:(DE-Juel1)VDB12272$$aHaber-Pohlmeier, S.$$b4$$uFZJ
000046162 7001_ $$0P:(DE-HGF)0$$aRozenski, J.$$b5
000046162 7001_ $$0P:(DE-HGF)0$$aDirix, G.$$b6
000046162 7001_ $$0P:(DE-HGF)0$$aMichiels, J.$$b7
000046162 7001_ $$0P:(DE-HGF)0$$aVanderleyden, J.$$b8
000046162 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b9$$uFZJ
000046162 7001_ $$0P:(DE-HGF)0$$ade Schryver, F. C.$$b10
000046162 7001_ $$0P:(DE-HGF)0$$aHofkens, J.$$b11
000046162 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/ja047023o$$gVol. 127, p. 8977 - 8984$$p8977 - 8984$$q127<8977 - 8984$$tJournal of the American Chemical Society$$v127$$x0002-7863$$y2005
000046162 8567_ $$uhttp://hdl.handle.net/2128/681$$uhttp://dx.doi.org/10.1021/ja047023o
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000046162 9201_ $$0I:(DE-Juel1)VDB57$$d31.12.2006$$gIBI$$kIBI-1$$lZelluläre Signalverarbeitung$$x0
000046162 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x1
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