001     46162
005     20200423204146.0
024 7 _ |a pmid:15969574
|2 pmid
024 7 _ |a 10.1021/ja047023o
|2 DOI
024 7 _ |a WOS:000230010600037
|2 WOS
024 7 _ |a 2128/681
|2 Handle
037 _ _ |a PreJuSER-46162
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Chemistry, Multidisciplinary
100 1 _ |a Habuchi, S.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Evidence for the isomerization and decarboxylation in the photoconversion of the red fluorescent protein DsRed
260 _ _ |a Washington, DC
|b American Chemical Society
|c 2005
300 _ _ |a 8977 - 8984
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of the American Chemical Society
|x 0002-7863
|0 8502
|v 127
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Recently, 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.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Decarboxylation
650 _ 2 |2 MeSH
|a Isomerism
650 _ 2 |2 MeSH
|a Lasers
650 _ 2 |2 MeSH
|a Luminescent Proteins: chemistry
650 _ 2 |2 MeSH
|a Luminescent Proteins: radiation effects
650 _ 2 |2 MeSH
|a Molecular Structure
650 _ 2 |2 MeSH
|a Photolysis
650 _ 2 |2 MeSH
|a Time Factors
650 _ 7 |0 0
|2 NLM Chemicals
|a Luminescent Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a fluorescent protein 583
650 _ 7 |a J
|2 WoSType
700 1 _ |a Cotlet, M.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Gensch, T.
|b 2
|u FZJ
|0 P:(DE-Juel1)131924
700 1 _ |a Bednarz, T.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB37437
700 1 _ |a Haber-Pohlmeier, S.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB12272
700 1 _ |a Rozenski, J.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Dirix, G.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Michiels, J.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Vanderleyden, J.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 9
|u FZJ
|0 P:(DE-Juel1)VDB572
700 1 _ |a de Schryver, F. C.
|b 10
|0 P:(DE-HGF)0
700 1 _ |a Hofkens, J.
|b 11
|0 P:(DE-HGF)0
773 _ _ |a 10.1021/ja047023o
|g Vol. 127, p. 8977 - 8984
|p 8977 - 8984
|q 127<8977 - 8984
|0 PERI:(DE-600)1472210-0
|t Journal of the American Chemical Society
|v 127
|y 2005
|x 0002-7863
856 7 _ |u http://dx.doi.org/10.1021/ja047023o
|u http://hdl.handle.net/2128/681
856 4 _ |u https://juser.fz-juelich.de/record/46162/files/72326.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/46162/files/72326.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/46162/files/72326.jpg?subformat=icon-180
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|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/46162/files/72326.jpg?subformat=icon-640
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|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:46162
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913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2005
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
915 _ _ |2 StatID
|0 StatID:(DE-HGF)0510
|a OpenAccess
920 1 _ |k IBI-1
|l Zelluläre Signalverarbeitung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB57
|x 0
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 1
970 _ _ |a VDB:(DE-Juel1)72326
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