Hauptseite > Publikationsdatenbank > The two photocycles of photoactive yellow protein from Rhodobacter sphaeroides > print

001     28482
005     20200423203444.0
024 7 _ |a pmid:12496261
|2 pmid
024 7 _ |a 10.1074/jbc.M209343200
|2 DOI
024 7 _ |a WOS:000181466800091
|2 WOS
024 7 _ |a 2128/2642
|2 Handle
037 _ _ |a PreJuSER-28482
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Haker, A.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a The two photocycles of photoactive yellow protein from Rhodobacter sphaeroides
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2003
300 _ _ |a 8442 - 8451
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
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336 7 _ |a Output Types/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 Journal of Biological Chemistry
|x 0021-9258
|0 3091
|y 10
|v 278
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The absorption spectrum of the photoactive yellow protein from Rhodobacter sphaeroides (R-PYP) shows two maxima, absorbing at 360 nm (R-PYP(360)) and 446 nm (R-PYP(446)), respectively. Both forms are photoactive and part of a temperature- and pH-dependent equilibrium (Haker, A., Hendriks, J., Gensch, T., Hellingwerf, K. J., and Crielaard, W. (2000) FEBS Lett. 486, 52-56). At 20 degrees C, for PYP characteristic, the 446-nm absorbance band displays a photocycle, in which the depletion of the 446-nm ground state absorption occurs in at least three phases, with time constants of <30 ns, 0.5 micros, and 17 micros. Intermediates with both blue- and red-shifted absorption maxima are transiently formed, before a blue-shifted intermediate (pB(360), lambda(max) = 360 nm) is established. The photocycle is completed with a monophasic recovery of the ground state with a time constant of 2.5 ms. At 7 degrees C these photocycle transitions are slowed down 2- to 3-fold. Upon excitation of R-PYP(360) with a UV-flash (330 +/- 50 nm) a species with a difference absorption maximum at approximately 435 nm is observed that returns to R-PYP(360) on a minute time scale. Recovery can be accelerated by a blue light flash (450 nm). R-PYP(360) and R-PYP(446) differ in their overall protein conformation, as well as in the isomerization and protonation state of the chromophore, as determined with the fluorescent polarity probe Nile Red and Fourier Transform Infrared spectroscopy, respectively.
536 _ _ |a Neurowissenschaften
|c L01
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: physiology
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Photoreceptors, Microbial: chemistry
650 _ 2 |2 MeSH
|a Photoreceptors, Microbial: physiology
650 _ 2 |2 MeSH
|a Photosynthesis
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Rhodobacter sphaeroides: physiology
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 2 |2 MeSH
|a Spectroscopy, Fourier Transform Infrared
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Photoreceptors, Microbial
650 _ 7 |0 0
|2 NLM Chemicals
|a photoactive yellow protein, Bacteria
650 _ 7 |a J
|2 WoSType
700 1 _ |a Hendriks, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a van Stokkum, I. H. M.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB572
700 1 _ |a Hellingwerf, K. J.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Crielaard, W.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Gensch, T.
|b 6
|u FZJ
|0 P:(DE-Juel1)131924
773 _ _ |a 10.1074/jbc.M209343200
|g Vol. 278, p. 8442 - 8451
|p 8442 - 8451
|q 278<8442 - 8451
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 278
|y 2003
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbc.M209343200
|u http://hdl.handle.net/2128/2642
856 4 _ |u https://juser.fz-juelich.de/record/28482/files/22133.pdf
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