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| Autor | Lars V. Schäfer / Gerrit Groenhof / Astrid R. Klingen / G. Matthias Ullmann / Martial Boggio-Pasqua / Michael A. Robb / Helmut Grubmüller |
| Titel | Photoswitching of the Fluorescent Protein asFP595: Mechanism, Proton Pathways, and Absorption Spectra |
| Zeitschrift | Angew. Chem. |
| Jahr | 2007 |
| Seiten | 536 –542 |
| DOI | 10.1002/ange.200602315 |
Literaturverz. |
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| Fußnoten | yes |
| Fragmente | 2 |
| [1.] Tim/Fragment 015 11 - Diskussion Zuletzt bearbeitet: 2014-10-27 05:38:51 Hindemith | BauernOpfer, Fragment, Gesichtet, SMWFragment, Schaefer 2007, Schutzlevel sysop, Tim |
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| Untersuchte Arbeit: Seite: 15, Zeilen: 11-15 |
Quelle: Schaefer 2007 Seite(n): 540, Zeilen: l.col.: 3 ff. |
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| The proposed kindling mechanism (Schafer et al., 2007; Andresen et al., 2005) is depicted in figure 8. Before the photon absorption the chromophore is in the dark zwitterionic trans state but when the photon arrives it changes in the cis state. The isomerization increases the acidity of the imidazolinone NH proton of the zwitterionic cis chromophore and induces proton transfer to Glu215 (state A-cis, figure 8).
Whether this proton transfer takes place in the electronic ground state or in the excited state cannot be judged on the basis of the current simulations. The proton transfer also [prevents photoisomerization of the zwitterionic cis species back to the initial dark trans state.] |
The proposed kindling mechanism is depicted in Figure 3. As shown previously, kindling is initiated by a trans–cis photoisomerization through a space-saving hula-twist mechanism.[ 11] The isomerization increases the acidity of the imidazolinone NH proton of the zwitterionic cis chromophore and induces proton transfer to Glu215 (state A-cis, Figure 3). Whether this proton transfer takes place in the electronic ground state or in the excited state cannot be judged on the basis of the current simulations. The proton transfer also prevents photoisomerization of the zwitterionic cis species back to the initial dark trans state. |
The source is given together with another source such that a literal quote cannot be understood. This is particularly the case in the second paragraph, as it describes "current simulations". |
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| [2.] Tim/Fragment 016 01 - Diskussion Zuletzt bearbeitet: 2014-10-27 05:46:23 Hindemith | BauernOpfer, Fragment, Gesichtet, SMWFragment, Schaefer 2007, Schutzlevel sysop, Tim |
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| Untersuchte Arbeit: Seite: 16, Zeilen: 1-7 |
Quelle: Schaefer 2007 Seite(n): 540, Zeilen: l.col.: 11 ff. |
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| [The proton transfer also] prevents photoisomerization of the zwitterionic cis species back to the initial dark trans state. The anionic cis intermediate is subsequently protonated at the phenolate oxygen atom to finally yield the stable neutral chromophore (state N-cis).
This situation is similar to that in GFP, where the neutral protonation state is also favored for the cis chromophore (Helms, 2002; Stoner-Ma et al., 2005; Agmon, 2005; Leiderman et al., 2006; Vendrell et al., 2006). GFP fluorescence originates from the anionic chromophore, which is formed through excited-state proton transfer (ESPT). |
The proton transfer also prevents photoisomerization of the zwitterionic cis species back to the initial dark trans state. The anionic cis intermediate is subsequently protonated at the phenolate oxygen atom to finally yield the stable neutral chromophore (state Ncis). This situation is similar to that in GFP, where the neutral protonation state is also favored for the cis chromophore.[16–20] GFP fluorescence originates from the anionic chromophore, which is formed through excited-state proton transfer (ESPT).
[16] V. Helms, Curr. Opin. Struct. Biol. 2002, 12, 169. [17] D. Stoner-Ma, A. A. Jaye, P. Matousek, M. Towrie, S. R. Meech, P. J. Tonge, J. Am. Chem. Soc. 2005, 127, 2864. [18] N. Agmon, Biophys. J. 2005, 88, 2452. [19] P. Leiderman, D. Huppert, N. Agmon, Biophys. J. 2006, 90, 1009. [20] O. Vendrell, R. Gelabert, M. Moreno, J. M. Lluch, J. Am. Chem. Soc. 2006, 128, 3564. |
The source is given on the previous page. |
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