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Probing the decay coordinate of the green fluorescent protein: arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra.
J Am Chem Soc. 2006 Feb 08; 128(5):1540-6.JA

Abstract

The fluorescence spectra of the wild-type green fluorescence protein (wt-GFP) and the anionic form of p-hydroxybenzylidenedimethylimidazolone (p-HBDI), which models the protein chromophore, were obtained in the 80-300 K temperature range in glycerol/water solvent. The protein spectra have pronounced and well-resolved vibronic structure, at least at lower temperatures. In contrast, the chromophore spectra are very broad and structureless even at the lowest temperatures. Analysis of the spectra shows that the experimentally observed red-shift of the protein spectrum upon heating is apparently caused by quadratic vibronic coupling of the torsional deformation (TD) of the phenyl single bond of the chromophore to the electronic transition. The broad spectra of the chromophore manifest the contribution of different conformations in the glycerol/water solvent. In particular, the lowest-temperature spectrum reflects the distribution over the same TD coordinate in the excited electronic state, which essentially contributes to the asymmetry of the spectrum. Upon heating, motion along this coordinate leads to a configuration from which the radiationless transition takes place. This narrows the distribution along the TD coordinate, causing a more symmetric fluorescence spectrum. We were able to reconstruct the broad, structureless fluorescence spectra of p-HBDI in glycerol/water solutions at various temperatures by convoluting the original wt-GFP spectra with the function describing the distribution of the transition energies of the p-HBDI chromophore. Thus, both the fluorescence broadening and increase in radiationless transition upon removal of the protein chromophore to bulk solvent are consistent with decay by a barrierless TD of the phenyl single bond.

Authors+Show Affiliations

Sackler Faculty of Medicine, Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Tel Aviv University, Tel Aviv 69978, Israel.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

16448124

Citation

Stavrov, Solomon S., et al. "Probing the Decay Coordinate of the Green Fluorescent Protein: Arrest of Cis-trans Isomerization By the Protein Significantly Narrows the Fluorescence Spectra." Journal of the American Chemical Society, vol. 128, no. 5, 2006, pp. 1540-6.
Stavrov SS, Solntsev KM, Tolbert LM, et al. Probing the decay coordinate of the green fluorescent protein: arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra. J Am Chem Soc. 2006;128(5):1540-6.
Stavrov, S. S., Solntsev, K. M., Tolbert, L. M., & Huppert, D. (2006). Probing the decay coordinate of the green fluorescent protein: arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra. Journal of the American Chemical Society, 128(5), 1540-6.
Stavrov SS, et al. Probing the Decay Coordinate of the Green Fluorescent Protein: Arrest of Cis-trans Isomerization By the Protein Significantly Narrows the Fluorescence Spectra. J Am Chem Soc. 2006 Feb 8;128(5):1540-6. PubMed PMID: 16448124.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Probing the decay coordinate of the green fluorescent protein: arrest of cis-trans isomerization by the protein significantly narrows the fluorescence spectra. AU - Stavrov,Solomon S, AU - Solntsev,Kyril M, AU - Tolbert,Laren M, AU - Huppert,Dan, PY - 2006/2/2/pubmed PY - 2006/4/4/medline PY - 2006/2/2/entrez SP - 1540 EP - 6 JF - Journal of the American Chemical Society JO - J Am Chem Soc VL - 128 IS - 5 N2 - The fluorescence spectra of the wild-type green fluorescence protein (wt-GFP) and the anionic form of p-hydroxybenzylidenedimethylimidazolone (p-HBDI), which models the protein chromophore, were obtained in the 80-300 K temperature range in glycerol/water solvent. The protein spectra have pronounced and well-resolved vibronic structure, at least at lower temperatures. In contrast, the chromophore spectra are very broad and structureless even at the lowest temperatures. Analysis of the spectra shows that the experimentally observed red-shift of the protein spectrum upon heating is apparently caused by quadratic vibronic coupling of the torsional deformation (TD) of the phenyl single bond of the chromophore to the electronic transition. The broad spectra of the chromophore manifest the contribution of different conformations in the glycerol/water solvent. In particular, the lowest-temperature spectrum reflects the distribution over the same TD coordinate in the excited electronic state, which essentially contributes to the asymmetry of the spectrum. Upon heating, motion along this coordinate leads to a configuration from which the radiationless transition takes place. This narrows the distribution along the TD coordinate, causing a more symmetric fluorescence spectrum. We were able to reconstruct the broad, structureless fluorescence spectra of p-HBDI in glycerol/water solutions at various temperatures by convoluting the original wt-GFP spectra with the function describing the distribution of the transition energies of the p-HBDI chromophore. Thus, both the fluorescence broadening and increase in radiationless transition upon removal of the protein chromophore to bulk solvent are consistent with decay by a barrierless TD of the phenyl single bond. SN - 0002-7863 UR - https://www.unboundmedicine.com/medline/citation/16448124/Probing_the_decay_coordinate_of_the_green_fluorescent_protein:_arrest_of_cis_trans_isomerization_by_the_protein_significantly_narrows_the_fluorescence_spectra_ L2 - https://doi.org/10.1021/ja0555421 DB - PRIME DP - Unbound Medicine ER -