The Thermal Diastereomerization of the Tryptophane-Derived Green Fluorescent Protein Chromophore |
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Authors: | Karoline Fendler Beate Hager Heinz Falk |
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Institution: | (1) Institute of Organic Chemistry, Johannes Kepler University Linz, Linz, Austria |
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Abstract: | Summary. Two model compounds for the tryptophane variant of the green fluorescent protein chromophore containing a 3-indolyl and 2-pyrrolyl
moiety were prepared. For the first one the (Z)-diastereomer was found to be more stable than the (E)-diastereomer by 5.7 kJ mol−1. It could be photo-diastereomerized and its thermal equilibration was studied, whereas the second one underwent photo-destruction.
From an Arrhenius plot an activation barrier for the (E) to (Z) diastereomerization of 85.6 kJ mol−1 could be determined. Thus, it could be demonstrated that in contrast to the corresponding phenyl derivative studied recently
the tyrosine- and tryptophane-derived chromophores of the green fluorescent protein are amenable to fast thermal diastereomerization,
which is of fundamental importance for the fluorescence and photoswitching processes in the corresponding proteins. |
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Keywords: | , Green fluorescent protein, Indolylideneimidazolinones, Thermal barrier, Photoswitching, Radiationless relaxation, |
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