Concerning the thermal diastereomerization of the green fluorescent protein chromophore

Beate Hager, Bettina Schwarzinger, Heinz Falk

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

Two model compounds for the green fluorescent protein chromophore were prepared. One of them incorporates the natural 4-hydroxybenzylidene group of the natural tyrosin derived chromophore, the other one bears a methyl group instead of the hydroxy group. Whereas the photochemically prepared (E)-diastereomer of the first compound very effectively reverted thermally (room temperature) to the thermodynamically stable (Z)-diastereomer, the (E)-diastereomer of the second derivative proved to be stable even at elevated temperatures for more than a day. This finding can be rationalized by constructing the appropriate resonance structures showing that only in the first case an effective delocalization enables partial single bond character of the benzylidene double bond. From the standpoint of chemical etiology, only Nature's choice of the tyrosin derived chromophore of the green fluorescent protein provides an efficient radiationless thermal relaxation channel for the unwanted photo-diastereomerization product formed after excitation besides the dominating fluorescence channel of its chromophore.

Original languageEnglish
Pages (from-to)163-168
Number of pages6
JournalMonatshefte fur Chemie
Volume137
Issue number2
DOIs
Publication statusPublished - Feb 2006
Externally publishedYes

Keywords

  • Benzylideneimidazolinones
  • Chemical etiology
  • Green fluorescent protein
  • Radiationless relaxation
  • Thermal barrier

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