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Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation.

Ludmila P BurakovaMaria S LyakhovichKonstantin S MineevValentin N PetushkovRenata I ZagitovaAleksandra S TsarkovaSergey I KovalchukIlia V YampolskyEugene S VysotskiZinaida M Kaskova
Published in: Organic letters (2021)
Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photoinactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.
Keyphrases
  • visible light
  • transcription factor
  • living cells
  • high resolution
  • protein protein
  • amino acid
  • cell free
  • energy transfer
  • protein kinase
  • radiation therapy
  • fluorescent probe
  • single molecule