Oxygen activation of Apo-oberlin-Coelenterazine Complex

E. Eremeeva, P.V. Natashin, L. Song, Y. Zhou, W.J.H. van Berkel, Z.J. Liu, E.S. Vysotski

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)

Abstract

Ca2+-regulated photoproteins use a noncovalently bound 2-hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo-obelin–coelenterazine complex and the kinetics of its conversion into active photoprotein after exposure to air. Our studies suggest that coelenterazine bound within the anaerobic complex might be a mixture of N7-protonated and C2(-) anionic forms, and that oxygen shifts the equilibrium in favor of the C2(-) anion as a result of peroxy anion formation. Proton removal from N7 and further protonation of peroxy anion and the resulting formation of 2-hydroperoxycoelenterazine in obelin might occur with the assistance of His175. It is proposed that this conserved His residue might play a key role both in formation of active photoprotein and in Ca2+-triggering of the bioluminescence reaction.
Original languageEnglish
Pages (from-to)739-745
JournalChemBioChem
Volume14
Issue number6
DOIs
Publication statusPublished - 2013

Keywords

  • green-fluorescent protein
  • jellyfish clytia-gregaria
  • crystal-structure
  • ca2+-discharged photoprotein
  • angstrom resolution
  • recombinant obelin
  • molecular-oxygen
  • aequorin
  • calcium
  • bioluminescence

Fingerprint Dive into the research topics of 'Oxygen activation of Apo-oberlin-Coelenterazine Complex'. Together they form a unique fingerprint.

Cite this