Oxygen Activation of Apo-obelin-Coelenterazine Complex

Описание

Тип публикации: статья из журнала

Год издания: 2013

Идентификатор DOI: 10.1002/cbic.201300002

Ключевые слова: aequorin, coelenterazine, luminescence, photoprotein, protein folding, Aequorin, Coelenterazine, Luminescence, Photoprotein, Protein folding, anion, apoprotein, calcium ion, coelenterazine, histidine, oxygen, photoprotein, proton, pyrazine derivative, unclassified drug, absorption spectroscopy, air, article, bioluminescence, biotransformation, kinetics, pH, priority journal, proton transport, Animals, Calcium, Histidine, Hydrozoa, Imidazoles, Luminescence, Luminescent Proteins, Models, Molecular, Oxygen, Protein Binding, Protons, Pyrazines, Spectrophotometry

Аннотация: 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-obelincoelenteПоказать полностьюrazine 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.

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Издание

Журнал: CHEMBIOCHEM

Выпуск журнала: Vol. 14, Is. 6

Номера страниц: 739-745

ISSN журнала: 14394227

Место издания: WEINHEIM

Издатель: WILEY-V C H VERLAG GMBH

Авторы

  • Eremeeva Elena V. (Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China; Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia; Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia; Siberian Fed Univ, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia)
  • Natashin Pavel V. (Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China; Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia; Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia; Siberian Fed Univ, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia)
  • Song Lei (Chinese Acad Sci, China Gen Microbiol Culture Collect Ctr, Inst Microbiol, Beijing 100101, Peoples R China)
  • Zhou Yuguang (Chinese Acad Sci, China Gen Microbiol Culture Collect Ctr, Inst Microbiol, Beijing 100101, Peoples R China)
  • van Berkel Willem J. H. (Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands)
  • Liu Zhi-Jie (Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China; Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China)
  • Vysotski Eugene S. (Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia; Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia; Siberian Fed Univ, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia)

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