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- W2108075188 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." @default.
- W2108075188 created "2016-06-24" @default.
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- W2108075188 date "2013-03-12" @default.
- W2108075188 modified "2023-09-27" @default.
- W2108075188 title "Oxygen Activation of Apo-obelin-Coelenterazine Complex" @default.
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- W2108075188 doi "https://doi.org/10.1002/cbic.201300002" @default.
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