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ACTION SPECTRUM AND QUANTUM YIELD FOR THE PHOTOINACTIVATION OF MNEMIOPSIN, A BIOLUMINESCENT PHOTOPROTEIN FROM THE CTENOPHORE MNEMIOPSIS SP. *
Author(s) -
Ward William W.,
Seliger Howard H.
Publication year - 1976
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1976.tb07260.x
Subject(s) - photoprotein , bioluminescence , luciferin , photochemistry , action spectrum , chemistry , biophysics , quantum yield , photobiology , biochemistry , biology , fluorescence , physics , luciferase , botany , optics , transfection , gene
— Ctenophores are bioluminescent marine invertebrates closely related to the coelenterates. The isolated bioluminescent systems of the ctenophores Mnemiopsis and Beroë and the hydrozoan jellyfish Aequorea are protein‐luciferin complexes (photoproteins) which flash upon the addition of Ca 2+ ions. The photoprotein mnemiopsin has an oxygen‐independent quantum yield for photoinactivation of bioluminescence as high as 0.5, placing it among the most light‐sensitive proteins known. We have measured the action spectrum for this photoinactivation at 107 narrow (3.4 nm) wavelength bands between 230 nm and 570 nm, covering a range of four decade units in the action. The action spectrum in the visible region is identical with the absorption spectrum of native photoprotein, implicating bound luciferin. The UV action spectrum implies that absorption by aromatic amino acid residues also leads to extremely efficient photoinactivation. Although photoinactivation is a rapid first‐order reaction, destruction of the luciferin is a slower, multiple‐order process. Therefore, protein‐bound luciferin is not the ultimate target of the photoinactivation. Absorption of light results in the dissociation of “active oxygen” from the photoprotein. Therefore, the ctenophore photoprotein is a precharged enzyme already containing bound luciferin and oxygen.