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Biochem J. Jul 1, 1984; 221(1): 269–272.
PMCID: PMC1144030

Mechanism of photoinactivation and re-activation in the bioluminescence system of the ctenophore Mnemiopsis.


The bioluminescence of the ctenophore Mnemiopsis takes place when the photoprotein mnemiopsin in the photocytes reacts with Ca2+. The luminescence is inhibited in sunlight and this photoinhibition is reversible by keeping the live specimens in the dark. The extracts of mnemiopsin are similarly photoinhibited, but the photoinhibition cannot be reversed in the dark. We have found that photo-inhibited mnemiopsin can be re-activated in the dark by incubation with coelenterazine and O2 only in solutions having a pH very close to 9.0. The re-activation in vivo probably takes place in the same manner, using the coelenterazine that is supplied from its abundant storage form. Various lines of experimental evidence suggest that the photoinactivation of mnemiopsin results in the dissociation of coelenterazine and oxygen from the molecule of photoprotein; the dissociated form of the former molecule is an inactive form of coelenterazine, not free coelenterazine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Girsch SJ, Hastings JW. The properties of mnemiopsin, a bioluminescent and light sensitive protein purified by hollow fiber techniques. Mol Cell Biochem. 1978 Apr 11;19(2):113–124. [PubMed]
  • Shimomura O, Johnson FH. Peroxidized coelenterazine, the active group in the photoprotein aequorin. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2611–2615. [PMC free article] [PubMed]
  • Shimomura O, Johnson FH, Kohama Y. Reactions involved in bioluminescence systems of limpet (Latia neritoides) and luminous bacteria. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2086–2089. [PMC free article] [PubMed]
  • Shimomura O, Masugi T, Johnson FH, Haneda Y. Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris. Biochemistry. 1978 Mar 21;17(6):994–998. [PubMed]
  • Ward WW, Seliger HH. Extraction and purification of calcium-activated photoproteins from the ctenophores Mnemiopsis sp. and Beroë ovata. Biochemistry. 1974 Mar 26;13(7):1491–1499. [PubMed]
  • Ward WW, Seliger HH. Properties of mnemiopsin and berovin, calcium-activated photoproteins from the ctenophores Mnemiopsis sp. and Beroë ovata. Biochemistry. 1974 Mar 26;13(7):1500–1510. [PubMed]
  • Ward WW, Seliger HH. Action spectrum and quantum yield for the photoinactivation of mnemiopsin, a bioluminescent photoprotein from the Ctenophore mnemiopsis SP. Photochem Photobiol. 1976 May;23(5):351–363. [PubMed]

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