Aequorea, bioluminescent

Direct Metal Analyses. Calcium ion can be detected to a lower limit of 10 M hy Aequorea bioluminescence. Strontium interferes to a minor extent (270,271). 

Cutler, M. W., and Ward, W. W. (1993). Protein-protein interaction in Aequorea bioluminescence. Bio luminescence Symposium, Maui, Hawaii, Nov. 3-10, 1993. 

Finally I would like to pay my tributes to Dr. Frank Johnson who initiated the study of the Aequorea bioluminescence, and to Dr. Yoshimasa Hirata who introduced me to the chemistry of the Cypridina luminescence. 

CHEMIEXCITATION MECHANISM FOR CYPRIDINA (VARGULA) AND AEQUOREA BIOLUMINESCENCE... 

Chemiexcitation mechanism for Aequorea bioluminescence. The indolyl at C6 of Cypridina luciferin plays an essential role as an electron-donating group for the efficient chemiexcitation mechanism, the ICT TS - Si route in the CTIL mechanism.1,2 Because 4-oxidophenyl (CT-CsH.,) at C6 of coelenterazine phenolate anion is also a good electron-donating group, the above mechanism will be applicable to the Aequorea system. We have already clarified that the Si state of coelenteramide... 

The existence of coelenterazine in various nonluminous organisms suggests that some of the coelenterazine-dependent luminous organisms might obtain coelenterazine from their food, either as the sole source of this substance or as a supplement to the coelenterazine biosynthesized in the body. In the case of the hydrozoan Aequorea aequorea, it was reported that the medusa is unable to produce its own coelenterazine and is dependent on a dietary supply of this compound for its capability of bioluminescence (Haddock et al., 2001). The organisms that biosynthesize coelenterazine remain to be identified, but it seems to be a common opinion at present that at least copepods do make their own coelenterazine. According to Thomson etal. (1995), the shrimp Systellaspis debilis is capable of coelenterazine... 

Gorokhovatsky, A. Y., et al. (2004). Fusion of Aequorea victoria GFP and aequorin provides their Ca2+-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer. Biochem. Biophys. Res. Commun. 320 703-711. 

Kishi, Y., Tanino, H., and Goto, T. (1972). The structure confirmation of the light-emitting moiety of bioluminescent jellyfish Aequorea. Tetrahedron Lett. 27 2747-2748. 

Morise, H., Shimomura, O., Johnson, F. H., and Winant, J. (1974). Inter-molecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13 2656-2662. 

Shimomura O, Johnson FH, Saiga Y (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J Cell Comp Physiol 59 223-239... 

British scientists immobilized53 in a porous sol-gel glass aequorin - the bioluminescent protein found in the jellyfish Aequorea aequorea. The luminescence from this protein is specifically triggered by the presence of calcium ions. The intensity of the luminescence, measured at the peak... 

Kendall, J.M. and Badminton, M.N. (1998) Aequorea victoria bioluminescence moves into an exciting new era. Trends in Biotechnology 16, 216-224. 

Aequorin is a Ca -sensitive, bioluminescent protein complex that was originally isolated from the jellyfish Aequorea victoria [166]. The protein complex is assembled in the presence of molecular oxygen from the protein apoaequorin and its cofactor, the luminophore coelenterazine [167] (see Fig. 18). The binding of Ca ions induces a conformational change in the complex, resulting in the oxidation of coelenterazine and a subsequent emission of blue light in the wavelength... 

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