By Gould R.F. (ed.)
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J. Biolumin. Chemilumin. 1990, 5, 25–30. , Shimomura, O. Structure of the functional part of photoprotein aequorin. Chem. Commun. 1986, 1566–1568. Nicolas, M. , Bassot, J. , Shimomura, O. Polynoidin: a membrane photoprotein isolated from the bioluminescent system of scale-worms. Photochem. Photobiol. 1982, 35, 201–207. , McCann, R. , Cormier, M. J. Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein. Biochem. Biophys. Res. Commun. 1985, 126, 1259–1268.
Johnson, F. H. Peroxidized coelenterazine, the active group in the photoprotein aequorin. Proc. Natl. Acad. Sci. USA 1978, 75, 2611–2615. , Johnson, F. H. Chemistry of the calcium-sensitive photoprotein aequorin. In Detection and Measurement of Free Calcium Ions in Cells (Ashley, C. , Campbell, A. ), pp. 73–83. Elsevier/North-Holland: Amsterdam, 1979a. , Johnson, F. H. Comparison of the amounts of key components in the bioluminescence system of various coelenterates. Comp. Biochem. Physiol. 1979b, 64B, 105–107.
3. The group R3 must be an OH group, and no substitution is allowed on the phenyl group bearing this OH. 2 Selected semi-synthetic aequorins derived from recombinant aequorin (Shimomura et al. 1993). No. 07 N N H N F O 1 R (-C6H4OH-p) 5 28 R5 1 N N H N R (-C6H4OH-p) R2 3 R (-C6H5) (-OH) a) Only the changes from the coelenterazine structure are shown in this column. Those unchanged are shown in parentheses in the above structures. b) The ratio in luminescence capacity: semi-synthetic aequorin/unmodiﬁed aequorin.