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- W2025880082 abstract "The Ca(2+)-activated photoprotein, aequorin, contains six tryptophan residues and has a bioluminescence emission maximum at 465 nm. On converting the six tryptophan residues to phenylalanine, the mutant aequorins exhibited varied luminescence activities and spectra, but one mutant, with tryptophan-86 replaced by phenylalanine, gave a bimodal emission spectrum, with maxima at 455 nm and 400 nm. This result suggests that tryptophan-86 may be importantly involved in the generation of the product excited state during aequorin bioluminescence." @default.
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- W2025880082 date "1992-04-20" @default.
- W2025880082 modified "2023-10-07" @default.
- W2025880082 title "Two excited states in aequorin bioluminescence induced by tryptophan modification" @default.
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- W2025880082 doi "https://doi.org/10.1016/0014-5793(92)81247-j" @default.
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