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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ohmiya Y,Ohashi M,Tsuji FIdoi
10.1016/0014-5793(92)81247-jkeywords:
subject
Has Abstractpub_date
1992-04-20 00:00:00pages
197-201issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(92)81247-Jjournal_volume
301pub_type
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