Two excited states in aequorin bioluminescence induced by tryptophan modification

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...

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Bibliographic Details
Published in:FEBS letters 1992-04, Vol.301 (2), p.197-201
Main Authors: Ohmiya, Yoshihiro, Ohashi, Mamoru, Tsuji, Frederick I.
Format: Article
Language:English
Subjects:
Aequorea victoria
aequorin
Aequorin - chemistry
Aequorin - genetics
Analytical, structural and metabolic biochemistry
Biological and medical sciences
bioluminescence
Ca 2+-binding protein
Ca2+-binding protein
calcium
Circular Dichroism
Cloning, Molecular
Coelenteramide
Coelenterata
Coelenterazine
Emission spectrum
Escherichia coli - genetics
Excited state
Fundamental and applied biological sciences. Psychology
Luminescence
Marine
Molecular Structure
Non metallic chromoproteins, photoproteins
Photoprotein
Proteins
Spectrum Analysis
Tryptophan - chemistry
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81247-J