Two excited states in aequorin bioluminescence induced by tryptophan modification.

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 Lett

journal_title

FEBS letters

authors

Ohmiya Y,Ohashi M,Tsuji FI

doi

10.1016/0014-5793(92)81247-j

keywords:

subject

Has Abstract

pub_date

1992-04-20 00:00:00

pages

197-201

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)81247-J

journal_volume

301

pub_type

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