Two excited states in aequorin bioluminescence induced by tryptophan modification

FEBS Letters

Ohashi, Mamoru¹  Tsuji, Frederick I.²  Ohmiya, Yoshihiro² 

[1] Department of Applied Physics and Chemistry, University of Electro-Communications, Chofu, Tokyo 182, Japan;Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565, Japan

关键词: Photoprotein;    Ca2+-binding protein;    Coelenterazine;    Coelenteramide;    Emission spectrum;    Excited state;   

DOI  :  10.1016/0014-5793(92)81247-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Ca²⁺-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.

【 授权许可】

Unknown