2 EXCITED-STATES IN AEQUORIN BIOLUMINESCENCE INDUCED BY TRYPTOPHAN MODIFICATION

被引:79
作者
OHMIYA, Y
OHASHI, M
TSUJI, FI
机构
[1] OSAKA BIOSCI INST,6-2-4 FURUEDAI,SUITA,OSAKA 565,JAPAN
[2] UNIV ELECTROCOMMUN,DEPT APPL PHYS & CHEM,CHOFU,TOKYO 182,JAPAN
[3] UNIV CALIF SAN DIEGO,SCRIPPS INST OCEANOG,DIV MARINE BIOL RES,LA JOLLA,CA 92093
关键词
PHOTOPROTEIN; CA2+-BINDING PROTEIN; COELENTERAZINE; COELENTERAMIDE; EMISSION SPECTRUM; EXCITED STATE;
D O I
10.1016/0014-5793(92)81247-J
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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.
引用
收藏
页码:197 / 201
页数:5
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