Quenching of tryptophan fluorescence of firefly luciferase by substrates

被引：9
|
作者：
Cherednikova, EY [1 ]
Chikishev, AY
Dementieva, EI
Kossobokova, OV
Ugarova, NN
机构：
[1] Moscow MV Lomonosov State Univ, Dept Phys, Moscow 119899, Russia
[2] Moscow MV Lomonosov State Univ, Ctr Int Laser, Moscow 119899, Russia
[3] Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119899, Russia
来源：
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY | 2001年 / 60卷 / 01期
关键词：
firefly luciferase; fluorescence; luciferin; ATP;
D O I：
10.1016/S1011-1344(00)00135-4
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 interaction of firefly luciferase with substrates (luciferin and MgATP) by steady-state and time-resolved fluorescence is studied. The efficient quenching of tryptophan fluorescence of the active enzyme takes place upon its binding with substrates. In the presence of ATP the quenching is of dynamic type and is caused by structural changes in the protein molec;le upon ATP binding. A model is proposed in which the complex has smaller fluorescence quantum yield than the free enzyme because of partial quenching of tryptophan fluorescence by the new microenvironment. Quenching of tryptophan fluorescence by luciferin due to the efficient energy transfer from tryptophan to luciferin is discussed. The calculated distance between Trp-419 and luciferin for the L. mingrelica luciferase in the enzyme-substrate complex is less than 12 Angstrom. (C) 2001 Elsevier Science B.V. All rights reserved.
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页码：7 / 11
页数：5
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