The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding

被引：32

作者：

Eremeeva, Elena V. ^{[1
,2
]}

Markova, Svetlana V. ^{[1
]}

Westphal, Adrie H. ^{[2
]}

Visser, Antonie J. W. G. ^{[2
]}

van Berkel, Willem J. H. ^{[2
]}

Vysotski, Eugene S. ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia

[2] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands

来源：

FEBS LETTERS | 2009年 / 583卷 / 12期

关键词：

Bioluminescence; Photoprotein; Trp fluorescence; CRYSTAL-STRUCTURE; CA2+-REGULATED PHOTOPROTEINS; VIOLET BIOLUMINESCENCE; ANGSTROM RESOLUTION; RECOMBINANT OBELIN; W92F OBELIN; CALCIUM; REGENERATION; APOAEQUORIN; EXPRESSION;

D O I：

10.1016/j.febslet.2009.04.043

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 intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1939 / 1944

页数：6

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