EPR SPECTROSCOPY OF 5-DOXYL-STEARIC ACID BOUND TO THE MITOCHONDRIAL UNCOUPLING PROTEIN REVEALS ITS COMPETITIVE DISPLACEMENT BY ALKYLSULFONATES IN THE CHANNEL AND ALLOSTERIC DISPLACEMENT BY ATP

被引：28

作者：

JEZEK, P ^{[1
]}

BAUER, M ^{[1
]}

TROMMER, WE ^{[1
]}

机构：

[1] UNIV KAISERSLAUTERN,FACHBEREICH CHEM,D-67663 KAISERSLAUTERN,GERMANY

来源：

FEBS LETTERS | 1995年 / 361卷 / 2-3期

关键词：

UNCOUPLING PROTEIN; ANION CHANNEL; ALKYLSULFONATE; FATTY ACID BINDING SITE; 5-DOXYL-STEARIC ACID;

D O I：

10.1016/0014-5793(95)00201-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：

Competition of fatty acids (FA) and alkylsulfonates with 5-DOXYL-stearic acid (5-SASL) binding to isolated mitochondrial uncoupling protein (UcP) is demonstrated using EPR spectroscopy. A distinct peak of the bound 5-SASL (h(+1I)) decreased with increasing concentration of competitors. Since alkylsulfonates are UcP substrates, it suggests that the FA binding site is located in the anion channel, Moreover, with increasing ATP the h(+1I) peak decreased and was smoothed with the 'micellar' peak into a single wider peak. A pH of 8.5 reversed this effect. It could reflect an allosteric release of 5-SASL from the ATP binding site which mimics the ATP gating mechanism.

引用

页码：303 / 307

页数：5

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