A structure-activity study of fatty acid interaction with mitochondrial uncoupling protein

被引：66

作者：

Jezek, P ^{[1
]}

Modriansky, M ^{[1
]}

Garlid, KD ^{[1
]}

机构：

[1] OREGON GRAD INST,DEPT CHEM BIOCHEM & MOL BIOL,PORTLAND 97291,DORSET,ENGLAND

来源：

FEBS LETTERS | 1997年 / 408卷 / 02期

关键词：

reconstitution; uncoupling protein; H+ transport; fatty acid uniport; chloride uniport; fatty acid flip-flap;

D O I：

10.1016/S0014-5793(97)00335-9

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：

Fatty acid (FA) uniport via mitochondrial uncoupling protein (UcP) was detected fluorometrically with PBFI, potassium-binding benzofuran phthalate and SPQ, 6-methoxy-N-(3-sulfopropyl)-quinolinium, indicating K+ and H+, respectively, The FA structural patterns required for FA flip-flop, UcP-mediated FA uniport, activation of UcP-mediated H+ transport in proteoliposomes, and inhibition of UcP-mediated Cl- uniport by FA, were identical. Positive responses were found exclusively with FA which were able to flip-flop in a protonated form across the membrane and no responses were found with 'inactive' FA lacking the flip-flop ability. The findings support the existence of FA cycling mechanism. (C) 1997 Federation of European Biochemical Societies.

引用

页码：166 / 170

页数：5

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