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A structure–activity study of fatty acid interaction with mitochondrial uncoupling protein
Author(s) -
Ježek Petr,
Modrianský Martin,
Garlid Keith D
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00335-9
Subject(s) - chemistry , uncoupling protein , fatty acid , protonation , biophysics , biochemistry , stereochemistry , biology , ion , organic chemistry , adipose tissue , brown adipose tissue
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.