Structural and functional characterization of uncoupling proteins: Alkylsulfonates as probes of UCP transport mechanism

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F03%3A00009012" target="_blank" >RIV/00216224:14330/03:00009012 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Structural and functional characterization of uncoupling proteins: Alkylsulfonates as probes of UCP transport mechanism
Original language description
The mechanism of fatty acid-dependent uncoupling by mitochondrial uncoupling proteins (UCP) is still in debate. We have hypothesized that the anionic fatty acid head group is translocated by UCP, and the proton is transported electroneutrally in the bilayer by flip-flop of the protonated fatty acid. Alkylsulfonates are useful as probes of the UCP transport mechanism. They are analogues of fatty acids, and they are transported by UCP1, UCP2 and UCP3. Alkylsulfonates cannot be protonated because of theirlow pKa; consequently, they cannot catalyze electroneutral proton transport in the bilayer and cannot support uncoupling by UCP. We report that propranolol forms permeant ion pairs with the alkylsulfonates, thereby removing this restriction. Because a proton is transported with the neutral ion pair, the sulfonate is able to deliver protons across the bilayer, behaving as if it were a fatty acid. When ion pair transport is combined with UCP1, we now observe electrophoretic proton transpor
Czech name
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Czech description
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Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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