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

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

Biophysics of the Genome

ISBN

80-210-3226-X

ISSN

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e-ISSN

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Počet stran výsledku

8

Strana od-do

74-81

Název nakladatele

Masaryk University

Místo vydání

Brno

Místo konání akce

Hlohovec, Czech Republic

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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