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J. Biol. Chem., Vol. 269, Issue 42, 26184-26190, Oct, 1994
P Jezek, DE Orosz, M Modriansky and KD Garlid
The uncoupling protein generates heat by catalyzing electrophoretic proton
transport across the inner membrane of brown adipose tissue mitochondria.
It also transports Cl- and other monovalent anions, and both proton and
anion transport are inhibited by purine nucleotides. Several long-standing
hypotheses bear on specific aspects of Cl- transport, H+ transport, and
nucleotide gating mechanisms in uncoupling protein. We reevaluated these
hypotheses in mitochondria and liposomes reconstituted with purified
uncoupling protein; GDP inhibition is strictly noncompetitive with Cl- and
unaffected by either transmembrane electrical potential or fatty acids. The
Km and Vmax values for Cl- are independent of pH, arguing against a common
binding site for Cl- and OH- ions. Cl- transport was inhibited by fatty
acids and stimulated by fatty acid removal, refuting the consensus
hypothesis that there is no interaction between fatty acids and anion
transport through uncoupling protein. These results support a mechanism in
which the transport pathway for anions is identical with the fatty acid
binding site and distinct from the nucleotide binding site.
Transport of anions and protons by the mitochondrial uncoupling protein and its regulation by nucleotides and fatty acids. A new look at old hypotheses
Institute of Physiology, Czech Academy of Sciences, Prague.
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