On the Mechanism of Transport by the Uncoupling Protein from Brown Adipose Tissue Mitochondria
The uncoupling protein enables brown adipose tissue mitochondria to uncouple respiration from ATP synthesis under thermogenic conditions by catalyzing re-entry of protons extruded by the respiratory chain. Two ligands, purine nucleotides and fatty acids, interact specifically with the protein to modulate its transport activity (for review see Rial & Nicholls, 1987).
KeywordsPermeability Hydroxyl Catalysis Cysteine Respiration
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- Cannon B, Nicholls DG, Lindbere O (1973) Purine nucleotides and fatty acids in energy coupling in mitochondria from brown adipose tissue. In: Azzone GF, Ernster L, Papa S, Quagliariello E, Siliprandi N (eds) Mechanisms in Bioenergetics. Academic Press, New York, pp 357–363Google Scholar
- Nicholls DG, Heaton G (1978) Anion uniport across the inner membrane of brown adipose tissue mitochondria. In: Azzone GF, Avron M, Metcalfe JC, Quagliariello E, Siliprandi N (eds) The Proton and Calcium Pumps. Elsevier, Amsterdam, pp 309–318Google Scholar
- Rial E, Nicholls DG (1987) The uncoupling protein from brown adipose tissue mitochondria. Cell Biol Rev 11:75–104Google Scholar