Abstract
The uncoupling protein (UCP) is the key factor in the thermogenesis of brown adipose tissue. UCP recycles the H+ generated by the oxidation of fatty acids in the respiratory chain through the inner mitochondrial membrane and generates neutralization heat. Thus, a large proportion of the oxidative energy is funneled into heat instead of ATP. By transporting H+ or OH-, UCP is functionally the most simple carrier known in the biological kingdom. Surprisingly, the primary structure of UCP is similar to that of the ADP/ATP carrier and the other members of the mitochondrial carrier family (Aquila et al., 1985). Since UCP occurs only in mammalians it can be regarded to be the latest member in the evolution of this protein family (Klingenberg, 1990).
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References
Akeson M, Deamer DW (1991) Proton conductance by the gramicidin water wire. Biophys J 60: 101–109
Andreyev AY, Bondareva TO, Dedukhova V, Mokhova EN, Skulachev VP, Tsofina LM, Volkov NI, Vygodina TV (1989) The ATP/ADP-antiporter is involved in the uncoupling effect of fatty acids on mitochondria. Eur J Biochem 182: 585–592
Aquila H, Link TA, Klingenberg M (1985) The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane. EMBO J 4: 2369–2376
Butt HJ, Fendler K, Bamberg E, Tittor J, Oesterhelt D (1989) Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J 8: 1657–1663
Cao Y, Várò G, Chang M, Baofu N, Needleman R, Lanyi JK (1991) Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin schiff base. Biochemistry 30: 10972–10979
Heaton GM, Wagenvoord, RJ, Kemp A, Nicholls DG (1978) Brown-adipose-tissue mitochondria: Photoaffinity labelling of the regulatory site of energy dissipation. Eur J Biochem 82: 515–521
Klingenberg M (1988) Nucleotide binding to uncoupling protein. Mechanism of control by protonation. Biochemistry 27: 781–791
Klingenberg M (1990) Mechanism and evolution of the uncoupling protein of brown adipose tissue. TIBS 15: 108–112
Läuger P (1976) Diffusion-limited ion flow through pores. Biochim Biophys Acta 455: 493–509
Locke RM, Rial E, Scott ID, Nicholls DG (1982) Fatty acids as acute regulators of the proton conductance of hamster brown-fat mitochondria. Eur J Biochem 129: 373–380
Nicholls DG (1974) Hamster brown-adipose-tissue mitochondria. Eur J Biochem 49: 585–593
Ptak M, Egret-Charlier M, Sanson A, Bouloussa O (1980) A NMR study of the iomzation of fatty acids, fatty amines and n-acylamino acids incorporated in phosphatidylcholine vesicles. Biochim Biophys Acta 600: 387–397
Rial E, Poustie A, Nicholls DG (1983) Brown-adipose-tissue mitochondria: the regulation of the 32000-Mr uncoupling protein by fatty acids and purine nucleotides. Eur J Biochem 137: 197–203
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© 1994 Springer-Verlag Berlin Heidelberg
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Klingenberg, M., Winkler, E. (1994). Structure-Function Relationship in the Uncoupling Protein of Brown Adipose Tissue. In: Forte, M., Colombini, M. (eds) Molecular Biology of Mitochondrial Transport Systems. NATO ASI Series, vol 83. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78936-6_2
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DOI: https://doi.org/10.1007/978-3-642-78936-6_2
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