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Uncoupling Protein—A Useful Energy Dissepator

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Abstract

The structure/function relationship in the uncoupling proteins (UCP) is reviewed, stressingUCP from brown adipose tissue (UCP1) since, so far, nearly no biochemistry is known forthe UCP variants UCP2, UCP3, and UCP4. The transport for H+ and Cl− and its dependenceon fatty acids in reconstituted vesicles is described. The inhibition and binding of nucleotidesto UCP1, in particular, the pH dependence and two-stage binding are analyzed. A model forthe role of fatty acid in H+ transport is shown. The role of specific residues in UCP1 isanalyzed by directed mutagenesis in a yeast expression system. The different regulation bythe cellular energy potential of UCP1 versus UCP3 is discussed.

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  1. Institute of Physical Biochemistry, University of Munich, Schillerstrasse 44, 80336, Munich, Germany

    Martin Klingenberg

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Klingenberg, M. Uncoupling Protein—A Useful Energy Dissepator. J Bioenerg Biomembr 31, 419–430 (1999). https://doi.org/10.1023/A:1005440221914

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