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Updated: Aug 17, 2026

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters
Published on: February 3, 2018
Uncoupling protein, H+ transport and regulation
M Klingenberg1, E Winkler, K Echtay
1Institute of Physical Biochemistry, University of Munich, Schillerstrasse 44, D-80336 Munich, Germany. klingenberg@pbm.med.uni-muenchen.de
Abstract:
The biochemical functions of uncoupling proteins (UCPs) are discussed with the view of UCP1 as a paradigm. In contrast with UCP1, the heterologous expression of UCP3 in yeast is found to result primarily in extra-mitochondrial deposits and thus is unsuitable for studying UCP3 function. On expression in Escherichia coli inclusion bodies, UCPs extracted and incorporated into vesicles showed no H(+) transport, only Cl(-) transport. Only after addition of coenzyme Q was fully nucleotide-sensitive high-H(+) transport reconstituted, with UCP1 as well as with UCP2 and UCP3. The newly discovered cofactor role of coenzyme Q in H(+) transport is proposed to imply co-operation with fatty acids for the injection of H(+) into the UCP channel.
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