Uncoupling protein, H+ transport and regulation. (November 2001)

• Record Type: Journal Article
• Authors: Klingenberg, M.; Winkler, E.; Echtay, K.
• Is Part Of: Biochemical Society transactions. Volume 29:Number 6(2001)
• Page Start: 806
• Page End: 811
• Publication Date: 2001-11
• Subjects: coenzyme Q -- reconstitution -- yeast/Escherichia coli expression; UCP, uncoupling protein -- CoQ, coenzyme Q; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0290806
• Languages: English
• ISSNs: 0300-5127

Abstract

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.