Uncoupling protein, H+ transport and regulation
2001 ◽
Vol 29
(6)
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pp. 806-811
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Keyword(s):
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.
1990 ◽
Vol 172
(6)
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pp. 3208-3213
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2009 ◽
Vol 3
(2)
◽
pp. 180-188
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1988 ◽
Vol 16
(1)
◽
pp. 48-49
◽
2019 ◽
Vol 24
(4)
◽
pp. 777-792
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Keyword(s):
2008 ◽
Vol 78
(6)
◽
pp. 973-981
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Keyword(s):