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Sulfhydryl groups are involved in H+ translocation via the uncoupling protein of brown adipose tissue mitochondria

Jezek, P.

Febs Letters 211(1): 89-93

1987


ISSN/ISBN: 0014-5793
PMID: 3026844
DOI: 10.1016/0014-5793(87)81280-2
Accession: 041487027

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Mersalyl inhibits H+ transport via the uncoupling protein (UP) in brown adipose tissue (BAT) mitochondria estimated as swelling in potassium acetate (Ki 67 microM) or as valinomycin-induced H+ extrusion in K2SO4 (Ki 55 microM) and KCl. The swelling in KCl is depressed only slightly. Some other SH-reagents (p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzoate) and thiolyte DB), but not hydrophobic reagents (N-ethylmaleimide and eosin-5-maleimide), exhibit analogous inhibition. Thus an essential SH-group localized at the water-accessible cytosolic surface of UP was found to be involved in H+ transport via UP but not in Cl- transport.

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