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Ion permeability induced in artificial membranes by the ATP/ADP antiporter
Author(s) -
Tikhonova I.M.,
Andreyev A.Yu.,
Antonenko Yu.N.,
Kaulen A.D.,
Komrakov A.Yu.,
Skulachev V.P.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80197-5
Subject(s) - antiporter , membrane , biophysics , chemistry , permeability (electromagnetism) , ion , biochemistry , biology , organic chemistry
The hypothesis on the additional function of the ATP/ADP antiporter (ANT) as uncoupling protein has been tested in proteoliposomes and planar bilayer phospholipid membranes (BLM). It is found that dissipation of the light‐induced ΔpH in the dark is very much faster in ANT‐bacteriorhodopsin proteoliposomes than in proteoliposomes containing baeteriorhodopsin as the only protein. Mersalyl treatment of ANT‐bacteriorhodopsin proteoliposomes causes further increase in the ΔpH dissipation rate due to formation of a high conductance pore. The properties of this pore are studied on ANT incorporated to BLM. They proved to be similar to those of so‐called multiple conductance channel or permeability transition pore of inner mitochondrial membrane. The conductance of the single channel is as high as 2.2 nS. The channel fails to discriminate between K + , Na + , H + and Cl − . Thus the obtained data are consistent with the assumption that native and modified ANT might function as an H + ‐specific conductor and as a permeability transition pore, respectively.