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The major Thiobacillus ferrooxidans outer membrane protein forms low conductance ion channels in planar lipid bilayers
Author(s) -
Silva Macarena,
Ferreira Arianna,
Rodriguez Manuel,
Wolff Daniel
Publication year - 1992
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(92)80372-n
Subject(s) - conductance , chemistry , lipid bilayer , bacterial outer membrane , membrane , ion , phosphatidylethanolamine , thiobacillus , crystallography , biophysics , thiobacillus ferrooxidans , biochemistry , phospholipid , sulfur , biology , organic chemistry , escherichia coli , phosphatidylcholine , mathematics , combinatorics , gene
A protein isolated and purified from the outer membrane of the acidophilic, chemolithotrophic bacterium, Thiobacillus ferrooxidans with an oligomeric molecular weight of 90 000 Da (p9O) was incorporated into phosphatidylethanolamine planar lipid bilayers. The protein formed slightly anionic channels in KCl solutions, with a conductance of 25 pS in 100 mM KCl. The current—voltage relationship was linear between ±6O mV, and the conductance was a saturating function of the salt concentration. These channels fluctuated from a single open to closed state at low potentials, but present flickering activity at higher potentials.