THE MAJOR THIOBACILLUS-FERROOXIDANS OUTER-MEMBRANE PROTEIN FORMS LOW CONDUCTANCE ION CHANNELS IN PLANAR LIPID BILAYERS
THE MAJOR THIOBACILLUS-FERROOXIDANS OUTER-MEMBRANE PROTEIN FORMS LOW CONDUCTANCE ION CHANNELS IN PLANAR LIPID BILAYERS
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DOI：
10.1016/0014-5793(92)80372-n
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发表时间：
1992-01-20
期刊：
影响因子：
3.5
通讯作者：
WOLFF, D
中科院分区：
文献类型：
--
作者：
SILVA, M;FERREIRA, A;WOLFF, D
从嗜酸的，chemolithotrophic细菌，氧化亚铁硫杆菌的外膜分离和纯化的蛋白质，寡聚体分子量为90 000 Da（p90）被纳入磷脂酰乙醇胺平面脂质双层。该蛋白在KCl溶液中形成轻微的阴离子通道，在100 mM KCl中电导为25 pS。电流-电压关系在+/-60 mV之间呈线性，电导是盐浓度的饱和函数。这些通道在低电位下从单一开放状态波动到闭合状态，但在较高电位下呈现闪烁活性。
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 (p90) 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 +/-60 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.