dc.creatorMora Silva, Macarena
dc.creatorFerreira, Arianna
dc.creatorRodriguez, Manuel
dc.creatorWolff, Daniel
dc.date.accessioned2018-12-20T15:09:17Z
dc.date.available2018-12-20T15:09:17Z
dc.date.created2018-12-20T15:09:17Z
dc.date.issued1992
dc.identifierFEBS Letters, Volumen 296, Issue 2, 2018, Pages 169-173
dc.identifier00145793
dc.identifier10.1016/0014-5793(92)80372-N
dc.identifierhttps://repositorio.uchile.cl/handle/2250/158002
dc.description.abstractA 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. © 1992.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceFEBS Letters
dc.subjectAutotrophic bacteria
dc.subjectIon channel
dc.subjectLipid bilayer
dc.subjectPorin
dc.subjectThiobacillus ferrooxidans
dc.titleThe major Thiobacillus ferrooxidans outer membrane protein forms low conductance ion channels in planar lipid bilayers
dc.typeArtículo de revista


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