Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes.
The open channel characteristics of the bacterial porin Omp32 from Comamonas acidovorans were investigated by means of conductance measurements in planar lipid bilayers of the Montal-Mueller type. Particularly at low salt conditions (< or = 30 mM KCl) Omp32 exhibited some unusual asymmetric and nonlinear functional properties. Current-voltage relationship measurements showed that conductance depends on the orientation of porin molecules and is a nonlinear function of the applied membrane potential. Conductance also depends on the salt concentration in a manner not common to porins and the salt concentration modulates the nonlinearity of conductance-voltage relationships. Omp32 is strongly anion-selective. The nonlinear and asymmetric conductance of the open channel is a new observation in porins.
Mathes
A
A
Max-Planck-Institut für Biochemie, Abteilung Molekulare Strukturbiologie, Martinsried, Germany.
Engelhardt
H
H
D055592:Biophysical Phenomena; D001703:Biophysics; D004553:Electric Conductivity; D016946:Gram-Negative Aerobic Rods and Cocci / Q000378:metabolism; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry; D008564:Membrane Potentials; D009994:Osmolar Concentration; D018272:Porins / Q000737:chemistry* / Q000378:metabolism*; D011189:Potassium Chloride
D007473:Ion Channels; D008051:Lipid Bilayers; D018272:Porins; D011189:Potassium Chloride