Fast and selective ammonia transport by aquaporin-8

The transport of ammonia/ammonium is fundamental to nitrogen metabolism in all forms of life. So far, no clear picture has emerged as to whether a protein channel is capable of transporting exclusively neutral NH₃ while excluding H⁺ and NH₄⁺. Our research is the first stoichiometric study to show the selective transport of NH₃ by a membrane channel. The purified water channel protein aquaporin-8 was reconstituted into planar bilayers, and the exclusion of NH₄ ⁺ or H⁺ was established by ensuring a lack of current under voltage clamp conditions. The single channel water permeability coefficient of 1.2 × 10^-14 cm³/subunit/s was established by imposing an osmotic gradient across reconstituted planar bilayers, and resulting minute changes in ionic concentration close to the membrane surface were detected. It is more than 2-fold smaller than the single channel ammonia permeability (2.7 × 10^-14 cm ³/subunit/s) that was derived by establishing a transmembrane ammonium concentration gradient and measuring the resulting concentration increases adjacent to the membrane. This permeability ratio suggests that electrically silent ammonia transport may be the main function of AQP8.