Mercury inhibits the L170C mutant of aquaporin Z by making waters clog the water channel.

We conduct in silico experiments of the L170C mutant of the Escherichia coli aquaporin Z (AQPZ) with and without mercury bonded to residue Cys 170. We find that bonding mercury to Cys 170 does not induce consequential structural changes to the protein. We further find that mercury does not stick in the middle of the water channel to simply occlude water permeation, but resides on the wall of the water pore. However, we observe that the water permeation coefficient of L170C-Hg(+) (with one mercury ion bonded to Cys 170) is approximately half of that of the mercury-free L170C. We examine the interactions between the mercury ion and the waters in its vicinity and find that five to six waters are strongly attracted by the mercury ion, occluding the space of the water channel. Therefore we conclude that mercury, at low concentration, inhibits AQPZ-L170C mutant by making water molecules clog the water channel.