Interaction of inorganic mercury salts with model and red cell membranes: importance of lipid binding sites.

The effect of two mercury salts, HgCl2 and Hg(NO3)2, on the thermotropic properties of phosphatidylserine (PS) model membranes and sonicated rat red cell membranes was investigated by fluorescence polarization. Both Hg(II) salts abolished the phase transition and decreased the membrane fluidity by interacting with PS. Maximal effect was observed at a Hg/PS ratio of 2.5-5 for mercuric chloride and at 1.5 for the nitrate salt. For both mercury compounds, 10 mM NaCl protected model membranes from the effects of Hg(II). HgCl2 and Hg(NO3)2 also decreased the fluidity of rat red cell membranes. Maximal effect was observed for 0.4 mM HgCl2 and 0.6 mM Hg(NO3)2, with 0.0125 mg protein/ml. Addition of NaCl to the Hg(II)-red cell system decreased the Hg(II)-induced perturbation of the thermotropic properties. For both membrane systems, the effects observed with Hg(NO3)2 were greater than those with HgCl2, which can be accounted for by the absence of competition with chloride ions in samples containing Hg(NO3)2.[Cl-] governs the availability of Hg(II) by determining its chemical speciation: increasing [Cl-] generates HgCl3- and HgCl4(2-), which do not interact with lipid binding sites. These results indicate that besides protein thiol groups, Hg(II)-lipid binding sites play an important role in the interaction of Hg(II) with red cell membranes that is qualitatively different from Hg(II) binding to protein thiol groups.