No facilitator required for membrane transport of hydrogen sulfide.

ABSTRACT: Hydrogen sulfide (H(2)S) has emerged as a new and important member in the group of gaseous signaling molecules. However, the molecular transport mechanism has not yet been identified. Because of structural similarities with H(2)O, it was hypothesized that aquaporins may facilitate H(2)S transport across cell membranes. We tested this hypothesis by reconstituting the archeal aquaporin AfAQP from sulfide reducing bacteria Archaeoglobus fulgidus into planar membranes and by monitoring the resulting facilitation of osmotic water flow and H(2)S flux. To measure H(2)O and H(2)S fluxes, respectively, sodium ion dilution and buffer acidification by proton release (H(2)S left arrow over right arrow H(+) + HS(-)) were recorded in the immediate membrane vicinity. Both sodium ion concentration and pH

SUBMITTER: Mathai JC 

PROVIDER: S-EPMC2757810 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature