Proton translocation associated with anaerobic transhydrogenation from glycerol 3-phosphate to fumarate in Escherichia coli. |
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Authors: | K Miki T H Wilson |
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Institution: | 1. Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Mass. 02115 USA;2. Department of Physiology, Harvard Medical School Boston, Mass. 02115 USA |
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Abstract: | An strain, that lacks aerobic glycerol 3-phosphate (G3P) dehydrogenase and succinate dehydrogenase, was grown anaerobically on glycerol and fumarate. The addition of fumarate to such cells resulted in the formation of dihydroxyacetone phosphate (DHAP) suggesting that G3P is oxidized to DHAP while fumarate is reduced to succinate. Associated with the transhydrogenation was an extrusion of protons from the cell into the incubation medium. The stoichiometry of protons extruded to DHAP formed was near 2. Everted membrane vesicles take up protons in the presence of added G3P and fumarate. |
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