Abstract
It has recently been reported that aluminum plays a very important role in reducing the activity of Krebs-cycle enzymes and glutamate dehydrogenase in rat brain homogenate. Therefore, it is necessary to identify the aluminum binding ability with the pivotal substrate α-ketoglutarate in biological systems. The interactions of aluminum with α-ketoglutarate were studied with pH-potentiometry, cyclic voltammetry, UV-vis, 1H, 27Al-NMR and Raman spectra multi-analytical techniques in acidic aqueous solution to measure the stoichiometries and stability constants of the complexes and its ketoenol tautomerism. The α-ketoglutarate was found to bind Al in a bidentate manner at the carboxylate and carbonyl moieties. The mononuclear 1:1 (AlLH-1, AlL+, AlHL2+) and 2:1 (AlL2-, AlL2H-23-) species, and dinuclear 2:1 (Al2L4+) species were found in acidic aqueous solution. Meanwhile, Al can promote α-KG tautomerize to its enolic-structure compounds in solutions. These findings may help to further understand the influence of Al on GDH enzyme reactions in biological systems.
