Figure 3.

The catabolism of excess amino acids through transdeamination in the liver mitochondrial matrix releases α-ketoglutarate (αKG) and ${\mathbf{\text{NH}}}_4^{+}$ through the deamination of glutamate catalyzed by glutamate dehydrogenase (GDH). Some $\text{N}{\text{H}}_4^{+}$ would dissociate to NH₃ and H⁺ in the matrix which has a more alkaline pH than the inter-membranous space and the cytosol. The permeation of NH₃ through aquaporin channels (e.g., aquaporin 8, APQ8) or the phospholipid bilayer would disrupt the H⁺ gradient set up by the electron transport system (ETS) across the inner mitochondrial membrane and uncouple ETS from oxidative phosphorylation.