Deuterons have a nasty effect when they get into the pump -- a bit like getting sugar into the gas tank. They cause a hiccough in the pump that releases dangerous reactive oxygen species (ROS), and they can cause the pump to break altogether. This results in “mitochondrial dysfunction,” a common feature of a broad range of metabolic, oncological and neurological diseases.
Niacin and riboflavin are critical players in the maintenance of low deuterium in the mitochondria.
There is a set of enzymes that convert niacin into nicotinamide adenine dinucleotide (NAD), and another set that convert riboflavin into flavin adenine dinucleotide (FAD). These two molecules (NAD and FAD) are essential for maintaining low deuterium in the mitochondria, and the science behind this is complex but fascinating.
Both NAD and FAD contain a double phosphate unit that hooks the two nucleotides together (see Figure 1). There are many enzymes that bind NAD or its phosphorylated form NADP, which has three phosphate anions. There is also a class of enzymes called flavoproteins that bind FAD, and use FAD as a holding station for protons and electrons being passed along to effect the chemical reaction that the enzyme specializes in.
Figure 1: Molecular structure of nicotinamide adenine dinucleotide (NAD). Nicotinamide and adenine are the nucleotides. Note the two phosphates circled in the middle.