Masters of Health Magazine August 2020 | Page 14

Often the protons and electrons originate from an NAD molecule that the enzyme also binds to. eNOS, the enzyme that was discussed at length in the paper Greg Nigh and I published that caught László’s attention, is a flavoprotein that binds both FAD and NADP. It also binds heme, another molecule that biology makes great use of to help facilitate chemical reactions, and one that will be revisited later in this article. Heme is also of course the molecule that contains iron bound to oxygen to support oxygen transport by hemoglobin in red blood cells.

Many enzymes, and pretty much all flavoproteins, have a special skill to select hydrogen (H) over deuterium (D) when they perform their reaction. There is a term called a “deuterium kinetic isotope effect” (KIE) that captures the extent to which a given enzyme can favor hydrogen over deuterium.

They achieve this unique skill by invoking a cosmic physics principle called “proton tunneling.” Essentially, if things are set up just so, protons can cheat in a chemical reaction, avoiding an energy barrier by metaphorically “tunneling through” a hill.

Deuterons are much worse at proton tunneling than protons, and this is how these enzymes are able to select for protons over deuterons when they synthesize their product. Importantly, these specialized enzymes often move hydrogen from or to an NAD(P) molecule, causing either NAD(P)H to become NAD(P)+ or vice versa. What is important to realize is that the “H” in NAD(P)H is almost never D, because the enzyme’s reaction fails when D displaces H.

And what is also important to realize is that the mitochondria are very adept at grabbing the H from either NADH or NADPH and adding it to the water pool that’s collecting deuterium depleted water (DDW), and they often use flavoproteins to do this. DDW is being widely marketed on the Web as a therapeutic form of water, and it is often as expensive as a good bottle of wine.

Glyphosate and Flavoproteins

You may have realized from the above discussion that glyphosate can be predicted to deplete the supply of both NAD and FAD to exposed organisms, because it disrupts the synthesis of the precursors coming out of the shikimate pathway. This is clearly one way in which glyphosate might compromise the mitochondria’s ability to maintain DDW.

However, it is plausible that glyphosate disrupts deuterium depletion in a much more direct way -- by suppressing the activity of the enzymes involved in the proton tunneling reactions.

Flavoproteins have a signature motif at the site where they bind FAD, and this same motif shows up where enzymes, even enzymes that are not flavoproteins, bind NAD. This motif, a characteristic highly conserved feature of a so-called Rossmann fold topology, has the pattern “GxGxxG.”

Here, “G” stands for glycine and “x” stands for “wildcard” -- meaning that any amino acid, including glycine, could go there. So this motif has at least three glycine residues binding phosphate that could logically be substituted by glyphosate, disrupting the protein’s ability to bind either FAD or NAD(P). Mutations of the glycines in this motif cause the enzyme to lose enzyme activity [6].

Glyphosate has been shown experimentally to suppress several different enzymes that bind to either NAD, NADP or FAD, including succinate dehydrogenase [7], the class of cytochrome P450 enzymes in the liver [8], Cytochrome P450 reductase [9], NADH dehydrogenase [10] and glucose 6 phosphate dehydrogenase (G6PD) [11].