Mercury Toxicity, Enzymes and Sulfur Bonds

Enzymes are proteins, and like all proteins they consist of chains of amino acids.  These chains have to be faulted in a specific way to give the enzyme its activity. In many enzymes, the structure of the enzyme is ensured by cross-bonding of the amino-acid chains. These cross-bonds consist of double sulfur bonds. Sulfur-bridges are covalent S-S bonds between two cysteine amino acids, which tend to be quite strong. These sulfur bonds are damaged when poisonous substances that are not naturally present have been added to the local environment.

Mercury binds to the -SH (sulfhydryl) groups, resulting in inactivation of sulfur and blocking of enzyme functions while producing sulfur metabolites with high toxicity that the body has difficulty dealing with. Sulfur is essential in enzymes, hormones, nerve tissue, and red blood cells. These sulfur bonds are crucial to human biology.


Insulin Chains

Thiol poisons, especially mercury and its compounds, reacting with
SH groups of proteins lead to the lowered activity of various enzymes
containing sulfhydryl groups. This produces a series of disruptions in
the functional activity of many organs and tissues of the organism.
I.M. Trakhtenberg[1]


Mercury, in its various forms, has a great attraction to the sulfhydryls or thiols. A thiol is any organic compound containing a univalent radical called a sulfhydryl and identified by the symbol -SH (sulfur-hydrogen).

Various molecules or atoms will affect the rate of an enzyme catalyzed reaction by binding to the enzyme. Some bind at the same site as the substrate (the active site) and prevent the substrate from binding. Others bind at sites on the enzyme remote from the active site and affect activity by modifying the shape of the enzyme. Many of these molecules reduce the activity of the enzyme and are referred to as inhibitors.

Mercury is the most potent enzyme inhibitor that exists; it is in a class of its own and well deserves its title as the most toxic non-radioactive element. It is because mercury and lead attach themselves at these highly vulnerable junctures of proteins that they find their great capacity to provoke biochemical shifts and then morphological changes in the body.

Transsulfuration pathways in the body are fundamental for life. When mercury blocks thiol groups cellular proteins lose their reactive properties, lose their ability to carry out their routine function. Because glycemic regulation is one of the body’s most central homeostatic mechanisms, mercury’s attack is most problematic, even at low concentrations, and indicates that it is playing a great role in the dramatic rise in diabetes.

The general model of insulin activity indicates that one insulin molecule engages the cystein-rich domain of the receptor, touching down on both sides of protein chain that are separated by the disulfide bond. If the geometry of the receptor has been changed by mercury the message that insulin has arrived to give the cell is not received. Mercury is an inhibitor capable of interfering with PTK catalytic activity exactly because it is collapsing/damaging these sulfur-containing cross-linkages which changes the geometry of both insulin receptor and insulin itself.

Adult onset (type 2) diabetes develops when glucose homeostatic regulation breaks down. Most type-2 diabetics produce enough insulin but have developed resistance to normal insulin action in target tissues and now we have an explanation why. When we look at the fact that peripheral cells each have approximately 3,500 receptor sites, (other cells have less) that there are 70 trillion cells in the body; and thousands of trillions of atoms an average person with a mouth full a amalgam might ingest each day, we can see why diabetes tends under most conditions, even with mercury directly assaulting these sulfur bonds, to be a slow onset disease and that’s why the prevalence increases with age.

When the available sites on the cells drop into the 1,200 to 1,500 ranges the cell and entire insulin hormone system run into serious trouble. When it comes to children and early onset diabetes thimerosal is one likely villain. Thimerosal is ethyl-mercury mixed with aluminum in the vaccine and if anyone ever wanted to discover the ultimate elixir of death, they probably found it. Injecting millions of children with 150,000 trillion atoms of supercharged death particles (50 micrograms in two thimerosal containing vaccines before this preservative was removing from most vaccines in 1999) was surely the ultimate treason against a generation of children.

Vaccines are the largest cause of
insulin dependent diabetes in children.
Dr. J. Barthelow Classen

Dr. J. Barthelow Classen, in the Journal of Pediatric Endocrinology and Metabolism (2003), published research into the links between vaccine and insulin-dependent diabetes. Classen's research indicates that vaccinations can cause autoimmune diseases and he cites research from New Zealand indicating that the incidence of diabetes there has increased by 50 percent since 1988 when hepatitis B was given to New Zealand children under 16.

He also cited a rapid rise in the incidence of childhood diabetes since the introduction of the HiB vaccine--50 cases of diabetes per 100,000 vaccinated children. According to Classen vaccines in general can cause interferon release, which can in turn induce human diabetes. “Our results conclusively prove there is a causal relationship between immunization schedules and diabetes,” states Dr. Classen. The Hep B vaccine was notorious for its heavy concentration of mercury. Though thimerosal (fifty percent mercury by weight) has been taken out of Hep B vaccines in the United States that is not the case in the third world.

Mercury interacts with sulfhydryl groups and disulfide bonds,
as a result of which specific membrane transport is blocked
and selective permeability of the membrane is altered.

Thus insulin's ability to lower blood sugar is compromised. Mercury is causing chronic hyperinsulinemia because insulin resistance causes serum hyperglycemia and intra-cellular hypoglycemia (since glucose cannot get into cells) and the cells perceive this state as starvation.[2] As a consequence, blood glucose levels become so elevated that the glucose "spills over" into the urine, and is converted into triglycerides (fat), which contribute to cardiovascular illness. Despite these high blood glucose levels, cells "starve" since insulin-stimulated glucose entry into cells is impaired, which leads to an acid condition ketosis. To compensate the body releases glugcagon, cortisol, and catecholamines which further raise blood sugar levels. More insulin is pumped out resulting in hyperinsulinemia and this creates a cascading biological disaster of triglyceride and cholesterol excess, hypertension, inflammatory cytokine release and further endocrine dysfunction.[3] [4]

Peripheral neuropathy is a common condition that can cause
numbness and tingling. It can be caused by diabetes or
overexposure to toxic chemicals, such as mercury or lead.

Park Nicollet Institute

It is through mercury’s attack on these sulfide bonds that mercury is able to change the biological properties of proteins and change important physiological functions. Full recognition of the poisonous strength of mercury comes through a focused study of the series of physiological processes that are affected when SH groups are disturbed.

Mercury is acting in the place of first cause creating the high levels of glucose through its interference in insulin and insulin receptor sites. All these glycated proteins are creating 50 times the amount of free radicals than non-glycated proteins.

Though mercury has other toxic routes creating havoc in cardiovascular tissues and even in nuclear cell processes, advanced glycosylation will normally accelerate mitochondrial damage, encourage expression of defective cancer genes, and cause protein damage underlying skin aging and wrinkling as well as providing for stiffer joints.



[2] Metabolic Dysglycemia Profile. Laboratory Assessments.

[3] Feener EP, Kin GL. Vascular dysfunction in dia-betes mellitus. Lancet 1997(suppl):9-13.

[4] Lempiainen P, Meykkanen L, Pyorala K, Laakso M, Kuusisto J. Insulin resistance syndrome predicts coronary heart disease events in elderly nondiabetic men. Circulation 1999;100:123- 128.