Oxygen is closely related to sulfur and selenium. Oxygen, sulfur and selenium share chemical properties and reactivity, and each one follows the previous one in a single column of the periodic table. Oxygen is the fire of life itself and loves to grab electrons from other molecules. This causes oxidation, which creates oxidative stress that must be quenched to avoid tissue damage.
Sulfur, right under oxygen, is a little bit bigger in atomic size, and so its outer electrons are less tightly bound. Selenium is bigger still, and it holds electrons even less tightly than sulphur. This means that selenium is best at passing electrons and sulphur is second best, while oxygen holds on the strongest. Sulfur and selenium can help metabolism when oxygen levels are low.
Any form of stress reduces oxygen dissolved in blood plasma. Stress comes in many forms - anxiety, dehydration, toxins, physical trauma, infection, and so on. Stress decreases the amount of oxygen dissolved in your body fluids, and decreases the amount of oxygen that reaches cells. Stress causes cellular suffocation.
Many factors interfere with blood-to-tissue oxygen delivery: tissue pH, vascular inflammation, cellular malnutrition and more.
The ability of sulfur/selenium thiol compounds, specifically magnesium thiosulfate and sodium thiosulfate, to enable the body to overcome hypoxic acidosis, explains many therapeutic effects of sulfur and selenium. Thiol compounds carry oxygen analogs as sulfur or selenium, which are small enough to enter sick tissue and help restore normal oxygen metabolism. They seemingly help anaerobic tissue compensate for hypoxia by fueling aerobic metabolism.
From the very moment of conception, life can be sparked by the unique redox environment created when a sperm fertilizes an egg. The sperm is extremely rich in proteins containing the mineral selenium, which is a potent reducing agent for glutathione, the most important antioxidant molecule in cells. The egg, on the other hand, is very rich in glutathione. Bring these two potent antioxidant strategies together, and you create an exceptionally reduced cell that can initiate life and promote development using the power of redox. That reducing power provides a metabolic spark as new life begins its journey, allowing the rapidly dividing cells to safely maintain a high rate of oxidation.
The ultimate sulfur molecule is glutathione, and its function in life is to combat oxidative stress. In reduced form it is a reservoir for electrons and the most potent antioxidant we make. Selenium is an ideal carrier for electrons. It picks them up easily but just as easily gets rid of them.
We must have enough selenium from the diet to combat oxidative stress. Some soils are famous for being extremely selenium-deficient and resulted in higher rates of hypothyroidism, goiter, cretinism, miscarriages, and extreme fatigue. A selenium deficiency state can be evident as fatigue and impaired cognitive function, as well as thyroid dysfunction.
Mercury binds to a form of selenium called selenocysteine. It is the regular cysteine molecule, but the sulfur element has been replaced by selenium. The affinity of mercury for that molecule is 10 to the 45th power. Unfortunately, that is actually a million-fold higher affinity than for the glutathione that would normally bind to that molecule. Mercury can bind so tightly to selenoproteins that a normal diet is not going to meet the body’s demands.
Glutathione protects the cells from oxidative-stress-induced apoptosis and glutathione levels are magnesium dependent. Glutathione is a very important detoxifying agent, enabling the body to get rid of undesirable toxins and pollutants. It forms a soluble compound with the toxin that can then be excreted through the urine or the gut. The liver and kidneys contain high levels of glutathione as they have the greatest exposure to toxins. The lungs are also rich in glutathione partly for the same reason. Many cancer-producing chemicals, heavy metals, drug metabolites etc. are disposed of in this way.
Glutathione (glū'tə-thī'ōn') is a polypeptide, C10H17N3O6S, of glycine, cysteine, and glutamic acid. Glutathione synthetase requires γ-glutamyl cysteine, glycine, ATP, and magnesium ions to form glutathione. In magnesium deficiency, the ss y-glutamyltranspeptidase is lowered. There is a direct relationship between cellular magnesium, GSH/GSSG ratios, and tissue glucose metabolism.
The data shows that magnesium-deficient people use more oxygen during physical activity—their heart rates increased by about 10 beats per minute. “When the volunteers were low in magnesium, they needed more energy and more oxygen to do low-level activities than when they were in adequate-magnesium status,” says physiologist Henry C. Lukaski.
Magnesium enhances the binding of oxygen to haem proteins. There is probably some kind of magnesium pump where oxygen climbs aboard the red cells and magnesium jumps off only to have to jump right back on the red cells again. Red blood cells have a unique shape known as a biconcave disk, which is mission-critical for oxygen transport. Magnesium is important to red blood cell shape and function. The interaction of calcium, magnesium and ATP with membrane structural proteins exerts a significant role in the control of the shape of human red blood cells.
Abnormal magnesium-deprived red blood cells lack the flexibility that allows them to enter tiny capillaries. These nondiscocytes are characterized by a variety of irregularities, including surface bumps or ridges, a cup or basin shape, and altered margins instead of the round shape found in discocytes. When people become ill or physically stressed (more magnesium-deficient), a higher percentage of discocytes transform into the less flexible nondiscocytes.