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Poisoning the Mitochondria

Discussion in 'General ME/CFS Discussion' started by Radio, Jan 23, 2014.

  1. Radio


    Sulfites are a big issue. If you are experiencing CFS/FMS symptoms, you should be aware of how they work and how they can affect you.

    How Sulfites can Hurt You

    Sulfites can hurt you if your protective Sulfite Oxidase enzyme (a chemical that converts one chemical to another chemical) is low. Sulfite Oxidase converts sulfites to sulfates, which are not
    harmful. If your Sulfite Oxidase enzyme is down, the sulfites will swim around your blood and inhibit important enzymes such as Tyrosinase, polyphenoloxidase, and ascorbate oxidase. This can result in the impairment of the synthesis of Dopamine and the conversion of Dopamine to Noradrenaline, which can lead to neurological fatigue. Sulfites can inhibit 90% of lung ATP energy production, can impair liver cell ATP energy production, and can deplete glutathione (chemical that helps the liver filter the blood and helps protect cell enzymes from damage). Anything that reduces your production of ATP energy can cause fatigue, since low levels of energy are synonymous with fatigue.

    Things that can inhibit your protective Sulfite Oxidase enzyme
    Things that can impair the protective sulfite oxidase are as follows: heavy metal molecules such as lead and mercury, Sulfa-drugs (e.g. a class of drugs within the sulfa group that can impair pterin synthesis, such as asthmatic inhalants and many antibiotics), molybdenum deficiency, proto-IX-porphyria (enzyme that makes blood inhibited), inherited genetic damage encoding of the SO-enzyme, severe B12-vitamin deficiency, and arrays of So2/SO3-group containing drugs including DMPS (an Rx chelation drug).

    How to live safely
    In summary, if one wants to be safe, they should avoid things that inhibit the protective sulfite oxidase enzyme (e.g. Sulfa Drugs, heavy metals); and if this protective enzyme does go down, then avoid the Sulfites themselves.

    Signs of a Sulfite problem

    Below are several clues that one is sensitive to sulfites (which probably means the sulfite oxidase enzyme is down):

    1) One becomes tired after ingesting one of the foods, listed above, that contains sulfites. One can look at the food label to see if the product contains sulfites.
    2) One coughs after ingesting sulfites, due to the impairment of the lung ATP energy.
    3) One has asthma.
    4) One develops low blood glucose (sugar) after ingesting sulfites (since sulfites disrupt the regulation of blood sugar).
    5) One gets a headache after ingesting sulfites. (brain fog)
    6) One experiences itching and reddening of the skin after ingesting sulfites contained in foods, drinks or drugs.

    Foods That Sometimes Contain Sulfites
    Sulfites are a kind of food preservative. The following is a list of foods that sometimes contain sulfite preservatives: dried fruit, bottled lemon juice, bottled lime juice, red wine, molasses, sourcrout juice, grape juice (all colors), and yellow die #5 found in Doritos. Foods that sometimes contain sulfites in lesser amounts are mashed potatoes made from dry powder, pickles in a jar, shrimp, cookies, crackers, beet sugar, and pie dough. If a food contains more than 10ppm (parts per million) of sulfite, the FDA requires that the product label list the amount of sulfite. In some cases, Molybdenum, B12-vitamin, P5P-vitamin, B1-vitamin, and tetrahydrofolate supplementation has helped to boost the protective sulfite oxidase a bit. Also, if mercury or lead molecules have induced Protoporphoria (enzyme that makes blood inhibited), detoxifying those heavy metals can help as well. In some cases, the Protoporphoria is inherited, and this is considered incurable at this time. In any case, if the protective sulfite oxidase is down, one can make a great difference by avoiding sulfite containing foods.

    Thiosulfate + 2 glutathione [​IMG] sulfite + glutathione disulfide + sulfide

    Thus, the two substrates of this enzyme are thiosulfate and glutathione, whereas its 3 products are sulfite, glutathione disulfide, and sulfide.

    This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:thiol sulfurtransferase. Other names in common use include glutathione-dependent thiosulfate reductase, sulfane reductase, and sulfane sulfurtransferase. This enzyme participates in glutathione metabolism.

    Sulfite Strategy
    Sulfite oxidase
    Oxidative phosphorylation
    The G473D mutation impairs dimerization and catalysis in human sulfite oxidase
    Effect of sodium sulfite on mast cell degranulation and oxidant stress
    Thiosulfate-thiol sulfurtransferase—thiol_sulfurtransferase

    Molybdenum is known to function as a cofactor for four enzymes

    • Sulfite oxidase catalyzes the transformation of sulfite to sulfate, a reaction that is necessary for the metabolism of sulfur-containing amino acids (methionine and cysteine).
    • Xanthine oxidase catalyzes the breakdown of nucleotides (precursors to DNA and RNA) to form uric acid, which contributes to the plasma antioxidant capacity of the blood.
    • Aldehyde oxidase and xanthine oxidase catalyze hydroxylation reactions that involve a number of different molecules with similar chemical structures. Xanthine oxidase and aldehyde oxidase also play a role in the metabolism of drugs and toxins.
    • Mitochondrial amidoxime reducing component (mARC) was described only recently (4), and its precise function is under investigation. Initial studies showed that mARC forms a three-component enzyme system with cytochrome b5 and NADH cytochrome b5 reductase that catalyzes the detoxification of mutagenic N-hydroxylated bases.
    Molybdenum functions only in the form of the Moco in humans, any disturbance of Moco metabolism can disrupt the function of all molybdoenzymes. Current understanding of the essentiality of molybdenum in humans is based largely on the study of individuals with very rare inborn metabolic disorders caused by a deficiency in Moco. Moco is synthesized de novo by a multistep metabolic pathway involving four genes: MOCS1, MOCS2, MOCS3, and GPHN (see figure). To date, more than 60 mutations affecting mostly MOCS1 and MOCS2 have been identified.

    Successful Treatment of Molybdenum Cofactor Deficiency Type A
    Molybdenm Linus Pauling Institute

    Functional SUOX Deficiency?

    Dr. Amy Yasko, "Sulfate levels may be used as a way to assess sulfite processing. Sulfites are converted to sulfates by SUOX which uses B12 and molybdenum in the reaction. If sulfate levels are high it may indicate that sulfite levels were too high and you want to be sure that you have enough B12 and molybdenum support in place such that the levels of molybdenum and B12 are not depleted in the process of converting sulfites to sulfates. Also high sulfites (by default high sulfates) is an indication that you may have too much activity via the transulfuration pathway and so you do not yet have the methylation cycle in balance"

    "There are three enzymes in the body that need molybdenum: sulfite oxidase (SUOX), xanthine oxidase, and aldehyde oxidase. Xanthine oxidase helps to convert intermediates to uric acid. Milk that has been homogenized increases the level of xanthine oxidase in the milk. This may be a more subtle aspect of dairy free diets to limit excess xanthine oxidase in the system. Too much xanthine oxidase, like increased sulfite oxidase activity runs the risk of depleting molybdenum. Finally aldehyde oxidase is involved in addressing yeast (Candida) in the body. The net effect of homogenized milk + Candida + high levels of sulfites is to increase the activity through these three molybdenum containing enzymes and potentially deplete levels of important intermediates"

    "High levels of overall sulfur in the body can trigger the cortisol stress reaction. There are entire PPTs I have given on the topic of stress. Also high levels of sulfur groups in general can exacerbate other situations in the body with excess glutamate and throw off the epinephrine/norepineprhine ratio."

    "One of the consequences of sulfite toxicity is the depletion of B1 vitamin in the body, B1 is also known as thiamine. Casein is one of the ways to protect vitamin B1 from destruction by sulfites, Supplementation with benfotiamine can also be considered in order to help support healthy vitamin B1 levels especially when sulfite toxicity is a concern. Tungsten in the system may impair important sulfite oxidase enzyme function. Those with higher levels of tungsten in the system may have a greater issue with sulfites and may want to support with forms of B1. In addition sulfite oxidase also needs sufficient molybdenum and B12 in the system for optimal function. So those with higher tungsten levels may also want to consider molybdenum and B12 support."

    To summarize, in my opinion the issue with high sulfates is three fold, one it indicates high levels of sulfites and excess transulfuration activity, two it suggests that molybdenum and B12 may be depleted from the system and three that the cortisol reaction and imbalances in norep/epi may be a factor due to high total levels of sulfur containing groups.

    Thiamine has a half-life of 18 days and is quickly exhausted, particularly when metabolic demands exceed intake. Thiamine is involved in a variety of glucose metabolism-related and neurological functions. After modification in the body to a diphosphate form, thiamine is involved in a vast array of functions:

    • Carbohydrate metabolism
    • Production of the neurotransmitters glutamic acid and GABA, through the TCA cycle
    • Lipid metabolism, necessary for myelin production
    • Amino acid metabolism
    • Neuromodulation.

    Methionine / Methylation Chicken or the Egg
    No Sulfites Help for Food Allergy
    Foods high in sulfur (thiols)

    Methionine synthase
    catalyzes the final step in the regeneration of methionine from homocysteine. The overall reaction transforms 5-methyltetrahydrofolateinto tetrahydrofolate (THF) while transferring a methyl group to Hcy to form Met. Methionine synthase is the only mammalian enzyme that metabolizes N5-MeTHF to regenerate the active cofactor THF. In cobalamin-dependent forms of the enzyme, the reaction proceeds by two steps in a ping-pong reaction. The enzyme is initially primed into a reactive state by the transfer of a methyl group from N5-MeTHF to Co(I) in enzyme-bound cobalamin, forming methyl-cobalamin that now contains Me-Co(III) and activating the enzyme. Then, a Hcy that has coordinated to an enzyme-bound zinc to form a reactive thiolate reacts with the Me-Cob. The activated methyl group is transferred from Me-Cob to the Hcy thiolate, which regenerates Co(I) in cob, and Met is released from the enzyme. The cob-independent mechanism follows the same general pathway but with a direct reaction between the zinc thiolate and N5-MeTHF.

    The mechanism of the enzyme depends on the constant regeneration of Co(I) in cob, but this is not always guaranteed. Instead, every 1-2000 catalytic turnovers, the Co(I) may be oxidized into Co(II), which would permanently shut down catalytic activity. A separate protein, Methionine Synthase Reductase, catalyzes the regeneration of Co(II) and the restoration of enzymatic activity. Because this process inevitably shuts down all methionine synthase activity, defects or deficiencies in methionine synthase reductase have been implicated in some of the disease associations for methionine synthase deficiency.

    Cysteine and cystine
    As the functional group of the amino acid cysteine, the thiol group plays a very important role in biology. When the thiol groups of two cysteine residues (as in monomers or constituent units) are brought near each other in the course of protein folding, an oxidation reaction can generate a cystine unit with a disulfide bond (-S-S-). Disulfide bonds can contribute to a protein's tertiary structure if the cysteines are part of the same peptide chain, or contribute to the quaternary structure of multi-unit proteins by forming fairly strong covalent bonds between different peptide chains. A physical manifestation of cysteine-cystine equilibrium is provided by hair straightening technologies.

    Sulfhydryl groups in the active site of an enzyme can form noncovalent bonds with the enzyme's substrate as well, contributing to covalent catalytic activity in catalytic triads. Active site cysteine residues are the functional unit in cysteine protease catalytic triads. Cysteine residues may also react with heavy metal ions (Zn2+, Cd2+, Pb2+, Hg2+, Ag+) because of the high affinity between the soft sulfide and the soft metal (see hard and soft acids and bases). This can deform and inactivate the protein, and is one mechanism of heavy metal poisoning.

    Mark Hyman, MD


    Many cofactors (non-protein-based helper molecules) feature thiols. The biosynthesis and degradation of fatty acids and related long-chain hydrocarbons is conducted on a scaffold that anchors the growing chain through a thioester derived from the thiol Coenzyme A. The biosynthesis of methane, the principal hydrocarbon on earth, arises from the reaction mediated by coenzyme M, 2-mercaptoethyl sulfonic acid. Thiolates, the conjugate bases derived from thiols, form strong complexes with many metal ions, especially those classified as soft. The stability of metal thiolates parallels that of the corresponding sulfide minerals.

    Molecular Aspects of Thimerosal-induced Autism
    Phosphatidylinositide 3-kinases

    Dr. Richard Deth

    Methionine synthase
    Pantothenic acid
    Last edited: Jan 30, 2014
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  2. Radio


    Poisoning the Mitochondria
    Here is a list of poisons that can be used in the study of oxygen consumption by mitochondria, including sources and considerations for their use.
    • Electron transport inhibitors
      • Rotenone
      • Antimycin
      • Cyanide
      • Malonate (succinate dehydrogenase inhibitor)
    • Uncoupling agents
      • 2,4-Dinitrophenol (DNP)
      • Carbonyl cyanide p-[trifluoromethoxy]-phenyl-hydrazone (FCCP)
    • Oligomycin (inhibitor of oxidative phosphorylation)
    With the exception of malonate and cyanide, these poisons are much more soluble in ethanol than in water. Adding even a small quantity of ethanol to an aqueous medium increases its capacity for oxygen. A Clark electrode detects such an increase as a temporary rise in oxygen content, followed by the steady state that would be expected after the addition of the agent. We refer to this 'blip' on the record as an ethanol artifact.

    Electron transport inhibitors
    ETS inhibitors act by binding somewhere on the electron transport chain, literally preventing electrons from being passed from one carrier to the next. They all act specifically, that is, each inhibitor binds a particular carrier or complex in the ETS. Irreversible inhibition results in a complete stoppage of respiration via the blocked pathway. Competitive inhibition allows some oxygen consumption since a "trickle" of electrons can still pass through the blocked site. Although it allows some oxygen consumption, competitive inhibition prevents maintenance of a chemiosmotic gradient, thus the addition of ADP can have no effect on respiration.

    Thiosulfate + cyanide [​IMG] sulfite + thiocyanate

    Cyanide poisoning
    occurs when a living organism is exposed to a compound that produces cyanide ions (CN−) when dissolved in water. Common poisonous cyanide compounds include hydrogen cyanide gas and the crystalline solids potassium cyanide and sodium cyanide. The cyanide ion halts cellular respiration by inhibiting an enzyme in the mitochondria called cytochrome c oxidase. Cyanide poisoning is a form of histotoxic hypoxia because the cells of an organism are unable to use oxygen, primarily through the inhibition of cytochrome c oxidase. Acute hydrogen cyanide poisoning can result from inhalation of fumes from burning polymer products that use nitriles in their production, such as wool, silk, polyurethane, or vinyl. If cyanide is inhaled it causes a coma with seizures, apnea, and cardiac arrest, with death following in a matter of minutes. At lower doses, loss of consciousness may be preceded by general weakness, giddiness, headaches, vertigo, confusion, and perceived difficulty in breathing.

    Chronic exposure
    In addition to pesticide and insecticide, cyanide is contained in tobacco smoke, smoke from building fires and some foods, like almonds, apricot kernel, apple seeds, orange seeds, and cassava (also known as yuca or manioc). Vitamin B12 in the form of hydroxycobalamin, or hydroxocobalamin, may reduce the negative effects of chronic exposure, and a deficiency can lead to negative health effects following exposure.

    Exposure to lower levels of cyanide over a long period (e.g., after use of cassava roots as a primary food source in tropical Africa) results in increased blood cyanide levels, which can result in weakness and a variety of symptoms, including permanent paralysis, nervous lesions, hypothyroidism, and miscarriages. Other effects include mild liver and kidney damage.

    Summary Fact Sheet on Cyanide
    Last edited: Jan 30, 2014
  3. Radio


    Where cyanide is found and how it is used
    • Cyanide is released from natural substances in some foods such as cassava, lima beans, almonds, Pits and seeds of common fruits, such as apricots, apples, and peaches, may have substantial amounts of chemicals which are metabolized to cyanide. The edible parts of these plants contain much lower amounts of these chemicals.
    • Cyanide is contained in cigarette smoke and the combustion products of synthetic materials such as plastics. Combustion products are substances given off when things burn.
    • In manufacturing, cyanide is used to make paper, textiles, and plastics. It is present in the chemicals used to develop photographs. Cyanide salts are used in metallurgy for electroplating, metal cleaning, and removing gold from its ore. Cyanide gas is used to exterminate pests and vermin in ships and buildings.
    • If accidentally swallowed, chemicals found in acetonitrile-based products that are used to remove artificial nails can produce cyanide when metabolized by the body.
    • Hydrogen cyanide, under the name Zyklon B, was used as a genocidal agent by the Germans in World War II.
    • Reports have indicated that during the Iran-Iraq War in the 1980s, hydrogen cyanide gas may have been used along with other chemical agents against the inhabitants of the Kurdish city of Halabja in northern Iraq.
    How you could be exposed to cyanide
    • You could be exposed to cyanide by breathing air, drinking water, eating food, or touching soil that contains cyanide.
    • Cyanide enters water, soil, or air as a result of both natural processes and industrial activities. When present in air, it is usually in the form of gaseous hydrogen cyanide.
    • Smoking cigarettes is probably one of the major sources of cyanide exposure for people who do not work in cyanide-related industries.

    Cyanide poisoning
    TST Gene:
    Thiosulfate Sulfurtransferase

    Why Is Malonic Acid Bad?

    Malonic acid is an extremely potent metabolic inhibitor. In whatever organ it is found, your metabolism is slowed down. In fact it almost grinds to a halt. Then this organ can’t use as much oxygen, nor make as much energy (body energy is called ATP) as it should. Consequently we make fewer amino acids and can’t make as much protein as we should. This leads to lowered immunity by reducing glutathione. The organ is extremely handicapped. There is even a direct effect of malonate on immunity.

    Malonate-Free Foods
    Last edited: Jan 30, 2014
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  4. Radio


    Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. The mammalian enzyme has an extremely complicated structure and contains 13 subunits, two heme groups, as well as multiple metal ion cofactors – in all, three atoms of copper, one of magnesium and one of zinc.

    This enzyme mediates the final reaction in the electron transport chain and transfers electrons to oxygen, while pumping protons across the membrane. The final electron acceptor oxygen, which is also called the terminal electron acceptor, is reduced to water in this step. Both the direct pumping of protons and the consumption of matrix protons in the reduction of oxygen contribute to the proton gradient. The reaction catalyzed is the oxidation of cytochrome c and the reduction of oxygen.


    Cyanide, sulfide, azide, and carbon monoxide all bind to cytochrome c oxidase, thus competitively inhibiting the protein from functioning, which results in chemical asphyxiation of cells. Methanol in methylated spirits is converted into formic acid, which also inhibits the same oxidase system.

    "The myelin sheath is made of phospholipids whose synthesis depends on cytochrome c oxidase activity"

    Histotoxic hypoxia
    is the inability of cells to take up or utilize oxygen from the bloodstream, despite physiologically normal delivery of oxygen to such cells and tissues. Histotoxic hypoxia results from tissue poisoning, such as that caused by alcohol, narcotics, cyanide (which acts by inhibiting cytochrome oxidase), and certain other poisons like hydrogen sulfide (byproduct of sewage and used in leather tanning).

    Histotoxic hypoxia refers to a reduction in ATP production by the mitochondria due to a defect in the cellular usage of oxygen. An example of histotoxic hypoxia is cyanide poisoning. There is a profound drop in tissue oxygen consumption since the reaction of oxygen with cytochrome c oxidase is blocked by the presence of cyanide

    Histotoxic literally means that the cells have been poisoned. There is no problem getting the oxygen to the tissue - the lungs, blood and circulatory system are all working just fine. However, the tissue is unable to use the oxygen. Cyanide leads to histotoxic hypoxia by poisoning the systems that utilize oxygen to create energy and preventing them from using the oxygen. Even though there is plenty of oxygen there, the cells experience a lack of oxygen and are affected as if there was too little/no oxygen available.

    Hydrogen sulfide is produced in small amounts by some cells of the mammalian body and has a number of biological signaling functions. (Only two other such gases are currently known: nitric oxide (NO) and carbon monoxide (CO).

    The gas is produced from cysteine by the enzymes cystathionine beta-synthase and cystathionine gamma-lyase. It acts as a relaxant of smooth muscle and as a vasodilator. Eventually the gas is converted to sulfite in the mitochondria by thiosulfate reductase, and the sulfite is further oxidized to thiosulfate and sulfate by sulfite oxidase. The sulfates are excreted in the urine. Due to its effects similar to nitric oxide (without its potential to form peroxides by interacting with superoxide), hydrogen sulfide is now recognized as potentially protecting against cardiovascular disease. The cardioprotective role effect of garlic is caused by catabolism of the polysulfide group in allicin to H 2S, a reaction that could depend on reduction mediated by glutathione.

    Though both nitric oxide (NO) and hydrogen sulfide have been shown to relax blood vessels, their mechanisms of action are different: while NO activates the enzyme guanylyl cyclase, H2S activates ATP-sensitive potassium channels in smooth muscle cells. Researchers are not clear how the vessel-relaxing responsibilities are shared between nitric oxide and hydrogen sulfide. However there exists some evidence to suggest that nitric oxide does most of the vessel-relaxing work in large vessels and hydrogen sulfide is responsible for similar action in smaller blood vessels.

    In Alzheimer's disease the brain's hydrogen sulfide concentration is severely decreased. In a certain rat model of Parkinson's disease, the brain's hydrogen sulfide concentration was found to be reduced, and administering hydrogen sulfide alleviated the condition. In trisomy 21 (Down syndrome) the body produces an excess of hydrogen sulfide. Hydrogen sulfide is also involved in the disease process of type 1 diabetes. The beta cells of the pancreas in type 1 diabetes produce an excess of the gas, leading to the death of these cells and to a reduced production of insulin by those that remain.

    Hydrogen sulfide
    Copper Linus Pauling Institute
    Oxidative phosphorylation
    Cytochrome c oxidase
    Histotoxic Hypoxia

    Glucose-6-phosphate dehydrogenase (G6PD),
    This is the most common genetic mutation in the human population. It causes red blood cells to be less able to recycle their glutathione, and can thus lead to early death of these cells. This is normally a disadvantage, but the benefit in malaria is that the malaria parasites inhabit the red blood cells and depend on the antioxidant system in the red blood cells for their survival, GDPDD would hamper control of oxidative stress,

    (G6PD) is the first and rate-limiting enzyme of the pentose phosphate pathway, is a major intracellular source of NADPH generation. Previous reports have demonstrated that NADPH produced by G6PD is required for both the production of ROS, including superoxide anions and NO, and the elimination of these ROS via glutathione peroxidase and catalase in different cell types. Recently, we revealed that G6PD is highly expressed in the adipocytes of several obese animal models, and its overexpression in the adipocytes provoked the dysregulation of lipid metabolism and adipocytokine expression, resulting in insulin resistance. Because the levels of G6PD expression are enhanced specifically in the adipocytes of obese subjects, we were prompted to investigate whether G6PD overexpression in adipocytes affects oxidative stress, inflammatory signals, and macrophage gene expression, thus mediating metabolic disorders.



    Whether one needs to supplement with D-ribose depends on one's lifestyle and state of health. Generally, the body makes enough D-ribose in tissues like the heart, skeletal muscle, nerve tissue, and the brain to meet its daily metabolic needs. However, people whose cells and tissues are oxygen depleted, or because of illness are otherwise metabolically challenged, may be deficient in D-ribose. Because their energy demands exceed what their bodies are able to produce, people with ischemic heart disease, congestive heart failure (CHF), hypertension, fibromyalgia, and chronic fatigue syndrome, in addition to serious athletes, need to supplement with D-ribose.

    Oxygen deprivation, which characterizes ischemic heart disease, forces the body make energy through a means other than oxidative phosphorylation. To survive, the body will switch to glycolysis, or glucose metabolism, a much less metabolically efficient, albeit very important, process which provides the body large amounts of energy in short bursts. The problem with glycolysis replacing oxidative phosphorylation as the primary means of energy production is that it will cause exhaustion over time. The body, no longer able to recycle ATP, will also become unable to synthesize it de novo, as the glucose it would have reserved for D-ribose synthesis is eventually used for fuel.

    Remember in energy utilization, the body breaks ATP down into ADP, which it recycles into ATP again. Under disease conditions of greater energy need, the body will start breaking down ADP for energy rather than recycle it back into ATP. The resulting AMP molecules, incompatible with sustained cellular function, are quickly broken apart. The byproducts of AMP molecules, D-ribose and adenine, get washed out of cells, which deprives the body of an energy substrate supply with which to synthesize ATP de novo.

    People with ischemia, diastolic dysfunction, or other compromising conditions need to supplement with D-ribose to replenish their energy pool and normalize cardiac function. For healthier individuals, D-ribose supplementation can alleviate symptoms of discomfort following exercise. Athletes can attenuate shaky weak limbs and fatigue following strenuous exercise and non-athletic people can avoid delayed onset muscle soreness. Supplementation with D-ribose serves as a rate-limiting step: it surpasses the need for D-ribose synthesis, a slow process which must be accomplished before ATP synthesis can begin. In other words, supplementing with D-ribose helps one faster generate energy.

    Supplementing D-ribose can activate a mast cell inflammatory response.

    G6PD deficiency is the most common human enzyme defect.
    Glucose-6-phosphate dehydrogenase
    Pentose phosphate pathway
    Glucose-6-Phosphate Dehydrogenase in Adipocytes Stimulates Oxidative Stress
    Ribose Wiki
    Last edited: Jan 30, 2014
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  5. alex3619

    alex3619 Senior Member

    Logan, Queensland, Australia
    I think, but have not checked to confirm, that raw cashews and many native foods around the world contain high amounts of cyanide. Cashews are not eaten raw, even "raw" cashews we can buy are actually cooked. Many wild foods are processed first by soaking, cooking etc. to remove cyanide. This is what happens with cassava.

    One of my old ME docs had great success with about 60% of patients who did not smoke, but zero percent who did. He wouldn't treat them unless they gave up smoking as a result of this finding in his clinic.
  6. taniaaust1

    taniaaust1 Senior Member

    Sth Australia
    I have molybdenum deficiency.. due to one of my SNPs. Ive been trying to get my molybdenum up for a few years to a normal level (standard molybdenum supplementation helped some but Im only still deficient a only half of normal range.

    Its hard that many of us have so many different things going on in our bodies. (I also have asthma) So this thread was quite interesting to me..thanks
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  7. Radio


    Hey, Taniaaust

    Please post the SNP that affect the molybdenum metabolism?
  8. taniaaust1

    taniaaust1 Senior Member

    Sth Australia
    Its rather a case of the molybdenum deficiency being caused by excess sulfites depleting it.. from having a CBS mutation (I assume me having that CBS mutation is why I had nearly a nil level showing up on my test).


    The CBS mutation not only leads to excess taurine, but can also lead to excess sulfur groups. For this reason, it may be a good idea to limit sulfur intake. Excess sulfur intake can trigger a stress response or chronic stress. Sulfur is normally bound to amino acids, but the CBS upregulation can instead release the sulfur groups to sulfites in the body. There are many things one may need to avoid with a CBS upregulation. Some of the items include garlic, broccoli, eggs, onions, legumes, meat, Epsom salt baths, alpha lipoic acid, glutathione, chelating agents such as DMPS, NAC, Milk Thistle, various other supplements, and much more. Please look to other sources for foods and supplements that are high in sulfur.

    Supplementing with molybdenum may help as excess sulfites deplete it. Manganese is also important in ammonia detoxification. A Low protein diet can help as the body will have less ammonia to detoxify. It's important to measure molybdenum and manganese with a minerals test before supplementing."

    above from my genetic genie methyalation report

    5 days of supplmentation with molybdenum had me able to do maths in my head again.. something I hadnt been able to do for years.
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  9. Radio


    Ok, where do we go from here?
    The core of my hypothesis is very simple. Oxidative phosphorylation is a contributing factor in many chronic diseases. The mitochondrial needs phospholipids to maintain cellular integrity. The first step in recovery is Methylation / phospholipid support. It is critical that we identify these environmental poisons and eat a diet that supports this dysfunctional metabolism.

    Supplementing Molybdenum intakes of 500 mcg/day to 1,500 mcg/day can increased
    urinary copper excretion.
    Last edited: Jan 31, 2014
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  10. Radio


    Table salt
    Contrary to popular belief, table salt is not just sodium chloride. It also contains additives that are designed to make it more free-flowing. Ferrocyanide, talc, and silica aluminate are commonly included. Aluminum intake leads to neurological disorders, particularly when no selenium is provided to help the body to chelate it. Aluminum bio-accumulates inside the body, causing further degeneration over time. Talc is a known carcinogen, though its effects upon ingestion have not been heavily studied. While it was once used in baby powders, the majority of such products now use cornstarch instead of talc, because of the known health risks. The F.D.A. has a special provision to allow talc in table salt, even whilst it is prohibited in all other foods, due to toxicity issues. According to current regulations, table salt can be up to 2% talc.



    Top 10 Foods Highest in Potassium

    RDA guidelines for potassium 4,500 milligrams a day
    Last edited: Feb 4, 2014
  11. Radio


    The PST sulfation pathway is necessary for the breakdown and removal of certain toxins in the body. This includes the processing of a type of chemical called a phenol. Phenols are a regular and necessary part of life.

    All foods contain some phenolic compounds. However, some foods have a much higher content than others do. If the sulfation pathway is not functioning well, as with many children with autism, a person may not be able to process out the phenolic compounds as fast as they consume them. There is a cumulative effect. When the phenols start backing up in the system, it can cause a myriad of negative reactions. Symptoms of phenol intolerance include night waking, night sweats, irritability, eczema and other skin irritations. The symptoms of phenol intolerance and yeast may be very similar because they both involve the body trying to deal with toxins. The detoxification pathway processes other phenolic compounds including salicylates (a subset of phenols), artificial food colorings, artificial flavorings, and some preservatives. Besides requiring PST, research has found the salicylates further suppress the activity of any PST enzyme present, making matters worse. Food dyes also have been shown to inhibit the PST enzyme.

    Epsom Salt supplies readily absorbable sulfates which attach to phenols and sets them up for being excreted via the kidneys.

    The Sunderland Protocol

    The role of sulphation may well be one of the pivotal factors in the causation of autism, yet it is poorly understood and has received scant attention. The role of sulphates in the immune system, in the effectiveness of hormones and in maintaining the integrity of intestinal function, kidney function and detoxification system is deserving of much greater attention than it currently receives.

    Owens (1998) has drawn the attention to the importance of sulphation issues in chemical bodies called GAGs (Glucosyl Acetyl Glucosamines) which have huge implications for many functions including brain development. Processes involving inflammation, such as that which would result from infections that may be acquired naturally or from introduction through vaccine programmes, will result in stripping of the sulphate containing GAGs from the intestinal wall.

    Owens has suggested that these GAGs will form the main reservoir of sulphates held in the body. Therefore, any lingering inflammatory process will result in sulphate depletion. Waring (2000b) has also presented data indicating that the conversion of sulphite to sulphate is severely inhibited after immunisation of adult students against hepatitis B.

    Sulphate ions are poorly absorbed from foodstuffs but may well be better absorbed through the skin. That is the rationale for the use of Epsom Salt (Magnesium Sulphate) in the bathwater of children with autism. (Taken from The Sunderland Protocol - a paper presented at the Durham Conference 2000).


    Sulphur is so critical to life that the body will apparently borrow protein from the muscles to keep from running to low. Many systems in the body will not function well in a low-sulphate environment. One of the things it influences is the hormone that helps humans recognize faces and " socialize ". Increasing sulphur in the body can improve socialization and related issues.

    If growth factors were bankers, sulphate would be their money. Growth factors use sulphate to do their business. That is why it is known that if you become VERY deficient in sulphate you will stop growing if you are a child, or you will start to break down (catabolize) your own muscle to make up for this deficiency. That means if your child has not been growing, and has very flimsy muscles, you should be concerned that their sulphate chemistry may be hurting. When this happens in very sick adults, it puts them into a state called cachexia, a wasting process that happens in Alzheimers disease, Aids, Cancer, and an autism spectrum disorder called Rett Syndrome.

    Dr Rosemary Waring, a biochemist researching the sulphate levels in autistic children, found that most people with autism conditions have a deficiency in a key detoxification pathway. The pathway involves using sulfur in the form of sulfate (known as sulfation). The enzyme involved is phenol sulfur-transferase (PST), but the problem is thought to hinge on an inadequate supply of usable sulfate ions, not the metabolic enzyme itself. Dr Waring has found that most autistic spectrum kids, and lots of others with neurological conditions, are very low in sulphate and excrete higher levels of sulphate in urine. They may be as low as 15% of neurologically typical people. People with low or no ability to convert compounds to sulfate have problems handling environmental chemicals including food colours, artificial flavoring, and preservatives, some medications, and even some chemicals produced within the body. They include people with other conditions such as Alzheimers disease, Parkinsons disease, Rheumatoid Arthritis, and chemical sensitivities.

    Once the process had started it would continue on a slow, but steady, downward spiral. Sulphates in the blood help rid the body of waste products by making them water soluble and therefore easily excreted. Low levels of sulphate may lead to retention of toxins as the body may have more toxins to process than it can because of a lack of sulphur, which in turn may lead to bio-chemical effects on the central nervous system.

    Epsom Salt can provide essential sulphate in a readily absorbable form to unclog this " bottleneck " by supplying more sulphur to increase the amount of toxins that can be processed from the body. As the body takes in more sulphur, more toxins are processed.

    Sulphates & the Gut

    Sulphation capacity affects the gastro-intestinal tract. The mucins which line the gut are sulphated glycoproteins which rely on sulphation to maintain their structure. The PST enzyme ensures that your mucous membranes are coated with a slimy surface to protect them and make them resilient (membranes of the gut, nose, ears etc.)

    Reduced sulphation has been associated with inflammation, gut dysfunction, and increased permeability. Sulphates help to hydrolate (surround toxins with extra water molecules) toxins out of your body. If the body builds up with toxins the gut can become permeable to indigested peptides from gluten and casein (milk products), which then travel to the brain looking like pseudo neurotransmitters, but actually acting as opiods.

    Researchers have noted that dairy and gluten digestion difficulties would be expected in people with low sulfation, lending credence to the gluten-free/casein-free diet approach for these individuals.

    In autism the balance of gastro-intestinal hormones seems to be altered, possibly due to the interaction between sulphation and digestive peptide hormones. Gastrin is active when sulphated, and so is cholecystokinin (CCK), a peptide active in both the gut and the brain. The secretion of CCK, liberated by gastrin, releases another hormone - secretin, which stimulates the release of digestive enzymes from the pancreas. This essential cascade process can be blocked at any stage, resulting in reduced levels of secretin, and therefore, a blocking of the essential pancreatic enzymes.

    The blockage may very well be averted if sufficient sulphates are available. Epsom Salts can provide those needed sulphates.

    PST/sulphate deficiency also impairs the metabolism of classical neurotransmitters such as serotonin and dopamine; impaired breakdown and metabolism of the bile pigments bilirubin and biliverdin; and decreased secretion of pancreatic enzymes and of bile from the gall bladder and biliary tract into the intestines. This would result in low uptake of certain vitamins and other nutrients from the intestines; reduced activity of gastrin (and subsequent reduced secretion of stomach acid, mucus, and pepsin in the stomach), and, probably, reduced production of secretin further downstream.

    B6 in the form of P5P (pyridoxal-5-phosphate)
    inhibits PST (phenol sulphur-transferase) activity. (This could be why some children show adverse effects when supplements high in P5P are started) However the same study showed that increasing magnesium supplementation reverses this inhibition.

    The PST sulfation pathway
    Sulphur -Sulphate -Liver Detoxification Sensitivity.htm
    Last edited: Feb 1, 2014
  12. Radio


    When the body is dealing with toxicity from any source it does put stress on the well as the immune system. Salicylates and phenols are no different. They are toxic in high amounts.

    The accumulation of phenols in the body exerts a toxic effect. The reactions are not considered "allergy" type reactions....they are "toxicological".

    If you're experiencing a worsening in symptoms when taking aspirin/ibuprofen....salicylates would be the first thing to look into. Many foods are high in salicylate....especially herbs, spices, fruits and veggies. If you find that your symptoms worsen when eating the foods that contain high amounts of could be that your PST/sulfation is weak.

    PST = phenolsulphotransferase. Its an enzyme which is involved in of the body's key detoxification pathways.

    When the enzyme is weak...detoxification is impaired. The PST enzyme detoxifies salicylates, phenols, neurotransmitters, hormones, medications, etc. Salicylates can inhibit the enzyme up to 50%.

    Some people have too little of an important enzyme called phenol sulfotransferase (PST). It is made in the intestines, which need PST to metabolize (detoxify) the salicylates and the high-phenolic petroleum-based additives.

    However, the brain also requires PST for "housekeeping" duties involving neurotransmitters- those chemicals which jump the tiny space (synapse) between brain cells (neurons). Each time a neuron "fires" and the neruotransmitter "jums" that space, PST must prepare the space to "fire" again. This is measured in nanoseconds, occurs millions of times a second all over the brain and must be perfectly synchronized.

    If a person is marginal or low in PST, and eats lots of high-phenolic foods and additives, there may not be enough PST left to do the "cleanup up" work in the brain, thus preventing neurons from firing effectively. Moreover, it seems that salicylates (which are also phenolic compounds) not only need PST but actually suppress it's production, making PST levels even lower.

    This explanation is over-simplified and the evidence is indirect, but it may help explain why the avoidance of salicylates at the start of the Feingold Program is important. Once suppression is stopped, there may be some recovery, leading to the later tolerance of salicylates usually seen. Surely, this is only part of a larger and complex picture, but in this area the circumstantial evidence is mounting.

    The PST sulfation pathway is necessary for the breakdown and removal of certain toxins in the body. This includes the processing of a type of chemical called a phenol. Phenols are a regular and necessary part of life. All foods contain some phenolic compounds. However, some foods have a much higher content than others do. If the sulfation pathway is not functioning well, a person may not be able to process out the phenolic compounds as fast as they consume them. There is a cumulative effect. When the phenols start backing up in the system, it can cause a myriad of negative reactions

    From my research....the main reason for low functioning PST is low sulfate in the body. Sulfate is essential to keep PST functioning....sulfate is also necessary in maintaing the integrity of the intestinal lining.
    Low sulfate levels = increased intestinal permeability (leaky gut).

    Low sulfate can occur for a variety of reasons. Some gut infections (bacteria/yeast) can produce large amounts of phenols....which may overload the PST enzyme....causing a shortage of available sulfate. There are other reasons but it can get quite complicated so I'll leave it at that.

    Anyways, yes.....all of this does place stress on the liver. If the gut is leaky that creates a huge burden on the liver as well. However, when PST is down.....the only way to take stress off of the liver is to take stress off of the PST enzyme.

    Aspirin, high phenolic foods, artificial flavorings, food dyes and preservatives are some of the things which inhibit the enzyme.

    Foods contain salicylates

    Cocoa has very high amounts of phenol/histamine. :bang-head:
    Last edited: Feb 4, 2014
    merylg likes this.
  13. Rand56

    Rand56 Senior Member

    Myrtle Beach, SC
    hi Radio

    Dr. Stephanie Seneff, a senior research scientist at MIT, also feels there is a big problem with sulfate deficiency along with sulfate transport within the body. Her best recommendation to raise those levels is thru sun exposure. Apparently the sun synthesizes chlolesterol sulfate in the skin along with Vit. D sulfate.

    She is also in the camp that lowering cholesterol is a bad idea in that the heart needs cholesterol.

    I've listened to a couple of her interview podcasts on and also she has a good interview with Dr. Mercola on

    If anyone is interested in listening/watching those, just go to both of those sites and search her name.

  14. Radio



    Phase I are excreted by the kidneys. The fat-soluble output products of Phase I are further processed in Phase II. The fat-soluble outputs of Phase I can be more poisonous than the original toxins. These intermediate substances are highly reactive --- they produce a lot of free radical activity. That is why it is so important to make sure that these intermediate products are removed by Phase II as soon as they are generated by Phase I. If Phase II detoxification is not working fast enough, the products of Phase I will accumulate and harm the liver. You may end up with multiple chemical sensitivity if this happens. Therefore, it is very important that you don’t increase Phase I unless Phase II is working well enough to handle the increased load. ie Don’t take just any product that says it improves “liver health” because it might induce too strong a Phase I reaction in you.

    If you don’t have the results of a liver function test to guide you, then the best place to start is:

    1) Improve Hormonal Status: Thyroid improves both the liver‘s Phase I and Phase II.

    2) Improve Phase II Detoxification: Substances that improve Phase II detoxification are sulfates, TMG, SAMe, lecithin, B12, B6, magnesium, folic acid, taurine, Ulva Rigida, calcium-d-glucarate, and things that help you increase glutathione. Garlic oil, rosemary, cabbage, and brussels sprouts also enhance Phase II activity. Lowering inflammation improves Phase II. Some substances that lower inflammation are: probiotics, transfer factor, IgA, colostrum, bromelain, pancreatic enzymes, progesterone, Mead oil, coconut oil, and emu oil. The fat-soluble vitamins in fish liver oil (A, E, D, and K) also control inflammation, although too much fish oil can be hard on the liver. Bioflavonoids help control inflammation, but these must also be removed by the liver, and may place a strain on the capabilities of the liver. You will have to experiment and find that which you can tolerate in this list.

    3) Improve Anti-oxidant Status: Nutrients that improve anti-oxidant status are vitamin A, C, E, coenzyme Q10, taurine, glutathione, selenium, NADH, and lipoic acid. They will help protect you from the free radical activity of the substances put out by Phase I. A small amount of bioflavonoids also improve anti-oxidant status, but they aren’t always appropriate.

    4) Reduce Exposure To Toxins: This is only common sense. If there are fewer toxins to process, you don’t overburden the liver. This means avoiding pesticides, heavy metals, and toxins in everyday household and personal care items. It also means reducing your exposure from toxins generated in the gut by harmful bacteria and yeast. Charcoal, fiber, and a decent intestinal transit time will help. The transit time needs to be slow enough that the food is digested, but fast enough that there isn’t time to reabsorb all the toxins that the liver has dumped into the intestines.

    What do you do if you Phase I is working much faster than Phase II?

    You try to improve Phase II. Also, try to limit exposure to toxins that will make Phase I work too fast. Eliminate exposure to exhaust fumes, paint fumes, tobacco, carbon tetrachloride, organo-phosphorus pesticides, and the preservatives BHT and BHA. Increasing the use of anti-oxidants will help protect you from some of the Phase I products.

    Can you take things to slow down Phase I?

    In general, you don’t want to interfere with the ability of the liver to perform its Phase I detoxification functions. However, sometimes you have to choose the lessor of two evils. If Phase II is so slow or Phase I is so fast that there is an excessive buildup of the Phase I intermediate outputs, then you may be suffering from many chemical sensitivities, and may have to consider slowing down Phase I. This would be only a temporary solution while you work on getting Phase II working.

    Taking 500 mg of niacinamide 3 or 4 times per day will inhibit the enzymes in Phase I. Certain bioflavonoids can interfere with Phase I enzymes. Bioflavonoids are also anti-oxidants and can reduce inflammation. For this reason, a modicum of bioflavonoids might be helpful. Something as simple as a half grapefruit per day can be protective.

    Be sure to consult with your physician before experimenting with any Phase I inhibitors since interfering with Phase I enzymes can slow the clearance of drugs. Example: doctors will tell you not to take grapefruit juice when using certain medications. Grapefruit juice interferes with the Phase I enzyme that clears/detoxifies most drugs. Milk thistle also interferes with this same enzyme, and should be approached with particular caution when taking prescription drugs.

    What do you do if you have the opposite problem and Phase II is working well, but your Phase I is slow?

    Phase I can be increased by protein, oranges, tangerines, broccoli, brussels sprouts, saturated fats, sassafras, schizandra, glucocorrticoids, ginseng, licorice, vitamin B2, B6, B12, folic acid, phospholipids, branch chain amino acids, niacin or NADH (coenzyme niacin). You can also attempt to get rid of the things that slow down Phase I. These are heavy metal toxicity, estrogen (birth control pills), certain bioflavonoids (quercetin, milk thistle, grapefruit juice), iron deficiency, sugar excess, partially hydrogenated fats, bacteria toxins, niacinamide, Nizoral, and Diflucan. [22] Some interfere with many of the phase 1 enzymes, and others are more specific. For instance, large doses of niacinamide would be expected to interfere with many of the enzymes, whereas Nizoral interferes with the 2C19 enzymes, and Diflucan interferes with the 3A enzyme.

    What is Phase III?

    Not much is known about Phase III. One known process is the further metabolism of glutathione conjugates. Another is the further metabolism of sulfate conjugates. Referring to a possible function of Phase III of the liver, Professor Sit Kim Ping, of the National University of Singapore states,

    “the efflux of sulfate conjugates of several phenolic compounds has been demonstrated to be ATP-dependent.”

    This means that if you have low cellular energy, your liver will have problems removing phenolics like estrogen, bioflavonoids, and food colorings with sulfation. Many of the mercury poisoned and the autistic have a problem removing phenolics. Could it be partially due to low cellular energy?

    When the Phase II glucuronidation pathway is overloaded, more of the work falls to the Phase II sulfation pathway. Then if the Phase II sulfation pathway becomes overloaded, more of the work falls to the Phase II glutathione conjugation pathway. The use of this last pathway will deplete the available glutathione and make us more susceptible to the free radicals produced by Phase I.

    This has implications for all of us, but particularly for those who are mercury poisoned. All of us are probably somewhat low on sulfates because of the intestinal inflammation, but those with mercury poisoning can be very low on sulfates because the body is dumping the sulfates in the urine. It seems that if you could improve the glucuronidation and bring the sulfate levels back up, then you would have a better chance of improving glutathione levels. Better glutathione levels in the mercury poisoned are very important. The glutathione levels should be up before you start the mercury chelation, or else the recirculating mercury will damage the nervous system. (Another way to spare glutathione is to avoid estrogens and to take a balanced amount of coenzyme Q10, NADH, lipoic acid, vitamin C and E.)

    Detoxification (The Liver)

    The mast cells in the light of new knowledge of heparin and sulfated mucopolysaccharides
    Last edited: Feb 1, 2014
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  15. Rand56

    Rand56 Senior Member

    Myrtle Beach, SC

    I also found this article she wrote. It was written in 2010 so this may be old news to many of you. I figure I'd pass it along anyway. It's titled.....

    Could Sulfur Deficiency be a Contributing Factor in
    Obesity, Heart Disease, Alzheimer's
    and Chronic Fatigue Syndrome?
    Radio likes this.
  16. Radio


    Could Sulfur Deficiency be a Contributing Factor in Chronic Fatigue Syndrome?
    by Stephanie Seneff

    Obesity is quickly becoming the number one health issue confronting America today, and has also risen to epidemic proportions worldwide. Its spread has been associated with the adoption of a Western-style diet. However, I believe that the widespread consumption of food imports produced by U.S. companies plays a crucial role in the rise in obesity worldwide. Specifically, these "fast foods" typically include heavily processed derivatives of corn, soybeans, and grains, grown on highly efficient mega-farms. Furthermore, I will argue in this essay that one of the core underlying causes of obesity may be sulfur deficiency.

    Sulfur is the eighth most common element by mass in the human body, behind oxygen, carbon, hydrogen, nitrogen, calcium, phosphorus, and potassium. The two sulfur-containing amino acids, methionine and cysteine, play essential physiological roles throughout the body. However, sulfur has been consistently overlooked in addressing the issues of nutritional deficiencies. In fact, the American Food and Drug Administration has not even assigned a minimum daily requirement (MDR) for sulfur. One consequence of sulfur's limbo nutritional status is that it is omitted from the long list of supplements that are commonly artificially added to popular foods like cereal.

    Sulfur is found in a large number of foods, and, as a consequence, it is assumed that almost any diet would meet the minimum daily requirements. Excellent sources are eggs, onions, garlic, and leafy dark green vegetables like kale and broccoli. Meats, nuts, and seafood also contain sulfur. Methionine, an essential amino acid, in that we are unable to synthesize it ourselves, is found mainly in egg whites and fish. A diet high in grains like bread and cereal is likely to be deficient in sulfur. Increasingly, whole foods such as corn and soybeans are disassembled into component parts with chemical names, and then reassembled into heavily processed foods. Sulfur is lost along the way, and there is a lack of awareness that this matters.

    Experts have recently become aware that sulfur depletion in the soil creates a serious deficiency for plants [Jez2008], brought about in part by improved efficiency in farming and in part, ironically, by successful attempts to clean up air pollution. Over the last two decades, the U.S. farming industry has steadily consolidated into highly technologized mega farms. The high yield per acre associated with these farms results in greater depletion of sulfur each year by the tall, densely planted crops. Plants require sulfur in the form of the sulfate radical (SO4-2). Bacteria in well aerated soil, similar to nitrogen fixing bacteria, can convert elemental sulfur into sulfate through an oxidation process. Coal contains a significant amount of sulfur, and factories that burn coal for energy release sulfur dioxide into the air. Over time, sun exposure converts the sulfur dioxide to sulfate, a significant contributor to acid rain. Acid rain is a serious pollutant, in that hydrogen sulfate, a potent acid, penetrates lakes, making them too acidic for lifeforms to thrive. The Clean Air Act, enacted by congress in 1980, has led to substantial decreases in the amount of acid rain released into the atmosphere. Factories have introduced highly effective scrubbing technologies to comply with the law, and, as a consequence, less sulfate makes its way back into the soil.

    Modern farmers apply highly concentrated fertilizer to their soil, but this fertilizer is typically enriched in phosphates and often contains no sulfur. Excess phosphates interfere with sulfur absorption. In the past, organic matter and plant residues remained after the fruit and grain were harvested. Such accumulating organic matter used to be a major source of recyclable sulfur. However, many modern machinery-based methods remove a great deal more of the organic matter in addition to the edible portions of the plant. So the sulfur in the decaying organic matter is also lost.

    It is estimated that humans obtain about 10% of their sulfur supply from drinking water. Remarkably, people who drink soft water have an increased risk to heart disease compared to people who drink hard water [Crawford1967]. Many possible reasons have been suggested for why this might be true ( Proposed theories for soft water/hard water differences in heart disease), and just about every trace metal has been considered as a possibility [Biorck1965]. However, I believe that the real reason may simply be that hard water is more likely to contain sulfur. The sulfate ion is the most useful form of sulfur for humans to ingest. Water softeners provide a convenient environment for sulfur-reducing bacteria, which convert sulfate (SO4-2) into sulfide (S-2), emitting hydrogen sulfide gas. Hydrogen sulfide gas is a poison that has been known to cause nausea, illness and, in extreme cases, death. When the bacteria are thriving, the gas will diffuse into the air and give off a foul odor. Obviously, it is rare that the concentration is sufficiently high to cause severe problems. But the sulfate ion is lost through the process. Water that is naturally soft, such as water collected from rain run-off, also contains little or no sulfur, because it has gone through an evaporation-condensation cycle, which leaves behind all the heavier molecules, including sulfur.

    Although sulfur is an essential element in human biology, we hear surprisingly little about sulfur in discussions on health. Sulfur binds strongly with oxygen, and is able to stably carry a charge ranging from +6 to -2, and is therefore very versatile in supporting aerobic metabolism. There is strong evidence that sulfur deficiency plays a role in diseases ranging from Alzheimer's to cancer to heart disease. Particularly intriguing is the relationship between sulfur deficiency and muscle wasting, a signature of end-stage cancer, AIDS, Crohn's disease, and chronic fatigue syndrome.

    The African rift zone, where humans are believed to have first made their appearance several million years ago, would have been rich with sulfur supplied by active volcanism. It is striking that people living today in places where sulfur is abundantly provided by recent volcanism enjoy a low risk for heart disease and obesity.

    In my research on sulfur, I was drawn to two mysterious molecules: cholesterol sulfate and vitamin D3 sulfate. Researchers have not yet determined the role that cholesterol sulfate plays in the blood stream, despite the fact that it is ubiquitous there. Research experiments have clearly shown that cholesterol sulfate is protective against heart disease. I have developed a theory proposing that cholesterol sulfate is central to the formation of lipid rafts, which, in turn, are essential for aerobic glucose metabolism. I would predict that deficiencies in cholesterol sulfate lead to severe defects in muscle metabolism, and this includes the heart muscle. My theory would explain the protective role of cholesterol sulfate in heart disease and muscle wasting diseases.

    I have also argued that cholesterol sulfate delivers oxygen to myoglobin in muscle cells, resulting in safe oxygen transport to the mitochondria. I argue a similar role for alpha-synuclein in the brain. There is a striking relationship between Alzheimer's and sulfur depletion in neurons in the brain. Sulfur plays a key role in protectiing proteins in neurons and muscle cells from oxidative damage, while maintaining adequate oxygen supply to the mitochondria.

    When muscles become impaired in glucose metabolism due to reduced availability of cholesterol sulfate, proliferating fat cells become involved in converting glucose to fat. This provides an alternative fuel for the muscle cells, and replenishes the cholesterol supply by storing and refurbishing cholesterol extracted from defective LDL. Thin people with cholesterol and sulfur deficiency are vulnerable to a wide range of problems, such as Crohn's disease, chronic fatigue syndrome, and muscle wasting, because fat cells are not available to ameliorate the situation.

    Cholesterol sulfate in the epithelium protects from invasion of pathogens through the skin, which greatly reduces the burden placed on the immune system. Perhaps the most intriguing possibility presented here is the idea that sulfur provides a way for the skin to become a solar-powered battery: to store the energy from sunlight as chemical energy in the sulfate molecule. This seems like a very sensible and practical scheme, and the biochemistry involved has been demonstrated to work in phototrophic sulfur-metabolizing bacteria found in sulfur hot springs.

    The skin produces vitamin D3 sulfate upon exposure to sunlight, and the vitamin D3 found in breast milk is also sulfated. In light of these facts, it is quite surprising to me that so little research has been directed towards understanding what role sulfated vitamin D3 plays in the body. It is recently becoming apparent that vitamin D3 promotes a strong immune system and offers protection against cancer, yet how it achieves these benefits is not at all clear. I strongly suspect that it is vitamin D3 sulfate that carries out this aspect of vitamin D3's positive influence.

    Modern lifestyle practices conspire to induce major deficiencies in cholesterol sulfate and vitamin D3 sulfate. We are encouraged to actively avoid sun exposure and to minimize dietary intake of cholesterol-containing foods. We are encouraged to consume a high-carbohydrate/low-fat diet which, as I have argued previously (Seneff2010), leads to impaired cholesterol uptake in cells. We are told nothing about sulfur, yet many factors, ranging from the Clean Air Act to intensive farming to water softeners, deplete the supply of sulfur in our food and water.

    Fortunately, correcting these deficiencies at the individual level is easy and straightforward. If you just throw away the sunscreen and eat more eggs, those two steps alone may greatly increase your chances of living a long and healthy life.

    Jeffrey Smith interviews Dr. Stephanie Seneff about Glyphosate

    Lipid rafts
    Lipid bilayer
    Last edited: Feb 4, 2014
  17. xrayspex

    xrayspex Senior Member

    thanks for info radio....too brainfoggy for much tonight but rich v rec'd molybdenum to me for mcs but i couldnt tell if helps.stilll have some and selenium
    some genova test said i am phase 2 slow or something, stuff doesnt break down in me and keep circulate

    interesting about salicylates, advil and tylenol and many meds cause burn pain in spine now
    i dont tolerate the sun either
    viruses and autoimmune problems complicate things

    but i work full time and walk hour a day but lie down thruout day and limit other stimulation to survive

    i think guifanesen dr st amand probly relates to salyicylates and detox problem
    merylg and Radio like this.
  18. xrayspex

    xrayspex Senior Member

    you had this posted "Phase I can be increased by protein, oranges, tangerines, broccoli, brussels sprouts, saturated fats, sassafras, schizandra, glucocorrticoids, ginseng, licorice, vitamin B2, B6, B12, folic acid, phospholipids, branch chain amino acids, niacin or NADH (coenzyme niacin). You can also attempt to get rid of the things that slow down Phase I. These are heavy metal toxicity, estrogen (birth control pills), certain bioflavonoids (quercetin, milk thistle, grapefruit juice), iron deficiency, sugar excess, partially hydrogenated fats, bacteria toxins, niacinamide, Nizoral, and Diflucan. [22] Some interfere with many of the phase 1 enzymes, and others are more specific. For instance, large doses of niacinamide would be expected to interfere with many of the enzymes, whereas Nizoral interferes with the 2C19 enzymes, and Diflucan interferes with the 3A enzyme."]

    interesting, i had found a blog today where a person who feels rotten after consume garlic found orange juice to be antidote,perhaps its cus of phase 1 as in above
    broccoli and brussels etc tho make me feel rotten
    Gondwanaland, Star-Anise and Radio like this.
  19. xrayspex

    xrayspex Senior Member

    i will watch that stephanie video u just posted, thanks (or will i watch columbo reruns, hmmm lol)
    Radio likes this.
  20. Rand56

    Rand56 Senior Member

    Myrtle Beach, SC
    My gawd I've turned Radio into a Stephanie Seneff freak!! haha just kidding. I find her quite fascinating to listen to. I've listened to a number of different podcasts from different people, and I think she is one of the best that can keep my attention!
    merylg and Radio like this.

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