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Does hydrated magnesium six H2O shell cage provide a better transport for gas exchange?

Discussion in 'Ask Jack' started by John Schumacher, Oct 26, 2020.

  1. Does hydrated magnesium six H2O shell cage provide a better transport for gas exchange to the extracellular matrix than DDW water?

    A hydrated Mg2+ ion has a relatively robust innermost hydration shell with six bound water molecules and a second hydration layer. Fully hydrated Mg2+ ions bind to RNA.

    We know the release of phosphate from the nucleotide binding pocket of a myosin motor occurs only after step-wise hydration of Mg2+ by four water molecules. https://www.biorxiv.org/content/10.1101/817254v1.full.pdf

    With all the talk about DDW, without first thinking about hydrated alkaline metal ions and their behavior in human plasma, it seems silly to me. I believe we need to first understand cellular hydration both externally to the phospholipid biliary within the phospholipid biliary and within the cytoplasm.

    For example:

    Gas-Phase Reactions of Hydrated Alkaline Earth Metal Ions, M2+ (H2O)n (M = Mg, Ca, Sr, Ba and n = 4–7), With Benzene https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1401488/ Ion transport processes across cellular membranes are governed by the role of competitive intramolecular and intermolecular interactions between solvent molecules, proteins or peptides, and the ions of interest. The transfer of an ion through a hydrophobic environment can be effected by two mechanisms. The ion-carrier mechanism involves naturally occurring multidentate ligands known as ionophores. These ligands can arrange to form cavities with higher selectivity toward a specific ion in solution. Ionophores, such as valinomycin and nonactin, bind potassium ions preferentially over the other alkali metals. Once the ion–ionophore complex is formed, the outer hydrophobic surface of the “carrier” facilitates the transport into or across the nonpolar environment. The second ion transport mechanism involves channel-forming ionophores, like the gramicidins, which form hydrophilic pathways extending across a hydrophobic membrane allowing the passage of ions. The selectivity observed in solution for complexes between ionophores and metal ions is a consequence of the small differences between the stability constants of the cations with water and those of the cations with the ionophores.

    Hydrated Magnesium Cations Mg+(H2O)n, n ≈ 20–60, Exhibit Chemistry of the Hydrated Electron in Reactions with O2 and CO2 https://pubs.acs.org/doi/10.1021/jp206140k Ion–molecule reactions of Mg+(H2O)n, n ≈ 20–60, with O2 and CO2 are studied by Fourier-transform ion cyclotron resonance (FT-ICR) mass spectrometry. O2 and CO2 are taken up by the clusters. Both reactions correspond to the chemistry of hydrated electrons (H2O)n–. Density functional theory calculations predicted that the solvation structures of Mg+(H2O)16 contain a hydrated electron that is solvated remotely from a hexa-coordinated Mg2+. Ion–molecule reactions between Mg+(H2O)16 and O2 or CO2 are calculated to be highly exothermic. Initially, a solvent-separated ion pair is formed, with the hexa-coordinated Mg2+ ionic core being well separated from the O2•– or CO2•–. Rearrangements of the solvation structure are possible and produce a contact-ion pair in which one water molecule in the first solvation shell of Mg2+ is replaced by O2•– or CO2•–.

    Magnesium is an electrolyte responsible for keeping potassium inside and sodium outside of the cell. Magnesium is found in abundance inside ATP cells (the body's energy cells) and is also involved with the contraction of muscle, nerve conduction and helps with cell division and repair. http://physicaldimensionsihg.com/the-importance-of-electrolytes-and-hydration Potassium is involved with the acid-base regulation keeping potassium levels regulated will help to buffer the lactic acid build up in muscle tissue.

    Mg2+ transport proteins to eukaryotes and across the cell membrane. The CorA family of magnesium transporters is the primary Mg2+ uptake system of most prokaryotes https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836678/

    ND Hauf, Racheal and JanSz like this.
  2. Even though @Jack Kruse did not answer nor address this subject on this thread, he did make a post: https://optimalklubs.com/cpc-51-why-clotting-chronic-fatigue-are-tied-to-covid/

    "Magnesium in a cell is a hydrophilic element on the periodic table, and without water, we lose intracellular Magnesium (Mg). 56 enzymes in mitochondria use Mg2+ as a cofactor. It turns out making melatonin is a Magnesium and water-dependent process. Making Vitamin D is also water and Mg dependent. There are 3 metabolic transactions from Cholesterol (Cholecalciferol) that occur under the surface of the skin where our “storage version” of Vitamin D (Calcidiol) is made. This 25(OH) version of D3 gets transformed in our kidneys and liver to the “active version” of Vitamin D (Calcitriol or 1,2,5 (OH) in the liver. All 3 reactions require Mg2+ as a cofactor. Mg, however, needs the mitochondria to make cell water in the cell to work properly. If the mitochondria do not make water, taking an Mg supplement is a waste of time and resources. It is physiologically impossible to have a 25(OH) blood test (“Storage-D”) to be less than 35 ng/dl and a Magnesium RBC level to be above 6.5mg/dL because of the negative feedback loops tied to calcium levels in our blood!"

    "As a result, this is why melatonin levels are off in these patients. With time this ruins their sleep because melatonin forms another coupled cycle with cortisol and adenosine. This is why Magnesium and Vitamin D deficits walk together in mitochondrial damaged patients. This is why COVID people get the side effects they get. Some kids with COVID have enough redox power to avoid clotting but they get chronic fatigue instead. It will not change until their redox power is returned by changing the environment they are in. If this is allowed to persist chronically it is only a matter of time that clotting will occur or that will develop another chronic mitochondrial disease, like cancers. I think this is why Oz is loaded with melanoma."

    So what's my point of this thread -> I believe we need to first understand cellular hydration both externally to the phospholipid biliary within the phospholipid biliary and within the cytoplasm.

    Concerning hydration, @Jack Kruse goes onto say, "A modern diet with undiagnosed high O6/O3 ratio due to seed oil usage with the use of carbohydrates out of season which also causes dehydration. One mole of fat creates 100-110 nmol of water. One mole of carbs produces 55 nmol of water in the mitochondria. Carbohydrates also contain more deuterium, and deuterium main function in the body when it gets into the mitochondrial matrix is to decrease the piezoelectric ability of the mitochondrial via the increased kinetic isotope effect. It makes the mitochondria act more like a diamond, and less like quartz. A diamond carbon lattice is not compressible, while the SiO2 lattice of quartz is. This is why quartz is piezoelectric and why a diamond aren’t. This is why Nature only creates carbs in strong light cycles when the sun can offset the lack of metabolic water production from the sun in mitochondria at cytochrome c oxidase."
    Last edited: Feb 17, 2021
    ND Hauf, Racheal and JanSz like this.
  3. The structure and regulation of magnesium selective ion channels - https://www.sciencedirect.com/science/article/pii/S0005273613002794
    • Cellular Mg2 + homeostasis is essential for life but the underlying structural mechanisms are only poorly understood.
    • Prokaryotic Mg2 + channels of known structure represent model systems of their eukaryotic homologues.
    • The MgtE and CorA Mg2 + channels are regulated by the free intracellular Mg2 + concentration.
    • Mg2 + channels are relevant to human disease conditions including multi-drug resistant cancer and bacterial pathogenes
    MgtE and CorA are unique among known membrane protein structures, each revealing a novel protein fold containing distinct arrangements of ten transmembrane-spanning α-helices. Structural and functional analyses have established that Mg2 +-selectivity in MgtE and CorA occurs through distinct mechanisms. Conserved acidic side-chains appear to form the selectivity filter in MgtE, whereas conserved asparagines coordinate hydrated Mg2 +-ions within the selectivity filter of CorA. Common structural themes have also emerged whereby MgtE and CorA sense and respond to physiologically relevant, intracellular Mg2 +-levels through dedicated regulatory domains. Within these domains, multiple primary and secondary Mg2 +-binding sites serve to staple these ion channels into their respective closed conformations, implying that Mg2 +-transport is well guarded and very tightly regulated. The MgtE and CorA proteins represent valuable structural templates to better understand the related eukaryotic SLC41 and Mrs2–Alr1 magnesium channels.

    As a structural co-factor, Mg2 + stabilizes the ribosome, lipid membranes, and nucleic acids. Mg2 + further serves as a pivotal component in metabolic networks and signaling cascades where it participates in regulating enzyme activity and targeting macromolecules to specific complexes or cellular locations. Less appreciated roles for Mg2 + include competition with Ca2 + for key intracellular binding sites.


    Ion selectivity and conductance - CorA is a conduct hydrate version of its charge-dense Mg2 + substrate,

    • creating a Mg2+ circuit.
    Note: the double helix pattern
    ND Hauf, Racheal and JanSz like this.
  4. Towards an understanding of the propensity for crystalline hydrate formation by molecular compounds - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5094445/

    Using Nuclear Magnetic Resonance (NMR) spectra we are gaining an understanding of “new” compounds.

    Previously unreported structures are denoted as ‘New’. The stoichiometry of water in hydrated structures is given in parentheses.

    Electrostatic potential maps and/or analysis of the crystal packing in an hydrate structures was used to rationalize why certain molecules did not readily form hydrates.


    (a, b) Multiple C—H⋯N (green) and/or C—H⋯π (yellow) intermolecular interactions exist in the crystal structures of compounds 2 and 3. (c) O—H⋯O and O—H⋯N hydrogen bonds (blue), and π–π stacking (face-to-face) interactions (yellow) are observed in the crystal structure of 10·2H2O.

    Ok so what's to point? ->

    In Dr. @Jack Kruse lastest post on Facebook Kruse Longevity Center ->
    Growth is necessary for the eye for wellness (dopamine and melatonin), but it is always stimulated by damage (ROS) initiated by certain light frequencies (blue) that create specific free radicals in the mitochondria. The damage is designed to be limited by regeneration programs/frequencies (red) powered by the free radicals. The light stimulus frequency is what releases AA and DHA from the photoreceptors in the eyes. These two lipids give their directions to the biogenic amines made within the eye by molecular resonance phenomena. The principle of molecular resonance is easy to understand. Light is an oscillatory wave from the outside and the chemicals in the photoreceptors are the inner oscillators. Mitochondria in the RPE can also be thought of as inner oscillators in this wireless system. To get a wireless resonance to operate we need the light oscillation to equal the inner oscillator’s absorbance spectrum. When this occurs this leads to wireless resonance between sunlight frequencies and the hydrated photoreceptors. The resonance is capable of vibratory oscillations that move the molecular parts in the photoreceptors. Since light is an electromagnetic wave it is propagating radiation that can cause both chemical oscillation and a photochemical oscillation in the retina. Codons that make proteins have a degenerate code, and this code allows for proteins that appear the same to have different oscillatory resonance and this is how variable solar frequency can control the day-night changes in proteins of the eye and skin.
    Those photochemical oscillations appear to interact by resonance communication with the mitochondria in the RPE to control the short loop of AA and DHA (SN-2) recycling that occurs in the photoreceptors. This resonance is specific to the RPE absorbance spectra. It turns out aromatic amino acids also have a specific absorbance spectrum in the UV range and purple light oscillation can control those amino acids to make the biogenic amines in the eye. Those two biogenic amines are dopamine and melatonin. They both contain aromatic amino acids that absorb UV light 260-289nm that leaks into the eye in small quantities.

    May I underscore his statement above -> "hydrated photoreceptors" => light -> organic-crystalline-water-structure <- magnetism

    Perhaps our question(s) should move towards a better understanding of the hydration shell of Magnesium <- which is paramagnetic... now why might that be an important quality?

    Attached Files:

    Last edited: Mar 29, 2021
  5. Racheal

    Racheal Silver

    holy shit!!!! :eek::eek::eek:

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