REDOX is linked to RBC's circadian clocks........just as my Patreon series has shown.

Circadian clocks are fundamentally important for coordinated physiology. Current models of the clockwork in eukaryotic cells are based on transcription-translation feedback loops.

The 2017 Nobel prize in medicine was awarded for research on these feedback loops. Non-transcriptional mechanisms in the clockwork have been difficult to study in mammalian systems in research for many reasons. Improper light controls is one reason.

This research group developed novel assays using (RBCs), which have no nucleus (or DNA), and therefore cannot perform transcription.

The results of the paper showed - transcription is not required for circadian oscillations in humans - and that non-transcriptional events appear sufficient to sustain cellular circadian rhythms.

Peroxiredoxins in RBCs, undergo ~24 hour redox cycles, which persist for many days under constant conditions (i.e. in the absence of external cues).

Moreover, these rhythms are entrainable (i.e. tunable by environmental stimuli, light, food), and temperature-compensated, both key features of circadian rhythms. By demonstrating these oscillations with a number of cytoplasmic redox parameters that are common to nucleated and non-nucleated cells. The group has seemed to have uncovered interconnectivity between distinct cytoplasmic (DDW metabolic) and nuclear circadian processes. It is clear they do not have the mechanism link to metabolic water fully dialed in.

Here is how it links:

Here are the scientific facts we know to be true today: Water makes up 99% of molecules in every cell. Water is a very small molecule that has more hydrogen bonds in it than any other compound. Liquid water contains the densest hydrogen bonding of any solvent, with almost as many hydrogen bonds as there are covalent bonds in its structure found anywhere on Earth. Water's hydrogen bond network changes at a pico and femtosecond level in any environment. Inside a cell, its atomic arrangement is controlled by electrostatic forces in a cell created by the redox power of the mitochondria in that cell. These hydrogen bonds can rapidly rearrange in response to changing conditions and environments (for example, solutes like K+ in a cell).

This is why small atomic radius atoms like K+ change what water in a cell can do inside our cell membranes. The water inside a cell is not like the water humans sell. Water in a cell is an electromagnetic capacitor for sunlight because of how sunlight alters the hydrogen bonds in water. The most common small cation in a cell is K+. K+ has massive effects on the water made inside a mitochondrion at cytochrome c oxidase which sits right before the ATPase. What does sunlight do to these hydrogen bonds inside cells with respect to K+ concentration? The addition of the small atomic radius of K+ makes water liquid crystalline inside the cell. This means its physical, electronic, and refractive index varies. What is the stoichiometry of K+ to water in mitochondria that is working fine between -300mV to -400Mv redox state?

Experiments by Ling have shown that each molecule of ATP in a cell controls 8,800 water molecule binding sites and 20 potassium ions to allow water to become structured inside every cell of your body. As redox varies so does the K+ concentration and # of water molecules created by mitochondria. Melatonin, NAD+, CO2 all vary in the same way as potassium does to redox power inside a cell. Environments change redox power by varying the charge density of the hydrogen bonds in water that mitochondria create.


The transcription of clock genes is sensitive to metabolic and electronic changes in water production in mitochondrial reduction and oxidation (redox) reactions; however, circadian cycles in protein oxidation have been reported in anucleate cells, where no transcription occurs. RBC's are such a cell and act as a light ferry to the mitochondria. The change in hydrogen bonds is the key to the mysteries of life.



These are the transcription and translation feedback loops in mammals, in contrast, the above research is deepening the picture by stating that you can get these circadian rhythms without involving DNA transcription/translation. In reality, these two systems work together and if I would have to guess the non-transcriptional cues are based on redox potential within the cell and a number of other epigenetic stimuli.

This shows you just how critical redox potential of -400mV is inside of a cell.

REDOX 101 LESSON: The last 30 minutes of this video has a ton of information about redox power in cell biology. The topic of this podcast was fluoride but a lot of the information was linked to mitochondrial redox power loss.


For example:
1. As redox drops the net negative charge in a cell drops and water creation in the mitochondrial matrix drops. Fluoride lowers your redox power because it destroys the dielectric constant of water inside of you. DHA has a massive pi electron cloud. Electrons are excited by sunlight photons. DHA's electron density is lost and this is why the cell can no longer store light energy in an illness state. As a result of these sequential changes, when a net negative charge is lost the hydrogen isotope type becomes like a catalytic controller for succinate and fumarate in the TCA cycle. Light hydrogen builds the right water from TCAP metabolism. When the net negative charge in a cell is lost, water has a higher deuterium content in it. This increases the atomic mass of water and it hinders proton tunneling in enzymes and between DNA and water that surrounds it. Nature requires that hydrogen proton flow in cell water must be made of light hydrogen isotope if the cycle is to move forward to reduce oxygen. Deuterium slows the proton flow via its higher kinetic isotope effect in cell water. As a consequence, fluoride use also slows the cyclic rate of the TCA cycle which is why redox power is lost.

2. Deuterium's isotope effect causes DNA to be a more heavy and more sticky mess because the deuterium content increases bonding energies between atoms. This is a huge deal in enzymes. Enzymes are catalysts that speed things up in cells by facilitating atomic motions. DNA needs parts of it to be deuterium free for faster action and there are other places where deuterium is useful in the DNA backbone to stop enzymes from copying the nuclear code. Deuterium will not let go of enzymes to do their job in the matrix!!!! This means we lose the ability to recycle DDW water!!

It also means that all cell membranes inside the cell and organelles are going to be loaded with deuterium too. They become quite sticky as a result. This affects the lipid rafts where DHA controls the lipid cytosocial architecture in how they operate with incident light frequencies. Why? NADPH is also the main reducing element in making cell membrane fats!!!!!

The deuterium content ruins optical signaling with ELF-UV because deuterium massively increases bonding energies anywhere it is located in a CELL!!!!! So you might begin to see why limiting proton motions is a BIG DEAL in a cell!

3. It also explains why cancer states are associated with more ELF-UV light release when our deuterium fractions are up. More deuterium = more mass = more light energy is needed to break bonds to move things fast inside a cell. The cell knows it needs more light power to overcome the bonding strength of deuterium in the cell membranes. This is why sick eukaryotic cells release more light in disease states. Deuterium also makes chromatin sticky because of its high kinetic isotope effect and it blocks the normal functioning of unwinding DNA for coding and protein translation. It ruins everything a cell needs to do in run through the cell cycle. This is why the growth switch stays ON and why some forms of cancer are more likely to manifest.

4. So how does deuterium get into DNA? When your circadian mechanism is broken fluoride can cause way more damage. Fluoride competes with oxygen due to its high electronegativity. It effectively steals electrons from oxygen. Electrons are excited by photons. With fewer electrons available less light energy can be stored inside a cell = poor redox power. This lowers mitochondrial respiration which lowers the amount of water a mitochondrion can make. hypoxia = a lack of oxygen. This stimulates HIF 1- alpha. HIF 1- alpha is an analog of the PER2 clock gene in mammals. When oxygen drops, cells stop using protons from TCA intermediates for their hydrogen source for fats and water that they create.

5. Cells also stop using TCA for hydrogen harvesting when they have to use the serine oxidation glycine cleavage system. The serine glycine cleavage system is a backup system for H+ harvesting. It is made up of an H-protein, a protein that carries the amino-methyl intermediate and then hydrogen through the prosthetic lipoyl moiety, and an L-protein, a common lipo-amide dehydrogenase-like lignoceric acid. Lignoceric acid is a fatty acid that makes up the lipid rafts of all eukaryotic cell membranes including the nuclear membrane. It controls the size and shape of the nuclear membranes!!!! Dysfunction at this level leads to chromosomal problems at mitosis because they are more sticky and we get something called aneuploidy. This is a precancerous step in a cell. And here we are back to the link to size and thermodynamics. Anything that is getting larger in the universe is losing energy. Things that can maintain their size and shape are doing so because they are controlling the arrangement of atoms in cells to store energy.

6. Enzymes speed up chemical reactions in organisms by a factor of 10^10 to 10^23, but they cannot do it without water made in the mitochondria matrix. They need light hydrogen protons to pull them off because they move rapidly and do not have a high kinetic isotope effect.

Most people do not realize that a lack of water/dehydration ruins enzyme kinetics in cells (TCA cycle). They also fail to realize that the mitochondrial matrix creates a special type of water that works ideally with enzymes. The water is created by sunlight. Sunlight has a specific prescription to make the right type of water. Most other EMFs outside the visible spectrum do not allow mitochondria to create cell water.

In fact, blue light and Xrays, for example, dehydrate cells. So EMFs are not all created equal when it comes to water. These nuances with EMFs and water are still hardly recognized in the conventional centralized biochemical community.


When it moves the other way, bad things called diseases manifest. Why is light hydrogen critical in biology? Hydrogen bonds form between water molecules, giving rise to supramolecular aggregates/clusters/coherent domains. Enzyme kinetics is linked to hydrogen movements in them. They must be light hydrogen and they must be well hydrated to work because they rely on proton movements. This is how polymorphisms (SNPs) really are altered in us. The clustering of water leads to a cooperative phenomenon, which means that forming one hydrogen immediately favors the formation of several other hydrogen bonds, and vice versa, breaking one bond leads to breaking up a whole cluster. Thus clusters are dynamic flickering networks with lifetimes of 10^- 11 to 10^-10 seconds. Sunlight changes those hydrogen bonding networks by moving charges around at very rapid rates. When the rate slows entropy in the cell rises and diseases result.

The cellular organization is the key to precision optical signaling. Life is all about optimizing AMO physics INSIDE OF CELLS. It transforms energy from the environment to do this. Modern quantum biology has experimentally proven that energy is trapped directly at the electronic level in cells. Energy is stored not only as vibrational and electronic bond energies in biochemicals, but also in the structure of the system: its enzyme kinetics, membranes, and in gradients, fields and flow patterns, compartments, organelles, cell water, and tissues. All this in turn enables organisms to mobilize their energies coherently at any time it is needed and hence make available the entire spectrum of stored energies for physiological work. It is energy on demand by atomic design.

CITES:

https://www.ncbi.nlm.nih.gov/pubmed/21270888

 

Peroxiredoxins are heme proteins and subject to retinal destruction due to melanopsin dysfunction. The physiological importance of peroxiredoxins is illustrated by their relative abundance. They are one of the most abundant proteins in erythrocytes after hemoglobin is peroxiredoxin. They are a ubiquitous family of antioxidant enzymes that control cytokine-induced peroxide levels and thereby mediate signal transduction in mammalian cells.

I hope you recall that cytochrome 2, 3, and 4 make hydrogen peroxide free radicals that are critically related to peroxiredoxins. Recall H202 is quenched by catalase. Catalase is another heme related protein subject to retinal destruction.

Peroxiredoxins can be regulated by phosphorylation, redox status such as sulfonation, acetylation, nitration, truncation and oligomerization states. All of these are affected by the light environment of the animal in question.

How does this relate to my November 2018 webinar for 5G therapy ideas? The picture below is a big clue for the Black Swan clinician why Nov 2018 is huge........



When you realize how to reduce these cysteine residues you can make a huge impact on these non-linear signals in RBC's to restore the ability to transfer information from light to increase the OAM of proteins in this circadian mechanism in RBC's. This is why parabiosis studies all favor young animals blood and modern medicine remains impotent to explain it.

These enzymes share the same basic catalytic mechanism, in which a redox-active cysteine (the peroxidatic cysteine) in the active site is oxidized to a sulfenic acid by the peroxide substrate. Cysteine becomes afunctional when it is oxidized and it turns out this is a big issue in the methionine cycle.

See my comments below in this thread about methionine as a TIME CRYSTAL for your blood.

The recycling of the sulfenic acid back to a thiol is what distinguishes the three enzyme classes. 2-Cys peroxiredoxins are reduced by thiols such as thioredoxins, thioredoxin-like proteins, and glutathione, while the 1-Cys enzymes are reduced by ascorbic acid and or glutathione in the presence of GST-π. This can be augmented with DDW by clinicians who understand the mechanisms in the November 2018 webinar.

 

So when non-solar EMF impacts RBC's what does this do to RBC's that are floating in 93% water?

How much do you know about the water your colony of mitochondria creates from metabolism? Do your medical experts know this? How does deuterium water fit this story? If they don't know why are they your expert? If not why are you letting them pack your parachute for Optimal wellness? #mitochondriacwisdom #5G #nnEMF #Hacking5Gwithwater

https://forum.jackkruse.com/index.php?threads/water-sunlight-redox.22760/

 

Rhythmic potassium transport regulates the circadian clock in human red blood cells.
https://www.ncbi.nlm.nih.gov/pubmed/29215003
"Because RBCs constitute the most abundant cell type in the human body, and have a vital function, it will be important to establish the physiological significance of circadian regulation of RBC ion transport, and whether its disruption has any pathophysiological consequence. For example, RBCs play an essential role in transporting CO2 from tissues to the lungs, which in turn is dependent upon the activity of the Band 3 bicarbonate transporter (SLC4A1) whose activity is sensitive to membrane potential37. It should now be tested whether circadian regulation of RBC membrane physiology affects RBC CO2-carrying potential. Likewise, circadian rhythms in RBCs may be an unexplored factor contributing to the strong diurnal pattern to the onset of myocardial infarction and other adverse events of the cardiovascular system"

 

What is the link of potassium to sunlight?

PHOSPHORYLATION is the answer.

Remember that tyrosine is an aromatic amino acid that absorbs photons from 200-400 nm. This makes those aromatic rings a PLAYGROUND for solar photons. This assumes you live in such a playground. Now if your light choice eliminates the possibility of this playground it is your choices that hinder your recovery.

Recruitment of hepatocyte nuclear factor 4 into specific intranuclear compartments depends on tyrosine phosphorylation that affects its DNA-binding and transactivation potential.

 

So what is the link from plants to animals about phosphorylation?

Plants use phosphorus to complete photosynthesis and animals use phosphorus to augment their many versions of photosynthesis.

Plants use chlorophyll to do it. We use hemoglobin in our RBC's to do it.


C3 plants use C3 photosynthesis which uses CO2 in a 3-carbon compound and C4 plants use C4 photosynthesis which incorporates the CO2 in a 4-carbon compound.

C3 plants like cooler weather and C4 plants like stronger light. 85% of plants are C3 types on EARTH.

These compounds represent different types of sugar that are made photoelectrically from the joining of CO2 and water with sunlight. Photosynthesis is the process of combining light and nutrients of the soil to create energy plants can use.

C3 and C4 photosynthesis go about this process differently. Most plants are C3 types. The advantage with C3 photosynthesis is that it is more efficient than the C4 variety under NORMAL solar light conditions since it requires FEWER enzymatic STEPS.

Does this mean living things more more protective steps when ABNORMAL light is used to drive biochemical kinetics? YEP.

C3 plants use C2. Carbon Dioxide is used to create the 3-carbon compound G3P in order to produce usable energy.

The higher CO2 concentration in C4 plants means that the stomata (water region), the gas exchange part of the plant, do not need to open up to get any more, so less water is lost. CO2 tensions are QUANTIZED to water concentrations in plants.

Does this mean that in animals that make this quantum gas that the amount of CO2 is somehow linked to the amount of water made in a mitochondria? Yes it does. This is why keeping your RBC's light ferries in its youngest state is paramount in being healthy. Young blood provides for better animal photosynthesis in all species.

C4 plants uses CO2 to create the 4-carbon compound oxaloacetate instead. C4 plants tend to do better in HIGHER oxygen environments. These environments are newer on evolutionation timescales for the photosynhesitc reactions. Does this imply that the Earth's climate when photosynthesis was innovated was radically different than it is today? Yes, it does.

C4 plants also go through photosynthesis more rapidly than C3 plants when there is a lot of light and heat nearby. Does this mean when CO2 rises evolution and all food webs will favor C4 plants? Yes, it does. So having C4 plants in your environment when C02 and nnEMF is probably a wise thing to do.

Additionally, C4 plants have much better water efficient uses than the C3 variety since they don’t have to keep their stomata open as much. They are better at conservation of the precious resource than C3. This is also why these plant sources will be dominant in times when C02 and nnEMF rise for creation of new food webs when the surface of the Earth is being varied by any force that alters the quantum balance.

There are several thousand different types of C4 species with 19 different plant families. Examples include corn, saltbush and many plants that thrive during the summer months.

WHAT IS THE LINK TO PHOSPHORUS BY WAY OF POTASSIUM?

Gilbert Ling was the first to see the link of ATP and potassium in animals. You migth want to go back and re-read Quantum biology 10 for that story. When you eat a more ketogenic template you make more ATP to maximally unfold proteins. This is based upon the ability of one mole of glucose only making 36 ATP vs 147 ATP from the beta oxidation of fats. ATP’s main function in a zero entropy quantum cell, opens protein conformational structure to expose more water binding sites in proteins. When this occurs POPERLY UNDER SOLAR LIGHT STIMULUS the amount of ATP is stochastically linked to potassium concentration inside the cell.

This is why potassium is found inside all cells and sodium is not. Sodium exclusion is not due to a membrane pump as most biochemistry books say it is. Gilbert Ling was the first biologists to say this and then proved this mathematically and experimentally close to 50 years ago. No one seems to know why this man was brilliant.

The only reason his work was not accepted was because biology does not realize that energy in cells is generated by semiconduction of charged particles that are separated from water. Becker’s proof on Ling’s conceptual framework did not come until 9 years after Ling showed why K+ (potassium) and Na+ (sodium) are included and excluded because they are BOTH linked to the semiconducting currents found inside cells WHEN THEY ARE energized by sunlight as their stimulus. This has been further proven in the molecular actions of rhodopsin, melanopsin in the skin/retina, and actin and myosin in muscle by Gerald Pollack, all using photon semiconduction. These semiconductive phenomena are WHAT DRIVE topologic variation in us.

ADP is an organic compound that is essential for the transfer of energy during photosynthesis. ADP is composed of a five carbon atom compound known as ribose, one adenosine molecule, and two phosphate groups. It is formed by removing one phosphate from adenosine triphosphate, ATP.
The energy needed for photosynthesis is obtained from sunlight. Plants store this energy in the form of ATP and then use it to carry out photosynthesis. Photosynthesis takes place in two distinct stages, the light stage and dark stage. The light stage is the light-dependent stage of photosynthesis, which occurs in the thylakoid membranes of the chloroplast. During this stage, white light is absorbed by the pigments in the chloroplast to form high-energy compounds, such as ATP and Nicotinamide Adenine Dinucleotide Phosphate, NADPH. In order to produce the energy required to drive chemical reactions in photosynthesis, ATP loses one phosphate to become ADP, and the NADPH loses one electron to become NADP+. Phosphorus also is key in animal photosynthesis and make H+ from the water made in mitochondrial matrix which is deuterium depleted.

H+ AND TOPOLOGY

Hydrogen without its sole electron is a metal plasma and as a result it becomes an excellent electrical conductor. When hydrogen loses its electron it becomes smaller. This is a shift in its topology and topologic changes always imply size and shape changes in things made from matter.

This iso-form of hydrogen is buried in our sun and in our mitochondria. This makes it my focus on how quantum electrodynamic theory is being used both in the sun and mitochondria. It also means the force carrier between both things is being controlled wirelessly by the solar plasma. This is functional how photosynthesis forms the food web and explains the REAL reason food is necessary. This means our mitochondria is filled with ionized plasma. Inside of every mitochondrion resides a small electric universe that powers a cell and makes life work. This is very similar to what the sun does when it “burns” hydrogen. Burning plasma may actually be the wrong term for UNDERSTANDING this process.

When we remove an electron we shrink hydrogen to a metal plasma. Hydrogen is transformed into a tighter, more compressed package because this gives hydrogen plasma a more favorable thermodynamic profile because less space equals more dielectric capacitance, from an electrical standpoint. This makes the metal plasma of hydrogen, itself, a chameleon for electrical action.

It is an electrical phenomenon of QED theory. Hydrogen can be non-metal when it has its electron; It is also an acid, and a proton, and can act as a superconductor. It interacts with water to do some unnatural things because of its ability to proton tunnel. When we add infrared light it becomes quite special. With 1538.5 nm photon frequency added to cell water, proton transfers in water are increased dramatically. Sunlight red light spectra goes from 600-3100nm light. 1538.5 is rght in the middle of this range. Proton transfers is synonmous with proton tunneling reactions and this occurs in ALL ENZYMES. Could this be why certain reactions need LESS ENZYMATIC control on things that use photosynthesis on EARTH?

Did you know every biologic enzyme known to man uses proton tunneling to work? Have your food guru’s told you that? Is this why glucose metabolism inside of you takes so many enzymes to operate? Mitochondrial input is made in electrons FROM foods. All food break down into electrons and protons that get fed into electron chain transport in mitochondria. The process is different at different spots in electron chain cytochromes. Could this be tied to the electromagnetic footprint of how the food was made by sunlight? YEP.

BACK TO PLANTS SINCE THEY MAKE ALL FOODS

During the dark stage, the energy-depleted compounds, ADP and NADP+ are converted back to high-energy forms, ATP and NADPH respectively. These high chemical compounds are then stored to drive other chemical reactions necessary for the synthesis of sugar and other carbon-containing compounds. ATP is also used in the oxidation of photosynthetically-produced carbohydrates in the mitochondria during cellular respiration. This can be made with food electrons or with red light alone.

In plants what differs in the their blood system?

Remember chlorophyl and hemoglobin are very closely aligned with light as the picture shows.
Leaves and red blood cells both have a protein in them that is a porphyrin. Both proteins share a very common atomic structure. Porphyrins are light absorbers.

WHAT ARE THE IMPLICATIONS?

There are several different types of chlorophyll including chlorophyll a, chlorophyll b, chlorophyll c, chlorophyll d, chlorophyll e and bacterio-chlorophyll. The various types of chlorophyll are found in different organisms and are all involved in photosynthesis. Chlorophyll is an important pigment in the process of photosynthesis and is found in all photosynthetic organisms including plants, blue-green algae and eukaryotic algae. It is a photoreceptor that is found in the chloroplasts of green plants. Chlorophyl uses in plants varies as light varies from the sun.

Chlorophyll a and chlorophyll b are the two major types of chlorophyll and differ only in the composition of one of their structural sidechains. Chlorophyll a is the most prevalent type of chlorophyll. It is found in plants, algae and other aquatic organisms. This type of chlorophyll absorbs red, blue and violet wavelengths. It gets its color by reflecting green, thus giving plants their green color. GREEN LIGHT IS NOT FAVORED BY PLANTS AT ALL HENCE WHY THEY REFLECT THE COLOR.

Chlorophyll b is found primarily in plants as well, but this type absorbs blue light only and is yellow in pigment. Chlorophyll c and chlorophyll d are less common and are found in different algae. Chlorophyll e is a very rare type of chlorophyll that is found in some golden algae, and, as the name suggests, bacterio-chlorophyll is found in certain bacteria.

Chlorophyll A likes and USES UV light a lot more than chlorophyll B does. Does this mean plants blood varies as their location on Earth varies? Yes it does. Is this why mitochondrial haplotypes also vary? Yes it does.

Chlorophyll and hemoglobin are topologic insulators that collect light and make it obey relativity once the light collides with this protein. Physics is experience, arranged in economical order for proteins. Biology is present wisdom, re-arranged constantly by locally by geometry with geologic time order. The Earth’s environment used to provide enough to satisfy every person’s needs. This is no longer true because of man’s interference by using other frequencies of light. Your environment is never static so neither should your mito-hacks or your beliefs be. We are built to be non-linear beings being able to harvest Earth’s linear seasonal environments with their ever-changing solar light frequencies. Now, Earth’s environment is non-linear on a second to second basis because of light switches and the electric power grid. Man’s mitochondria are currently engrossed in a constant state of adaptation trying to stave off acute decay to survive. So far our species is losing this battle of attrition. Light does not have to obey relativity. Its speed is constant everywhere it can run free. It cannot run free in living systems.

Topologic insulators are trappers and transformers of light from the sun in cells. When it gets trapped in these topologic insulators, for the first time, the speed of light becomes relative to tissue density and this alters the optics within proteins. Therefore, trapped sunlight in proteins makes our surfaces relative, and that relativity changes the space/time of our cells and tissues. This happens at our surfaces in the eye, skin, gut, and lung as mentioned in my MANY webinar.

Sunlight shifts blood into the skin by changing polarization in tissues that allow for dermal pooling due to molecular resonance changes in eNOS and NO. More than 50% of your blood volume can change your skin surface when specific solar spectral density is present.

This can lower your blood pressure and it raises you sulfated vitamin D3. It changes the anatomical structure of the skin by changing the optics of surfaces. It becomes a sensory stimulus for the interoceptive system to induce biochemical substrates via photosynthesis in plants and changes in the ATPase using red light and water in animals.

ANIMALS ARE PHOTOSYNTHETIC. I had a skeptic in Mexico (2019 event) at my table during a breakfast conversation who needs to read this thread. Sunlight increases sulfated Vitamin D3, histamine, and sulfhydryl groups while lowering (photolysis) adrenaline, steroids, testosterone, estrogen, thyroid hormone, DNA, and RNA.

Sunlight is capable of inducing biochemical reactions via photolysis and it induces coordinated endocrine adaptation effects in the eye and the skin surfaces. It affects the sympathetic and parasympathetic systems in the brain by way of the central retinal pathways. The varying AM solar light is the key stimulus for the circadian timing mechanism of the body clock via the central retinal pathways. All these effects are built into the electronics of your proteins under solar power and magnetic flux.

This is why uncoupled mammals will do way better in places like Mexico..........

 

The take home here? Potassium and ATP are linked deeply to light and this is why the quality of your blood links to sunlight. Keeping your blood young is the basis of every parabiosis study ever done and everyone seems oblivious to it.

Potassium (K+) signaling goes awry in an environment loaded with nnEMF. What are the implications? When K+ goes awry so does your cellular redox potential and so does your mitochondrial heteroplasmy rates in tissues affected by this. Potassium levels tell us about the relationships to cellular ATP made by mitochondria. In this way, they are like CO2 and water levels in cells because mitochondrial ox/phos makes CO2 and water as their normal exhaust products since the reverse photosynthesis. K+ stoichiometry:

For every 0.3 mEq below 3.8 mEq that potassium is on a standard blood lab draw, means there is 100 mEq deficit inside a cell. The atomic size and its redox potential are huge for potassium's ability to “gluing water” for it to function as the optimal electrical adapter to transfer energy throughout the cell coherently. THAT WATER MUST BE MADE BY METABOLISM OF FOODS. We make 110 gms of water from fat burning of 100 gms of fat while only making 55 Gms of water from burning of glucose. So this is why beta-oxidation creates a longer life.


ATP is designed to unfold proteins fully to open their carbonyl and imino side chain groups on all amino acids to intracellular water. This action allows binding and polarization to separate water into subatomic particles that are positively and negatively charged. This action is called building or expanding the exclusion zone (EZ) of water using sunlight as the KEY stimulus.


Expanding the exclusion zone allows water to form polarized layers around the hydrophilic proteins, and the earth’s magnetic field then orients these polarized liquid crystals by a principle called “spintronics.” Controlling the electron spin at a right angle to the direction of flow of electrons allows for the formation of massive superconducting proton cables all over your body. This is why sleeping on a magnetic pad at certain times might be a smart move when you understand the context of your redox potential.

“Spintronics” was FIRST described in the February 2014 webinar for members. In 2016 the Nobel prize was given for it, and now in 2019 it has become the holy grail of quantum computation.

Varying sunlight changes water networks. This gives us alternating positive and negative magnetic dipoles of water molecules that have their electrons locked in at 90-degree angles to the current of flow around these proteins. In this way, the magnetic field can control the action of water and collagen where they meet, both inside and outside of cells. Gilbert Ling found that the orientation of positive to negative water molecule binding was 3.1 Angstroms apart when these conditions are met. Do we know that sunlight frequencies vary the size and shape of the EZ in 2019? YEP.


You must pay attention to your Potassium (K+) levels in a varying nnEMF world. The reason potassium is critical inside a cell and supersedes magnesium and sodium ion concentration is that it is naturally tied to beta and gamma carboxyl side chain groups found in proteins, where potassium specifically binds because of “quantum advantages.” These beta and gamma carboxyl bonds allow K+ to ADSORB to this protein site and donate electrons (this is why K+ has the second highest redox potential to Lithium in life; to the polarized water gel crystal.

Each molecule of ATP in a cell controls 8,800 water molecule binding sites and 20 potassium ions to make this liquid crystalline semiconductor inside every cell of your body. Potassium acts like “the glue” to keep your protein backbone and water in a gel state inside your cell to maintain the semiconducting plates together in a cohesive form. This is why K+ is critical in setting the redox potential of water in a cell. In this way, you are building a special type of semiconductor that forms “the fourth phase of matter” and can act like a “topologic insulator.”(TI) A ‘TI’ allows quantum effects to happen in warm wet environments.

CITES:

https://arxiv.org/abs/1508.06135

Insulators normally do not conduct electrons and are considered non-conductors, but topological insulators are a special form of matter that life appears to use to its advantage because of some quirky quantum principles it has. It appears it can conduct proton currents below the water surface within a cell, which makes it quite special for living things. The action at water and collagen surface is where the quantum dance of life begins.

This helps explain why the DC current of regeneration Dr. Robert O. Becker was found on the surface of water and proteins. Sunlight is the key to the connection. He found that the DC current went away at night time when the sun was not shining. This tells us that we have a deep wireless connection with the ball of gas in the sky. K+ is key to that wireless connection. It is not found deep within a cell. In nerves, Becker found the DC current of regeneration was under the myelin layer but outside the axon. For this reason, peripheral neuropathy is a big sign of poor redox potential and poor solar exposure due to many factors like clothing glasses and creams or employment or culture. People with a poor solar connection also tend to have degenerative disc disease. Tissues need a higher redox potential to regenerate. Protein synthesis is the most expensive cost of energy a cell has. This tells us about people's ubiquitination rates are indirect measures of their % heteroplasmy in their mitochondria in these tissues.

They are all clues to the quantum clinician and wise patient on how their choices in their environment is hampering their version of reality we call life. When you constantly have to turn over protein, you are wasting huge stores of energy stored within your cells. Every time we turn over protein we have to use our methionine sources and this acts to AGE our blood and this is why homocysteine rises in the blood plasma. It is the major time crystal I use to see who has older blood than younger blood in their own environment to understand how their environment is KILLING them below their perception at the submolecular level. I gave you QT#14 Patreon to understand this. It is time you all get these concepts together to see where I am headed because nature has directed my attention there.

 

Why is the methionine cycle a proxy for your blood circadian biology? Does it tell us what our spleen does and why it is close to impossible for humans to get splenic cancer?

Why do people with methylation defect often get high homocysteine levels and heart disease? Is it their SNP's or is a lack of sun behind the risk? In the literature, there is a clear association of cardiovascular disease and methylation defects due to SNP's. Those problems directly linked to problems is NO production from our skin and arterioles below the skin and this leads to PAD, CAD, and many other problems. So is the SNP the real problem or did evolution give us the SNP because it evolved in a strong solar environment initially?



Nitric Oxide is produced as a by-product of the methylation cycle. Did you know that? Therefore, with poor methylation and a chronic lack of solar stimulus, may lead to insufficient amounts of NO may be produced to keep the endothelial lining healthy. So do we really need all these supplements for poor methylation of might the free sunlight benefit those with methylation defects? What makes NO in humans? Sun exposure on the skin releases NO from the tissues. So if you have a methylation defect you need more sun not less. This is what the functional medicine and allopathic doctors just do not get it.

 

Look at all those aromatic amino acids and methyl groups.............

 

Many members and voyeurs need this lesson too.

Mexico wisdom on display.

 

Why are so many young people getting Crohn's disease and gut cancers in a tech-driven world? Could it be related to a poor connection of light from the sun to the mitochondria via their blood plasma?

Are Omega 6's PUFA really the boogey man for disease food gurus tell you?

Nope. They remain ignorant of the circadian cycle around this story and you Black Swans have to get it right and let them keep going on their wrong path. At this point, it is becoming comical how wrong they have been for decades.

The data is piling up now how light disruption leads to a broken circadian mechanism and mtDNA destruction.

How so?

HNF4A gene product protein represses the operation of CLOCK and BMAL1, which act as key molecular cogs that drive the circadian rhythms in mammals.

Inside the cell, the cogs of the clock are universal, but the hands of the clock are specific to each organ, so how the clock does its work in each cell is different.

Jack, can you give us an example of how this protein works in humans?

This protein from the HNF4A gene also plays a pivotal role in the expression and synthesis of SHBG. SHBG is raised when this protein is not controlled by light cycles. It is an important glycoprotein made primarily in the liver, which in addition to lowering insulin-resistance also serves in reducing levels of free Estrogen as-well as prolonging the half-life of Testosterone. It also causes problems in the kidney and intestine. This protein is also associated with MODY1 diabetes. I believe it is one of the key links to melanopsin dysfunction in the guts of many people.

Jack is this why people with gut diseases like Chrohn's can get colon cancers? Is this why young people now are getting both diseases at record rates? YEP.

We now know the increased amplification of hepatocyte nuclear factor 4 alpha has been observed in colorectal cancer.

In humans, there are two isoforms of HNF4: they are HNF4α and HNF4γ, encoded by two separate genes HNF4A and HNF4G respectively.

The food gurus like to blame omega 6's like LA for diseases but too few of them seem to know about the circadian control of this mechanism by HNF4.

HNF4 was originally classified as an orphan receptor that exhibits constitutive transactivation activity apparently by being continuously bound to a variety of fatty acids like linoleic acid (LA).

The existence of a cellular ligand for HNF4 has been somewhat controversial, but linoleic acid (LA) has been identified as the endogenous ligand of native HNF4 expressed in mouse liver. It turns out the binding of LA to HNF4 is reversible and it linked to the repression of CLOCK and BMAL1. So LA in foods really has bystander effect here when the light cycles are disrupted. Once again, the food gurus turn up WRONG.

How does your internal organ clocks run? New research identifies a circadian network in the liver which is linked to diabetes and liver cancer. The liver is the key organ in the gut!!! Disruption of the circadian rhythm may be a risk factor for several age-related chronic diseases. No shocker to any clinician here.

https://www.sciencedaily.com/releases/2018/12/181211161519.htm

 

The clock mechanism breakdown in the blood and gut seem to be behind the recent surge in Crohn's disease, IBD, and gut cancers in young humans. Biophysics 101.

 

Why do people with methylation defect often get high homocysteine levels and heart disease? Is it their SNP's or is a lack of sun behind the risk? In the literature, there is a clear association of cardiovascular disease and methylation defects due to SNP's. Those problems directly linked to problems is NO production from our skin and arterioles below the skin and this leads to PAD, CAD, and many other problems. So is the SNP the real problem or did evolution give us the SNP because it evolved in a strong solar environment initially?
Nitric Oxide is produced as a by-product of the methylation cycle. Did you know that? Therefore, with poor methylation and a chronic lack of solar stimulus, may lead to insufficient amounts of NO may be produced to keep the endothelial lining healthy. So do we really need all these supplements for poor methylation of might the free sunlight benefit those with methylation defects? What makes NO in humans? Sun exposure on the skin releases NO from the tissues. In the gut, the microbiome controls NO release. Did you know that? So if you have a methylation defect you need more sun not less. What does this mean for the gut? It means you need fewer carbohydrates and more ketosis to control the light release from your microbiome to preserve the ascorbate in your mesentery to improve blood flow in your gut. This is what the functional medicine and allopathic doctors just do not get it about today's world. Black Swans do.
BH4 above is critical in the blood plasma. It is a chromophore protein that is used in the eNOS pathway of vessels. Once it is destroyed it affects microcirculation and these changes mimic the lesions we see in Crohn's pathology and many other new age gut maladies.
Why do I think it happens more in a blue-lit 5G world? When this process is broken it affects other cellular antioxidants.
eNos becomes uncoupled from NO release in the gut via the microbiome and instead of NO production to improve mesenteric flow, peroxynitrite radicals dominate and this reduces mesenteric flow and destroys apoptosis making cancer generation much more likely. Peroxynitrite is made to a far greater degree when tetrahydrobiopterin is absent (BH4). I think every gastroenterologist needs to know this today. In fact, I believe any stressor causes this process to happen but alien light does it quickest. When one eats carbohydrates during night time the effect is increased because it causes the microflora to release even more light than a prokaryote normally would and this effect is the key stimulus to making the gut cells acutely lose all of its endogenous protection. If one adds blue light or nnEMF the effect becomes logarithmic and one can develop rapid cancer progression as we lose control of ascorbate controls in the mesenteric circulation. Ketosis reduces the consumption of ascorbate and this is why it prolongs longevity in those with gut issues. It also improves gut blood flow and mimics the effect we see in parabiosis studies. When will they learn? #BlackSwanwisdomondisplay

 

This is my favorite thread so far. Thank you.

 

Ketogenic templates affect both SVCT1 and SVCT via the oxalate switch to control ascorbate levels to control catecholamines and neurotransmitter health. This is why humans lost the enzyme to make Vitamin C endogenously because they are not designed to eat like a herbivore as they migrated out of Africa to more stressful climates. It also explains why animals with L haplotypes had to adapt to even higher ketogenic diets to make heat to survive cold.

When you get cold you become ketogenic by design and you are burning your own fat to make C02 and mitochondrial water and ENDOGENOUS plasma vitamin C from oxalates. Eating vitamin C does not happen in cold climates because it does not grow in the photosynthetic web of life. It is present in many kinds of seafood. People forget we left our African crib by WATERWAYS. This is why we lost our ability to make Vitamin C. If we live on our own fat as we go we have no need for exogenous Vitamin C. corollary is if our life becomes more then cold stressed we will deplete out endogenous mechanism and as a result, our cortisol and melatonin levels drop like rocks. Today we've built a world that drains our endogenous abilities because we have more light stress. Cold stress and seasonal light stress is all nature gave us to work with as we left Africa. That is why haplotypes and SNP's and SAP's varies in humans over 200K years.

All the pieces fit when you see them working in unison in your species. This is why 24/7 ketosis is not needed too in many cases. It is if you live in a blue-lit nnEMF city. If one does this before the advent of blue light or nnEMF oxalate kidney stones were more likely. Today's world makes getting oxalate stones less likely because we are using oxalates as our storehouse for Vitamin C to fix the deficits of the PVN and adrenal stressors we've built.



Few do. Welcome to the submolecular world of the Black swan circa 2019.

 

A patient asked me recently why I am good at what I do......I thought about the question for a while and told her when people come to see me most are used to driving on single lane highways. I teach them how to drive on the Autobahn. Most people have no idea the road they are on is adaptable. The human brain is only capable of what it conceives. It can't conceive what it has never experienced. I provide that experience for my patients and tribe. I demand more of you than you do of yourself. I hate settling and you should too.


^^^^artificial light day or night destroys all these things in humans = blue light and nnEMF. Got it?

 

Leaky lymphatics causes visceral fat hypertrophy = melanopsin dysfunction in the arteries of the gut. Guess why? What happens to any tissue or anything that loses energy in the universe? They get larger by scaling laws. What happens to your ankle when it gets sprained? What happens to your heart as it fails? what happens to a star that is dying?

“the hypertrophy of mesenteric adipose tissue may result from mispatterned and ruptured lymphatic vessels. Alteration of mesenteric adipose tissue was associated with activated NF-κB signaling pathway.” How does NF-kappa beta link to this story? Melanopsin causes increases in this inflammatory signal by destroying photoreceptors in the gut. This begins in the RBC's of people with Crohn's. When will they learn it is a story of aberrant light?
https://academic.oup.com/ibdjournal/article-abstract/25/2/283/5117900

 

RBCs have the key to the BZ ascorbate puzzle. RBC Glut1 triggers dehydroascorbic acid uptake in mammals unable to synthesize vitamin C. Humans are one such animal. This is why the survival benefit exists in parabiosis studies and no one seems to realize it. This is why this was written: https://forum.jackkruse.com/index.php?threads/redox-is-linked-to-rbcs-circadian-clocks.22813/ When you look deeper you see this: Glut1 expression increases during human erythropoiesis too.

Erythropoietin (EPO)-stimulated erythropoiesis of human CD34+ progenitors resulted in the appearance of erythroid progenitors, as monitored by cell morphology. Markers used to assess the progression of erythropoiesis included glycophorin A (GPA) and the transferrin receptor CD71.

Of all cells, human erythrocytes express the highest level of the Glut1 glucose transporter. However, the regulation and function of Glut1 during erythropoiesis are not known in the literature. This is why Szent Gyorgyi and Pauling's work on Vitamin C still is relevant. The retracted Vitamin C paper I mentioned From Sir Albert contained the clues I needed to find the source of the BZ reaction that keeps RBC's in optimal shape. Without mitochondria, you need an oscillating reaction to keep the cells reduced. Recent reports published now show that glucose transport actually decreases during human erythropoiesis despite a >3-log increase in Glut1 transcripts. This is a huge clue where the pot of gold is. In contrast, Glut1-mediated transport of L-dehydroascorbic acid (DHA), an oxidized form of ascorbic acid (AA), is dramatically enhanced in human RBC's = POT OF GOLD

 

Biofactors. 2003;17(1-4):37-46.
Role of ascorbate in oxidative protein folding.
Bánhegyi G1, Csala M, Szarka A, Varsányi M, Benedetti A, Mandl J.
Author information

Abstract
Both in prokaryotic and eukaryotic cells, disulfide bond formation (oxidation and isomerization steps) are catalyzed exclusively in extracytoplasmic compartments. In eukaryotes, protein folding and disulfide bond formation are coupled processes that occur both co- and posttranslationally in the endoplasmic reticulum (ER), which is the main site of the synthesis and posttranslational modification of secretory and membrane proteins. The formation of a disulfide bond from the thiol groups of two cysteine residues requires the removal of two electrons, consequently, these bonds cannot form spontaneously; an oxidant is needed to accept the electrons. In aerobic conditions the ultimate electron acceptor is usually oxygen; however, oxygen itself is not effective in protein thiol oxidation. Therefore, a small molecular weight membrane permeable compound should be supposed for the transfer of electrons from the ER lumen. The aim of the present study was the investigation of the role of ascorbate/dehydroascorbate redox couple in oxidative folding of proteins. We demonstrated that ascorbate addition or its in situ synthesis from gulonolactone results in protein thiol (and/or glutathione; GSH) oxidation in rat liver microsomes. Since microsomal membrane is hardly permeable to ascorbate, the existence of a transport metabolon was hypothesized. Three components of the system have been described and partially characterized: (i) A microsomal metalloenzyme is responsible for ascorbate oxidation on the outer surface of the ER. Ascorbate oxidation results in ascorbate free radical and dehydroascorbate production. (ii) Facilitated diffusion of dehydroascorbate is present in microsomal vesicles. The transport is presumably mediated by a GLUT-type transporter. On the contrary, the previously hypothesized glutathione disulfide (GSSG) transport is practically absent, while GSH is transported with a moderate velocity. (iii) Protein disulfide isomerase catalyzes the reduction of dehydroascorbate in the ER lumen. Both GSH and protein thiols can be electron donors in the process. Intraluminal dehydroascorbate reduction and the consequent ascorbate accumulation strictly correlate with protein disulfide isomerase activity and protein thiol concentration. The concerted action of the three components of the system results in the intraluminal accumulation of ascorbate, protein disulfide and GSSG. In fact, intraluminal ascorbate and GSSG accumulation could be observed upon dehydroascorbate and GSH uptake. In conclusion, ascorbate is able to promote protein disulfide formation in an in vitro system. Further work is needed to justify its role in intact cellular and in vivo systems, as well as to explore the participation of other antioxidants (e.g. tocopherol, ubiquinone, and vitamin K) in the electron transfer chain responsible for oxidative protein folding in the ER.

 

WHAT MIGHT LIFE REALLY BE?

Could it be described as a "fractal optical ring resonator" that does some of the most interesting and unexpected things to light in order to build multiple quantum computers and machines throughout our cells?

What might it do to oxidized ascorbate in RBC's SVCT2 in tissues like RBC's or astrocytes supporting the PVN?


The title of the article below is "Physicists Built a Machine That Breaks the Normal Rules of Light".

The article should have read, when you change the environment light is in you uncover non-linear effects around light that life has figured out how to take advantage of for 3.8 billion years. I think physicists perspective of what they think light really is, IS THE PROBLEM today in biophysics. We do not know it all yet about light and the more we learn the better people will do in medicine that uses light as the main prescription to get people well using quantum biology.
Physicists have assumed time-reversal symmetry is how light acts in all environments. Anyone who is alive knows we cannot live our lives in reverse. This should be really solid EXPERIMENTAL proof that you do not understand all the nuances light offers on Earth or inside of human tissue. The arrow time is a reflection of how light operates in a living system when it is captured and used. This is what gives things an arrow of time.


Their first assumption stated is thus, if you were to play a tape of light's behavior forward and then backward, you would see it behave in the same way moving in both directions in time. This is called time-reversal symmetry. Outside of life do we have data that shows non-living systems can alter time reversal symmetry? If we do, this means your perspective about light and CIRCADIAN biology is DEAD WRONG.
When will they learn that cells/tissues are "fractally built optical ring resonators" that contain topologic insulators codified magnetically in DNA that must be hydrated by water made from the mitochondrial matrix to get these effects in the living state? When will they learn that the mitochondrial matrix powers these loops using sunlight?

I wonder how long it will take?

https://www.livescience.com/64490-weird-light-ring.html