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TENSEGRITY 9 is LIVE. Welcome comments here.

Discussion in 'Mitochondrial Rx' started by Jack Kruse, Nov 19, 2014.

  1. caroline

    caroline Moderator

    I have missed all this the last couple of days ..... I have been walking in Bush/rainforests, swimming naked in streams/ocean, laying on the grass at night watching the stars and even rolling around naked in the early morning dew, eating seafood/oysters and getting around the clock oxy.

    Did Jack tell me to do all this ...nope - not really! this is my interpretation of the massive amounts of information he has given us and what I need to do for myself to live an optimal life

    The "cult" word has been used before .... those folks didn't think nn EMF had any credibility at all and have all left.

    I definitely am not the sharpest knife in the drawer .... but I have been interested in improving my health for most of my life ..... and all this makes huge sense to me and so I will implement what I can.

    In the 3+ years I have been reading what Jack kruse has been writing ....... I do my very best to understand what he is shining his flashlight on and how to apply it to my life - and that it is totally up to me.

    My life has changed dramatically ......someone very dear to me keeps telling me that I am very placid and kind and loving and healthy ..... I would never have been called placid before!

    Am I a groupie? ... I hate that word - it is extremely uncomplimentary and, in fact, quite ugly! Am I a groupie because I follow along and implement what I can and all this has made a huge difference to my life .... I guess maybe! Has Jack told me what to do - nope - I decide for myself ...well except for the oxy twice a day ...lol

    I have a huge amount of respect for Jack kruse and what he is trying to do .... after all - this is all free for anyone who wants to take the time to follow along and interact and ask questions.

    Is Jack kruse 100% right about all this? no idea .....but he is head and shoulders above anything else I read. This is all in motion ..... and I will try my best to keep up!

    There are lots of great minds/thinkers here that are learning along with us and sharing .... and asking the big questions that I don't have the knowledge to ask ......

    As far as I can tell .... Dr. k. has always valued each one of us - we all have different strengths and it makes for a great melting pot of ideas.

    I absolutely don't have a head for science ...but I do get it.

    Will I be told what to do? nope ...I have always been way too stubborn for that!
  2. nonchalant

    nonchalant Silver

    This quote from the blog really caught my attention:
    I remember the first two forms of proteins are generated from DNA. The next two folds depend on redox status. If we have to sample the local environment to accomplish proper folding, it would cause entropy to increase, right? So having to replace lots of proteins would age us more quickly.

    And a distorted or obscured view of the local environment would cause poor folding in the new protein. The last two folds must be to create a structure that would perform in a certain way given the local/current environment. Like tuning a musical instrument -- that would vary in different environments, right? Probably the same for a light-emitting instrument as well.
  3. yewwei.tan

    yewwei.tan Gold

    Yet another Paper summary 'Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein
    ' -- http://onlinelibrary.wiley.com/stor...vg&s=339510d6ac27f00f89ca7a1a4b5131e89c855d36

    H-tunneling is driven by the thermally induced dynamics of the enzyme. In some of those enzymes that break stable C–H bonds the reaction proceeds purely by quantum tunneling, without the need to partially ascend the barrier.

    The quinoprotein and flavoprotein amine dehydrogenases are ideally suited to studies of H-transfer. The reactions catalysed are conveniently divided into reductive and oxidative half-reactions. Enzyme reduction occurs by breakage of a substrate C–H bond, the kinetics of which are conveniently followed by absorbance spectrophotometry owing to reduction of the redox centre (and concomitant change in absorbance spectrum) in the enzyme active site

    The oxidative half-reaction usually involves long-range electron transfer to acceptor proteins (e.g. cytochromes, copper proteins or other flavoproteins).

    Our work has focused on the tryptophan tryptophylquinone (TTQ)-dependent amine oxidases methylamine dehydrogenase (MADH) and aromatic amine dehydrogenase (AADH), and also the flavoenzymes trimethylamine dehydrogenase (TMADH) and heterotetrameric sarcosine dehydrogenase (TSOX).

    TTQ reduction is concerted with C–H bond cleavage from an iminoquinone intermediate that forms rapidly in the reductive half-reaction

    The rate of reduction of the TTQ cofactor has a large kinetic isotope effect (KIE ¼ 16.8 ± 0.5 at 298 K), larger than the upper value expected for reactions described by transition state theory, and is suggestive of tunneling.

    Tunneling reactions are associated with KIE values greater than unity, owing to the higher probability of proton over deuterium tunneling.

    Reactions that proceed purely by quantum tunneling are independent of temperature, and thus the KIE should likewise be independent of temperature

    Our studies of TTQ reduction in MADH indicated that the value of the KIE was temperature independent, but significantly the reaction rate was strongly dependent on temperature!

    Temperature dependent fluctuations of the enzyme-substrate complex are required to distort the active site into a geometry that is compatible with a pure tunneling reaction.
    Another paper "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology" -- http://rstb.royalsocietypublishing.org/content/361/1472/1351.full

    Enzymes often rely on the coupling of electrons and protons to affect primary metabolic steps involving charge transport and catalysis. Amino acid radical generation and transport are synonymous with proton-coupled electron transfer (PCET)

    PCET is especially prevalent at metallo-cofactors that activate substrates at carbon, oxygen, nitrogen and sulphur atoms.

    The caveat to PCET is that the transfer of the proton, as the heavier particle, is fundamentally limited to short distances, whereas the electron, as the lighter particle, may transfer over very long distances

    When transport distances are short, the electron and proton may transfer together.

    When they are long, however, the predicament of the disparate transfer distances is resolved by the evolution of enzymes to control proton-transfer (PT) and electron-transfer (ET) coordinates on highly different length scales.


    The electron and the proton may transfer along the same collinear path with or without X–H bond breaking. The former describes long-range ET in biology.

    Here, electron transport along pathways containing X–H⋯Y bonds is modulated by the hydrogen bond, typically via the electronic coupling matrix element

    The coupling between the proton and the electron is more pronounced when the X–H bond breaking is involved. This subclass of PCET includes hydrogen atom transfer (HAT), which is the specific case for an electron and a proton originating from the same atom

    Amino acid radical generation often occurs by HAT as does the activation of the C–H bonds of substrates by oxidized cofactors such as those in lipoxygenase, galactose oxidase, and ribonucleotide reductase.

    In these cases, the thermodynamics for transport of the electron and the proton compels that they couple. This is most easily elucidated by the square scheme shown in figure 2.


    The other major category of PCET in biology (figure 1) is characterized by ET and PT pathways that are orthogonal to each other

    Theoretical treatments of PCET confirm that proton motion can affect electron transport even when the electron and proton do not move along collinear coordinates

    Furthermore, the same electron and proton do not have to be coupled throughout the entire transformation. As the electron moves, it may encounter different protons along a transport chain.

    All that is required for direct coupling is that the kinetics (and thermodynamics) of electron transport depends on the position of a specific proton or set of protons at any given time. It is direct coupling of the electron and proton that is the most elementary characteristic of a PCET event.

    The case of orthogonal PCET is more frequent than might be expected because the evolution of this pathway permits enzymes to manage the disparate electron and proton length scales.

    Electrons can transfer into and out of active sites over long distances in concert with protons that hop to or from the active site along amino acid side chains or along structured water channels.

    Mono-oxygenases such as cytochrome P450 and peroxidases are exemplars of enzymes that operate by this type of PCET in biology

    Orthogonal PCET is also prevalent in reductases. Crystal structures of hydrogenases (Peters et al. 1998; Nicolet et al. 1999; Volbeda & Fontecilla-Camps 2005) indicate that the mechanism for hydrogen production occurs by transporting protons into the active site along pathways distinct from those traversed by the electron equivalents. Electrons are injected putatively into the active site via a chain of [FeS] clusters, while proton channels and acidic/basic residues at the active site manage the substrate inventory.

    The discussion will begin by presenting model systems that permit the proton and electron tunnelling events to be disentangled for collinear and orthogonal PCETs. We will then show, by the lessons learned from these model systems, that PCET may be exploited in biomimetic mono-oxygenases, which display unprecedented multifunctional, catalytic activity.​
  4. yewwei.tan

    yewwei.tan Gold

    (continuation part 1 of "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology" -- http://rstb.royalsocietypublishing.org/content/361/1472/1351.full)

    2. Proton-coupled electron transfer model systems

    (a) Collinear proton-coupled electron transfer networks
    The first model systems designed to interrogate PCET reactions in a controlled manner are depicted in figure 4a.

    An electron donor (D) and acceptor (A) are assembled with a PT interface (–[H+]–), thus aligning ET and PT coordinates in a collinear D–[H+]–A fashion.

    PCET is triggered by laser excitation of the donor or acceptor and resolved kinetically by performing time-resolved spectroscopy.


    Since charge redistribution within this interface is negligible, the only available mechanism for PCET arises from the dependence of the electronic coupling matrix element on the position of the protons within the interface. Similar results have been obtained for donors and acceptors separated by guanine–cytosine base pairs

    To induce proton motion along an ET pathway, collinear systems with asymmetric interfaces such as salt bridges between donor–acceptor pairs have been constructed

    The effects of tunnelling on PCET rates through asymmetric interfaces have been uncovered with assembly shown in figure 4b. Note that in figure 4b the - [H+] - interface is represented in its non-ionized tautomeric form, which has been shown to prevail for carboxylic acids of comparable pKαs in low-dielectric environments

    Photoexcitation of the Zn(II) porphyrin photoreductant prompts ET to the naphthalene diimide electron acceptor via the amidinium–carboxylate acid interface

    (b) Orthogonal proton-coupled electron transfer networks

    The collinear PCET networks of §2a impose an inherent limitation on negotiating the length-scale disparity between PT and ET. The network is assembled by the hydrogen bonds of the PT interface; hence, PT distances are confined to the hydrogen bond length scale.

    To overcome this limitation, we are constructing the PCET model systems shown in figure 6a in which ET and PT coordinates are orthogonalized.


    In the ‘Hangman’ porphyrin architecture, a carboxylic acid or amidine is positioned over a PFeIII(OH) (P=porphyrin) redox platform via a xanthene or dibenzofuran space

    By appending an electron acceptor to the porphyrin platform, the PCET reaction may generate the ferryl: PFeIII(OH)−e−−H+→PFeIV(O) by PT to the hanging group upon ET from the haem centre.

    Conversely, by appending an electron donor to the porphyrin platform, the PCET reaction PFeIII(OH)+e−+H+→PFeII(OH2) may be accessed, where PT occurs from the hanging group upon ET to the haem

    The Hangman constructs allow us to investigate incisively the role of proton tunnelling in PCET because the PT distance is easily tuned with the length of the Hangman pillar.

    (c) Proton-coupled electron transfer biocatalysis

    A PT network disposed orthogonally to a haem redox cofactor is prevalent in structures of enzymes that derive their function from oxygen activation.

    Figure 7a focuses on the haem and its hard-wired water channel along which PT is directed. The highly activated ferryl oxygen of the redox cofactor, [​IMG]FeIV=O (compound I-type intermediate in which a FeIV=O centre resides in a porphyrin cation radical, [​IMG]), is produced by PT from the water channel to a ferric peroxy intermediate, as shown in figure 7b.

    Formation of the high-valent metal oxo fragment is thus accomplished by coupling PT to an internal 2e−redox event.


    The Hangman porphyrin is a simplified construct of cytochrome P450. The protonic pendant acid group of the Hangman porphyrin plays the same role as the water channel of the natural enzyme

    In the presence of olefins, epoxidation occurs at high turnover. In the absence of substrate, the compound I-type intermediate reacts with peroxide to generate oxygen and water in a catalase-like reactivity, also at high turnover

    The studies on these Hangman porphyrins and other macrocyclic redox platforms (Liu & Nocera 2005) clearly demonstrate that exceptional catalysis may be achieved when redox and PT properties of a cofactor are controlled independently.

    A key requirement is that the PT distance is kept short, which may be accomplished by orthogonalizing ET and PT coordinates

    Moreover, the Hangman platforms show that a multifunctional activity of a single metalloporphyrin-based scaffold is achieved by the addition of proton control to a redox platform.

  5. yewwei.tan

    yewwei.tan Gold

    (continuation part 2 of "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology" -- http://rstb.royalsocietypublishing.org/content/361/1472/1351.full)

    3. Proton-coupled electron transfer in enzymes: a study of ribonucleotide reductase
    The study of PCET in natural systems provides the convenience that both the ET and the PT groups are held at fixed distance by the secondary and tertiary structures of the protein.

    However, PCET investigations of the natural systems brings the new challenge that the PCET reaction is typically part of a more complicated cascade of events including, but not limited to, protein–protein interactions, binding/release of substrate, protons or redox equivalents, and intra-protein conformational dynamics, all of which may be necessary for enzymatic function.

    Thus, the PCET event must be isolated in the biological system, prompting us to develop new biochemical and biophysical methods for the study of PCET in biology. Paramount among these new methods are:

    1. photo-active non-natural amino acids/redox platforms that enable PCET to be photo-triggered;
    2. non-natural amino acids that permit the examination of ET and PT by control of pKa and redox potentials;
    3. the implementation of new biochemical methods that permit the non-natural amino acids to be selectively introduced along putative PCET pathways of the enzyme.
    (a) The putative proton-coupled electron transfer pathway in ribonucleotide reductase (RNR)

    Class I E. coli RNR is composed of two homodimeric subunits designated R1 and R2, and a complex between the two catalyses the reduction of nucleoside diphosphates to deoxynucleoside diphosphates

    R2 harbours the diferric tyrosyl radical (.Y122) cofactor that initiates nucleotide reduction by generating a transient thiyl radical (.C439) in the enzyme active site located in R1

    The crystal structures of both R1 and R2 have been solved independently, and a docking model, which places the Y. on R2 at a distance greater than 35 Å away from the C439 residue on R1, has been proposed

    Radical transfer over this distance has been proposed to occur via a PCET radical-hopping pathway involving radical intermediates of the aromatic amino acid residues shown in figure 8


    (b) Proton-coupled electron transfer in the R2 subunit of ribonucleotide reductase

    These studies support the contention that Y356 is a redox active amino acid on the radical propagation pathway. Open and closed circles in figure 9 represent deprotonated (indicated by open circles) and protonated (filled circles) FnY-R2s, respectively, based on the pKa values in table 1.

    Both deprotonated and protonated forms have similar activities for Ep<80 mV versus Y., establishing that the protonation state of Y356 does not affect the activity of the enzyme and hence that a proton at Y356 is not obligated to the pathway

    These results lead us to propose that, upon oxidation of Y356, the proton is transferred ‘off-pathway’ in an orthogonal manner to bulk solution, either directly or via amino acid residues of the enzyme. This result becomes more profound when taken together with the suggestion that the oxygen of a water/hydroxo bound to Fe1 in the resting-state crystal structure of R2 (Högbom et al. 2003) is the probable PT partner of Y122

    The three different regimes of RNR activity are highlighted as either gated by a physical/conformational change (regime 1), rate-limited by radical transport (regime 2), or reduced to background levels (regime 3) depending on the peak reduction potential difference between the corresponding Ac-FnY.-NH2 and Ac-Y.-NH2


    Against this backdrop of a long-distance ET in R2, a further insight into the role of PCET has come from transient kinetic studies of W–Y dipeptides. We have shown that the rate and the directionality of radical transfer between W and Y in dipeptides can be controlled by changing the pH of the bulk solution, thereby affecting the reduction potentials of the corresponding radicals

    At physiological pH values, Y. has a lower reduction potential and the direction of ET is W.–Y→W–Y.;

    the direction changes at high pH, W–Y.→W.–Y−. These results dovetail with biochemical studies of RNR

    Nordlund & Eklund (Nordlund et al. 1990; Nordlund & Eklund 1993) were the first to recognize the potential mechanistic importance of W48 and [.W48H]+ by proposing the Fe1→H118→D237→W48 pathway in cofactor assembly and nucleotide reduction, based on the structurally analogous and spectroscopically well-characterized Fe(haem)→H→D→W ET pathway in cytochrome c peroxidase

    These results, taken with site-directed mutagenesis studies (Rova et al. 1995), have led us to support a model in which W48 is central to a PCET pathway in R2 that directs both the cofactor assembly and the initiation of nucleotide reduction

    As for the latter, previous kinetic studies have led to the proposal that PCET occurs in the forward and reverse directions along the 35 Å pathway, each time nucleotide reduction occurs

    The crystal structure R2 (Högbom et al. 2003) shows that the indole nitrogen of W48 is hydrogen bonded to the carboxylate oxygen of D237 located 2.9 Å away (figure 8). Based on the W–Y dipeptide results, D237 most probably provides a site to incorporate PCET by coupling ET along the radical transport pathway to an orthogonal PT to or from W48, thus providing a mechanism in R2 to control the direction of radical transport between Y122 and Y356.

    (c) Proton-coupled electron transfer in R1 subunit of ribonucleotide reductase

    The Y731↔Y730↔C439 triad in R1 connects Y356 of R2 to the active site

    As shown by the distances in figure 8, the triad is in hydrogen-bonding contact.

    Briefly, the 20-mer C-terminal peptide tail (R2C20, NH2–YLVGQIDSEVDTDDLSNFQL–COOH) of the R2 subunit has been retained because this peptide contains the critical Y356 and the binding determinant of R2 to R1

    Using solid-phase peptide synthesis, the C-terminal peptide tail of R2 is produced with a photo-oxidant appended proximal to Y356 on the peptide (figure 10, red circle)

  6. yewwei.tan

    yewwei.tan Gold

    (continuation part 3 of "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology" -- http://rstb.royalsocietypublishing.org/content/361/1472/1351.full)

    Laser excitation of the modified peptide provides a method to generate .Y356, bypassing hole generation at the metallo-cofactor therein and allowing us to instantaneously ‘turn on’ the PCET pathway in RNR.

    The design shown in figure 10 is predicated on using a photo-generated .Y356 to initiate radical transport into R1, produce the thiyl radical at the active site, and consequently induce RNR activity

    Photoionization of W with UV light (λ<290 nm) irreversibly generates W., which in turn oxidizes Y within the pH range relevant to RNR

    The excitation wavelength required for W photoionization (and consequently W. formation) falls within the protein envelope. The drawbacks attendant to the protein acting as an ‘inner-filter’ of the excitation light led us to explore the viability of unnatural benzophenone-containing amino acids (BPA) as an excited-state oxidant of tyrosine

    Excitation of the BPA-modified peptide with UV light (λexc>325 nm) yields the benzophenone-ketyl radical and tyrosyl radical on the sub-nanosecond timescale; the photo-generated radicals recombine with a 500 ns time constant.


    Figure 11 shows that, under single turnover conditions with the peptide bound to R1 and in the presence of CDP substrate and ATP effector, the enzyme is active when excited by light and inactive in the absence of excitation.

    As seen in figure 11, this mutant is effectively inactive towards photo-initiated nucleotide reduction. This result provides strong evidence that radical transport is indeed pathway specific in R1 and suggests a collinear PCET pathway.

    (d) A model for proton-coupled electron transfer in ribonucleotide reductase

    Figure 12 presents the present model for PCET in RNR. Beginning at the cofactor, an orthogonal PT between Y122 and the diiron oxo/hydroxo cofactor establishes the need only for the transfer of an electron through the span of R2.

    Oxidation of Y356, the redox terminus of the R2 pathway, demands a PCET reaction; however, this also appears to involve a PT orthogonal to the ET pathway. By moving the protons at Y122 and Y356 off pathway, the radical transport in R2 involves a long-distance ET coupled to short PT hops at the tyrosine endpoints

    The direction of ET along the pathway may logically be ascribed to control by an orthogonal PT between W48 and D236.

    Within R1, the activity studies of the Ac-(W/BPA)-R2C20 peptide and R1, together with those of the Y730/731F R1 mutant, suggest a collinear PCET pathway through R1 in which both the electron and the proton may be transferred between Y731–Y730–C439.

    In this case, ET is used for radical transport rather than the PCET, as observed in R1 of RNR. In contrast to most systems studied to date in biology, RNR appears to incorporate all the variances of PCET mechanisms in its transport of a radical across two subunits and over 35 Å.

  7. yewwei.tan

    yewwei.tan Gold

    OK. I have many ideas about that paper I just posted, but I think I need some time to process them into something coherent :confused:

    Some preliminary thoughts:
    • pH drastically affects redox of directionality of electron tunnelling between peptides. Isolating protons pumps is a targeted way to control pH surrounding a particular region. And obviously pH makes no sense without water (pH = -log[H3O+])

    • Long range PCET seems to require orthogonal alignments of electron and proton donors. Transition metals serve best as the centre of these arranges, both due to the number of bonds they can form, as well as the motility of D-shell electrons which can be excited by light into motion (and cause subsequent Proton Tunnelling)

    • Complete hunch, but it feels like the simple cube structure of iron sulfur clusters is the best shape for controlling the 'Hangman Distance' shown above. I talked about this here -- http://forum.jackkruse.com/index.ph...about-infrared-and-ct.9675/page-5#post-146901 .

      What I do not know is what exactly controls the distance between Fe and S within an Iron Sulfur cluster. Yup, we know that EMF affects it, but what specific portion would increase or decrease that bond, or modulate between the different Fe-S clusters is something that I do not know.

      The Cytrochrome C Oxidase paper and Complex III activity references make use of Fe-S clusters as electron donors, so obviously this can be put under control. The blog also mentions Fe-S cluster control, though in the context of FAD moieties on Complex I

    • Again we see mention of Thiol groups (in the form of a Thiyl Radical), and again we see the UV absorption peaks, which actually drive Electron Tunnelling and subsequent Proton Tunnelling if the shape allows for it (either the Orthogonal or Collinear structure). I really need to dive into Thiol Group function o_O

    • I feel that negatively charged free radicals are attracted to the proton-filled active sites of enzymes. The uniqueness of the magnetic footprint of a particular free radical would attract it to a unique active site based on a particular set of proton eigenstate configurations. I have zero clue about the specifics of this mechanism, so I don't know if it is true.

    • It's true that either Electron Tunnelling or Proton Tunnelling can lead to subsequent ET or PT, since a tunnelling effect would could a charge imbalance. I would think that ET happens more readily due to the lightness of an electron and the heaviness of a proton, but then again, there are many more protons than electrons being pumped out, and the heaviness of the proton actually makes them easier to control and therefore make it possible to create localised regions of heavy proton concentration.

    • Still have no clue how entanglement fits into the picture, though I want to believe that Actin and Integrin networks can transmit signals somehow to couple the activities of non-local electrons.
    Last edited: Nov 21, 2014
  8. kovita

    kovita Gold

    Yew, thanks for this weekend. i am sure I will not waste it watching TV ;-)
    Shijin13 and caroline like this.
  9. yewwei.tan

    yewwei.tan Gold

    Ha, I traded some beach time and definitely some Tumblr time for all that reading. The flow state from reading research papers is more addictive apparently :p
    Shijin13 and caroline like this.
  10. Jack Kruse

    Jack Kruse Administrator

    shrewd picking that up......
    Shijin13 and Josh (Paleo Osteo) like this.
  11. Inger

    Inger Silver

    Well... Patrick I think Jack cannot say too much too soon - there need to be some education to understand.. and it takes time. It is not simple (even if it is very simple.. it is all so paradoxical)
    so one reason it feels like he changes his protocols a bit is, he has to give it bit by bit.
    Then.... because I hate cults and dogmas.... have had enough of these :rolleyes:... I actually love it when Jack is like he is... he certainly evolves too!!!
    Dogma is always the same and have the same rules for every one. Very rigid. Jack is the total opposite....
    I believe too Jack learns new stuff every day, and he is open. He evolves. I find it fascinating. Very sexy.

    Do I understand all the theory? No way...lol I am as far from a geek as it gets ;)
    But I get the idea... and I try it out. We always need to judge for ourselves too. Jack says it all the time. He is the least dogmatic person I know, I have to say
    That said, I understand you feel confused and angry. The way it flows on this site is very different than it does normally in our society. When we are used to that way of thinking, it can feel very confusing! But just stay open.. like a child.. contemplate.. and look for the truth always! You will find it. Let go of what other thinks or says. Just do your own thing :). We need that so badly these days. Too much brainwash and rigid thinking around. It is pretty darn tragic. :(

    and Patrick... I moved too.... to an environment with less EMF....... so good to come away from the darn smart meter... 3 and 4 G etc....
    I do not regret it one bit :)
    Shijin13 likes this.
  12. Inger, it's 'funny' almost but now I feel yes I NEED to move. It is hard to say what I am 'thinking' or 'feeling' but my body above all feels de-hydrated (though I drink lots of spring water or at least is supposed to be spring water). There is something wrong with me, like I say I feel so de-hydrated that nothing I do can change it. Dr Kruse has mentioned that diabetics are chronically de-hydrated. So again I am sorry for 'shooting my mouth' off fighting Irish I suppose. It's just it freaked me out I am trying to do all the 'right things' and I still have the problem. And yes there is 'denial' hard to admit I suppose I am powerless in spite of all that I do living in the 'microwave' here. Then again I question myself has the notion of the 'microwave' just entered my mind to make me feel this way. But I doubt that really, I don't have any 'labs' to point to perhaps it is a good idea for me to get some. But this has been a bit of an earthquake for me and I hope Dr Kruse will understand.................
    Shijin13 likes this.
  13. Inger

    Inger Silver

    well, I know Jack understands. I understand you too... that you got upset. My boyfriend cannot understand the EMF thing truly either... he does keep his cellphone on speaker and away from his body always, so he does understand the rough stuff, but he says, like your friends, look so many healthy and good looking people live in cities and they have sooo much wifi and EMF. He does not really get how bad it is at all... yet ;)
    But he lives on the countryside, no smart meter, no 3 or 4 G, no wifi from neighbors, only his own and the router is far away from the bedroom. He works in a not heated hall where he has all the training equipment that he repairs.... so he get lots of cold air too, he does not spend much time in cities at all. So actually he has a very low EMF environment overall. He spends very little time in front of the computer. He does have wireless stuff in his home tho. But I think he really have a pretty good environment. That might be why he is so healthy too. Even if he smokes and work late into the night (he have changed that a bit since he met me... thankfully)

    If you cannot get fully well even if you do all the other things right... there is only one thing left. Your environment...........
    and it does not help how much you drink if your body is not able to rehydrate and keep the water :(
    Well, I think it is amazing that you are capable of moving :) just do it as soon as you can is my advice :)
  14. Brother John

    Brother John Silver

  15. Brother John

    Brother John Silver

    Would you care to take a stab at answering the question that Pat asked in his first post in this thread?
    Jack said: "This also points out why those advocating a low carb high fat diet who have bad mitochondria might be dispensing bad public information. There is a deep down side to these dietary templates and that is the lesson I am trying to teach you here today. Context is critical when you understand how a mitochondria works."
    Jack has not replied to that, near as I can see.
    Brother John
  16. Brother John

    Brother John Silver

    No one on this forum has replied to Pat's question regarding Jack's statement: "This also points out why those advocating a low carb high fat diet who have bad mitochondria might be dispensing bad public information. There is a deep down side to these dietary templates and that is the lesson I am trying to teach you here today. Context is critical when you understand how a mitochondria works."
    Would you care to respond?
    Brother John
  17. Jack Kruse

    Jack Kruse Administrator

    It's been answered.
  18. HoneyChild

    HoneyChild Gold

    I thought ketosis without DHA = bad.

    Ketosis with DHA = good.
  19. Josh

    Josh Gold

    I think this addresses it from Facebook:

    Scaling out a little....


    Last edited: Nov 21, 2014
    Shijin13 and Brother John like this.
  20. NeilBB

    NeilBB New Member

    Put it together Brother. Free radicals/ROS are important signalling molecules for long term health and longevity. You need to be able to sense your environment. Free radicals are produced to excess in most today due to environmental mismatches (nn-EMF excess, circadian dysregulation).

    The mainstream wants you to take antioxidants to "fix" the problem. This reduces the temporary excess but does not help the signalling process--in long run hurts it.

    LCHF people reduce ROS through avoidance of carbohydrate-derived electron input to complex I. Same answer, if not modulated by seasonal input eventually. See my post here...

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