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cytochrome

oxide. Nitric oxide binds to cytochrome oxase. It slows electron flow. It mimics what cyanide does to us except we don't die. And we limit the amount of ATP we need. Why? Because fundamentally, what
Concept
cytochrome
Score
4 · because · fundamental
Status
candidate — not yet promoted to canon

Corpus evidence — top 10 passages

Most-relevant passages from the entire indexed corpus (67,286 paragraph chunks across YouTube transcripts, PubMed, arXiv, archive.org, Stanford Encyclopedia of Philosophy, OpenAlex, and more) ranked by semantic similarity (bge-small-en-v1.5).

  1. 01 · yt0.804

    That's where the other cytochrome proteins are made. And the other cytochrome proteins further were able to make other uh magneto-chemistry, which is superoxide, hydrogen peroxide. These are all chemicals that become electric resistance molecules that slow light down to do different things distal to it. And when you actually see what nitric oxide does, it also acts at cytochrome c oxidase, which is the fourth cytochrome, right before the ATPase. So, now you have a cap on how hemoglobin can work, and it turns out when nitric oxide binds to hemoglobin at a significant amount when we're hypoxic,

    yt/wwNutyiyQ2I-interview-with-dr-jack-kruse-04-08-2025/transcript.txt

  2. 02 · blog0.787

    One of acetylcholine's important functions, in the brain as elsewhere, is the relaxation of blood vessels, and this is done by activating the synthesis of NO, nitric oxide. (Without NO, acetylcholine constricts blood vessels; Librizzi, et al., 2000.) The basic control of blood flow in the brain is the result of the relaxation of the wall of blood vessels in the presence of carbon dioxide, which is produced in proportion to the rate at which oxygen and glucose are being metabolically combined by active cells. In the inability of cells to produce CO2 at a normal rate, nitric oxide synthesis in b

    blog/raypeat-com/new-page-title-here.md

  3. 03 · yt0.763

    Because where does that cytochrome Where is it found? This is important for you to understand. It's found right before the ATPase. So, you We're creating a huge amount of electrical resistance at that level, so that that energy then can be distributed to other places to cause other innovations in the cell. And doesn't that make sense when you think about the story that Darwin could never figure out? Why all of a sudden did we get 32 phyla seems like overnight? Well, because guess what? We figured out we needed to use photo-bioelectric resistance to capture the light to use it to do other thing

    yt/wwNutyiyQ2I-interview-with-dr-jack-kruse-04-08-2025/transcript.txt

  4. 04 · _intake0.761

    Consider what oxygen and nitrogen coupling are tied to that too few mention: ROS and RNS. No one seems to understand how they work in unison coupled together in ubiquitination. Superoxide is a molecule used to send information to various parts of the body. That information is buried in electron spin. In the beginning of an uncoupling state or an early disease state, too much superoxide is always the major issue the literature points too. This side tracks peoples perception because they don’t understand there are simultaneous other effects going on simultaneously elsewhere inside our quantized

    _intake/kruse-blog-corpus/articles/ubiquitination-10-bio-hacking-ros-and-rns.md

  5. 05 · _intake0.758

    As it slows, time speeds up for an organism and illness and death become more likely. This is why taking cyanide is so deadly. It stops ECT transport of electrons immediately and death is the result. This linkage between incident light, free radical chemistry, and oxygen tensions becomes the critical measuring sticks for how well the mitochondria part of the cell yokes to the nucleus and cytosol of cell. The better they work together in unison the less food is needed to run life. This lowers the looseness of ECT = increases the % heteroplasmy that is SAFE based upon the environmental signals t

    _intake/kruse-blog-corpus/articles/biohacking-time-with-methylene-blue.md

  6. 06 · pubmed0.754

    In recent papers on protonmotive redox mechanisms in cytochrome oxidase in [(1987) FEBS Lett. 222, 235-245] and [Glynn Biological Research Reports (1987) 3, 1-7], I have suggested that a copper centre may enable the H2O/OH or H2O/O couple to act as the hydrogen-carrying arm of a redox loop by means of a (CuOH2)+/(CuOH)+ or (CuOH2)+/(CuO)+ system at the centre. I here explain that critical comments by Malmström [(1988) FEBS Lett. 231, 268-269] on the first of these papers, which might also be levelled at the second, depend on a misunderstanding. I also respond to Malmström's comment about testi

    pubmed/PMID-2834228-strategy-of-research-on-the-chemiosmotic-mechanism-of-cytoch/info.md

  7. 07 · _intake0.749

    This is one of their major down pitfalls. Why is this a bad thing? Oxygen is the 3rd most abundant element and has special features that make it “*life and light friendly”.* Since life is carbon-based, and among the elements, only 9 are more electronegative than carbon. This means we have few atomic choices that can serve as electron acceptors from carbon-based life forms. Of the 9, selenium, sulfur, iodine, krypton, bromine, nitrogen, chlorine, oxygen, and fluorine, oxygen ranks second in electronegativity to fluorine. This means the reduction of oxygen (adding of electrons) provides close th

    _intake/kruse-blog-corpus/articles/how-man-helps-the-eye-clock.md

  8. 08 · yt0.749

    It's got 12 electrons. So, when you put it inside that cage, it means light can't affect its oxidation state. So, what did that do? They took CO2, created more oxygen, and that's how you got the whole food uh pyramid. That's where every single food web ties back to that process. 50 year 50 million years later, right at the beginning of the Cambrian explosion, evolution kicks out the idea of heme proteins. Where does it get this idea? From the story I just told you. Oxygen now is going from 0% up to like 10 or 15% and oxygen's toxic, so they take bacteria and and archaea, put them together. And

    yt/wwNutyiyQ2I-interview-with-dr-jack-kruse-04-08-2025/transcript.txt

  9. 09 · blog0.748

    Hypothyroidism was also associated to high phospho-p38 mitogen-activated protein kinase and decreased phospho-extracellular signal-regulated kinase 1/2 and cyclin D1 levels. Similarly to thyroid hormones, but without changing thyroid status, nitric-oxide synthase inhibitor N(omega)-nitro-L-arginine methyl ester increased basal metabolic rate, prevented mitochondrial nitration and complex I derangement, and turned mitogen-activated protein kinase signaling and cyclin D1 expression back to control pattern. We surmise that nNOS spatial confinement in mitochondria is a significant downstream effec

    blog/raypeat-com/new-page-title-here.md

  10. 10 · _intake0.745

    The amount of light absorbed at cytochrome 1 is also stochastically linked to the amount of oxygen needed by a mitochondria. Remember all electrons in mitochondria are sent to reduce oxygen to O2. This is the only reason animals need to breathe. In this way oxygen is a measuring stick for how fast electron tunneling needs to be. This means that tunneling speeds are also linked to temperature of the surrounding local environment. As oxygen from the environment lowers in pseudohypoxia, ECT must also slow.

    _intake/kruse-blog-corpus/articles/biohacking-time-with-methylene-blue.md

Curation checklist

  • ☐ Verify excerpt against source recording
  • ☐ Tag tier (axiom · law · principle · primary derivation · observation)
  • ☐ Cross-cite to ≥1 primary source (PubMed / arXiv / archive.org)
  • ☐ Promote to bucket-canon/05-biophysics/