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Selenophosphate in Biochemical Reactions
Below is an exploration of whether selenophosphate (HSePO₃˛⁻) serves as a raw material, intermediate, or final product across major biochemical reaction types in the human body. I’ve assumed “selnium phospharte” was intended as “selenophosphate,” a recognized biochemical compound, since “selenium phosphate” isn’t standard.
1. Oxidation-Reduction (Redox) Reactions
Description: Redox reactions transfer electrons, vital for energy and antioxidant defense. Deep Dive: Glutathione peroxidase (GPx) reduces H₂O₂ using selenocysteine (Sec): H₂O₂ + 2GSH → 2H₂O + GSSG. Sec cycles through selenenic acid (R-SeOH) and selenenyl sulfide (R-Se-SG). Selenophosphate’s Role: Deeper: Selenophosphate synthetase (SPS2) makes it from H₂Se + ATP → HSePO₃˛⁻ + AMP + Pi, enabling redox via selenoproteins.
2. Group Transfer Reactions
Description: Transfer functional groups (e.g., phosphate) via kinases or transferases. Deep Dive: Phosphofructokinase-1 in glycolysis: Fructose-6-P + ATP → Fructose-1,6-bisphosphate + ADP. SPS2 transfers phosphate to selenide. Selenophosphate’s Role: Deeper: Could it act like ATP elsewhere? Likely not—specialized for selenium delivery.
3. Hydrolysis Reactions
Description: Break bonds with water, e.g., proteases. Deep Dive: Trypsin hydrolyzes peptides: R₁-CONH-R₂ + H₂O → R₁-COOH + R₂-NH₂. Selenophosphate’s Role: Deeper: Stable in water, no hydrolysis role.
4. Isomerization Reactions
Description: Rearrange structures, e.g., isomerases. Deep Dive: Phosphoglycerate mutase: 3-PG → 2-PG. Selenophosphate’s Role: Deeper: Fixed structure, no isomerization likely.
5. Ligation Reactions
Description: Form bonds with energy, e.g., ligases. Deep Dive: DNA ligase: 5’-PO₄ + 3’-OH + ATP → phosphodiester bond + AMP + PPi. Selenophosphate’s Role: Deeper: Selenium transfer is translation-related, not classic ligation.
6. Addition/Elimination Reactions
Description: Add/remove groups to/from double bonds. Deep Dive: Fatty acid synthase adds acetyl units. Selenophosphate’s Role: Deeper: No double-bond chemistry link.
Conclusion
Selenophosphate is synthesized biochemically (not natural as a mineral) via SPS2. It’s a raw material and intermediate in selenocysteine synthesis, supporting redox reactions indirectly through selenoproteins (e.g., GPx, TrxR). Not a final product, nor directly involved in hydrolysis, isomerization, ligation, or addition/elimination. Its key role is enabling antioxidant and thyroid metabolism. 701Endrun










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Selenium, Vitamin C, and Viral Infection: Deep Recalculation
You’re digging into whether the Baka’s ZEBOV seropositivity ties to low-dose survival due to health, questioning if it’s the same as our selenium/Gabon nut focus. You’re skeptical of bat-fruit transmission theories and propose selenium’s soil presence means it’s in all local fruit—maybe enough to stop EBOV like vitamin C might. The real question: Does selenium prevent viral infection, with or without vitamin C? Let’s rethink this, varying vitamin C levels (low, medium, high, optimal) across all reactions.
Baka Low-Dose Hypothesis
Idea: Baka got subclinical EBOV doses, and being “healthy” (diet, genetics) let them survive without severe disease. Similar to our Gabon nut angle—compounds aiding resilience, not prevention. But EBOV’s macrophage-killing doesn’t care about “health” unless something blocks entry. Selenium (SeMet, ~5–50 µg/day) and nuts’ phenolics/fats don’t stop it—survival’s likely exposure luck or innate factors, not immunity.
Bat-Fruit Transmission Critique
Theory: Bats (alleged EBOV reservoirs) drop fruit; gorillas/humans eat it, spreading EBOV. Issues: Bats aren’t proven EBOV carriers (seropositive, no live virus isolated). Selenium in Gabon nuts (~1–10 µg/100g) reflects soil—same for bat-eaten fruit (e.g., figs). If present, it’s low, organic SeMet—not antiviral selenite. No evidence fruit selenium prevents EBOV in any species—transmission’s likely direct (e.g., bushmeat), not fruit-mediated.
Core Question: Does Selenium Prevent Viral Infection?
Without Vitamin C:
  • Lipinski (2015): Selenite (50–100 µM) blocks enveloped virus entry (EBOV, SARS-CoV-2) via thiol oxidation. Dietary SeMet/SeCys (~1–2 µM blood max) don’t form selenite or hit thresholds—entry occurs.
  • Selenoproteins: GPx/TrxR reduce cellular damage post-infection, not pre-infection—EBOV infects macrophages, COVID-19 binds ACE2.
Conclusion: Selenium alone doesn’t prevent infection—mitigates severity at best.
Vitamin C’s Role and Variants
Vitamin C (ascorbate): Antioxidant, immune booster, potential antiviral. EBOV/COVID-19 studies suggest high doses reduce severity—does it synergize with selenium? Let’s vary C levels and rethink reactions:
Low Vitamin C (~10–30 mg/day, Deficiency)
Scurvy range—common in malnourished populations.
  • SeMet/SeCys (200 µg/day): Selenoproteins function (GPx reduces H₂O₂), but low C impairs collagen synthesis, weakens barriers—EBOV breaches macrophages, COVID-19 spikes ACE2.
  • Gabon Nuts (~5–50 µg Se): Minimal selenoprotein boost; phenolics’ antioxidant effect dwarfed by C deficiency—viral entry unchecked.
  • Selenite (Lipinski): Hypothetical high dose still oxidizes thiols, but low C limits immune response—partial prevention, poor survival.
Outcome: No prevention—selenium’s edge dulled by C shortage.
Medium Vitamin C (~50–100 mg/day, RDA)
Typical intake (e.g., Baka via fruit).
  • SeMet/SeCys (200 µg): Selenoproteins + moderate C reduce oxidative stress—EBOV macrophage damage persists, COVID-19 severity drops slightly (e.g., Zhang et al., 2020).
  • Gabon Nuts: Low Se + phenolics + C (~50 mg from diet) support innate resilience—EBOV infects, but survival odds rise vs. deficiency.
  • Seleni/www/us/ca/palo-alto/vrx/insights/sci/med/science/vit/Se/sepo4/next/next

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Reassessing Selenium and ZEBOV/COVID-19 Immunity
You’ve challenged immune priming as an explanation for the Baka’s ZEBOV seropositivity, noting EBOV destroys macrophages regardless of prior exposure. Fair point—EBOV’s immune evasion is brutal. Let’s re-analyze if SeMet or SeCys supplementation could match any theoretical immunity, extending to COVID-19, per Lipinski’s selenite claim, and reconsider the Baka’s case.
ZEBOV’s Immune Evasion
ZEBOV infects macrophages and dendritic cells early, replicating rapidly and triggering cytokine storms while impairing adaptive immunity. Primed antibodies might bind, but EBOV’s glycoprotein (GP) shields it, and macrophage destruction sidesteps immune memory. Baka seropositivity (5–10%, 1990s data) implies survival of exposure, but not necessarily resistance—could selenium play a role?
Lipinski’s Selenite Mechanism
Lipinski (2015) claims selenite (Na₂SeO₃) oxidizes thiol groups on enveloped virus GPs (e.g., ZEBOV’s GP), blocking cell entry at ~50–100 µM in vitro. This is extracellular, pre-infection inhibition—independent of immune cells. For COVID-19 (SARS-CoV-2), spike protein thiols might be similarly vulnerable, though untested. SeMet/SeCys must replicate this to match the claim.
SeMet and SeCys: Do They Deliver?
Metabolism:
  • SeMet: Incorporated into proteins (e.g., albumin) or reduced to H₂Se via trans-selenation, then to selenophosphate for selenoproteins.
  • SeCys: Directly used in selenoproteins (e.g., GPx, TrxR) via tRNA^[Sec].
Antiviral Potential:
  • Supplement (200 µg/day): Blood selenium hits ~1–2 µM, mostly protein-bound SeMet/SeCys—no free selenite forms.
  • Lipinski’s Threshold: 50–100 µM selenite—SeMet/SeCys are 25–100x too low and lack oxidative capacity extracellularly.
  • Mechanism: No evidence SeMet/SeCys oxidize viral GPs. Selenoproteins (e.g., TrxR) reduce cellular thiols, opposite to selenite’s effect.
ZEBOV: Can’t block macrophage entry—EBOV infects despite selenoproteins. COVID-19: No spike protein inhibition—SARS-CoV-2 enters via ACE2 regardless.
Baka’s Case Without Priming
Gabon nuts (~1–10 µg Se/100g, SeMet) yield ~5–50 µg/day—blood selenium <0.5 µM, all organic. No selenite, no Lipinski effect. If not priming, possibilities:
  • Subclinical Exposure: Low-dose infections survived via innate resilience, not selenium.
  • Genetic Factors: Unique immune responses (e.g., TLR variants) resisting EBOV’s macrophage hit—unproven.
  • Nutritional Synergy: Gabon nuts’ fats/proteins aid survival, not Se-specific.
Selenium’s Role: Minimal SeMet boosts selenoproteins slightly, reducing oxidative damage post-infection, but EBOV’s speed outpaces this.
SeMet/SeCys vs. Baka vs. COVID-19
SeMet/SeCys (200 µg/day):
  • ZEBOV: Selenoproteins (GPx, TrxR) mitigate cytokine storm damage, but don’t stop entry—better than Baka’s low dose, yet insufficient.
  • COVID-19: Reduces severity (e.g., Zhang et al., 2020), not infection—general immune support, not Lipinski’s block.
Baka (~5–50 µg/day): Lower selenoprotein boost, no entry inhibition—survival likely luck or non-selenium factors.

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Selenophosphate in Biochemical Reactions
Below is an exploration of whether selenophosphate (HSePO₃˛⁻) serves as a raw material, intermediate, or final product across major biochemical reaction types in the human body. I’ve assumed “selnium phospharte” was intended as “selenophosphate,” a recognized biochemical compound, since “selenium phosphate” isn’t standard.
1. Oxidation-Reduction (Redox) Reactions
Description: Redox reactions transfer electrons, vital for energy and antioxidant defense. Deep Dive: Glutathione peroxidase (GPx) reduces H₂O₂ using selenocysteine (Sec): H₂O₂ + 2GSH → 2H₂O + GSSG. Sec cycles through selenenic acid (R-SeOH) and selenenyl sulfide (R-Se-SG). Selenophosphate’s Role: Deeper: Selenophosphate synthetase (SPS2) makes it from H₂Se + ATP → HSePO₃˛⁻ + AMP + Pi, enabling redox via selenoproteins.
2. Group Transfer Reactions
Description: Transfer functional groups (e.g., phosphate) via kinases or transferases. Deep Dive: Phosphofructokinase-1 in glycolysis: Fructose-6-P + ATP → Fructose-1,6-bisphosphate + ADP. SPS2 transfers phosphate to selenide. Selenophosphate’s Role: Deeper: Could it act like ATP elsewhere? Likely not—specialized for selenium delivery.
3. Hydrolysis Reactions
Description: Break bonds with water, e.g., proteases. Deep Dive: Trypsin hydrolyzes peptides: R₁-CONH-R₂ + H₂O → R₁-COOH + R₂-NH₂. Selenophosphate’s Role: Deeper: Stable in water, no hydrolysis role.
4. Isomerization Reactions
Description: Rearrange structures, e.g., isomerases. Deep Dive: Phosphoglycerate mutase: 3-PG → 2-PG. Selenophosphate’s Role: Deeper: Fixed structure, no isomerization likely.
5. Ligation Reactions
Description: Form bonds with energy, e.g., ligases. Deep Dive: DNA ligase: 5’-PO₄ + 3’-OH + ATP → phosphodiester bond + AMP + PPi. Selenophosphate’s Role: Deeper: Selenium transfer is translation-related, not classic ligation.
6. Addition/Elimination Reactions
Description: Add/remove groups to/from double bonds. Deep Dive: Fatty acid synthase adds acetyl units. Selenophosphate’s Role: Deeper: No double-bond chemistry link.
Conclusion
Selenophosphate is synthesized biochemically (not natural as a mineral) via SPS2. It’s a raw material and intermediate in selenocysteine synthesis, supporting redox reactions indirectly through selenoproteins (e.g., GPx, TrxR). Not a final product, nor directly involved in hydrolysis, isomerization, ligation, or addition/elimination. Its key role is enabling antioxidant and thyroid metabolism. 701Endrun
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Selenite and Selenate Interconversion in Human Biochemistry
Your question asks if human biochemistry includes processes that convert selenite (SeO₃˛⁻) to selenate (SeO₄˛⁻) and selenate back to selenite, either directly or indirectly. Let’s break this down based on selenium metabolism.
Background on Selenite and Selenate
Selenite (Se⁴⁺, SeO₃˛⁻) and selenate (Se⁶⁺, SeO₄˛⁻) are inorganic selenium oxyanions. Selenite has selenium in the +4 oxidation state, while selenate is +6, making conversions between them redox processes—oxidation for selenite to selenate, reduction for selenate to selenite. In nature, microbes and plants perform these reactions, but what about humans?
Selenite to Selenate (Oxidation)
Direct Conversion: No enzyme in human biochemistry is known to directly oxidize selenite to selenate. Human selenium metabolism focuses on reducing inorganic selenium (like selenite) to selenide (Se˛⁻) for selenoprotein synthesis, not oxidizing it upward. No oxidases or oxygenases specifically target selenite to produce selenate. Indirect Conversion: Indirect oxidation is also unlikely. Selenite enters cells via transporters (e.g., sodium-dependent phosphate transporters) and is reduced by glutathione (GSH) or thioredoxin reductase (TrxR) systems to selenide (H₂Se), bypassing selenate. For example: No pathway diverts to selenate. Reactive oxygen species (ROS) or peroxidases might theoretically oxidize selenium compounds, but human systems lack evidence of selenate as an intermediate or product here. Selenate, if ingested, is absorbed as-is or reduced, not formed from selenite.
Selenate to Selenite (Reduction)
Direct Conversion: No specific human enzyme directly reduces selenate to selenite. In bacteria, selenate reductase (e.g., SerABC) performs this: SeO₄˛⁻ + 2e⁻ + 2H⁺ → SeO₃˛⁻ + H₂O, but humans lack an equivalent. Selenate metabolism in humans skips selenite, reducing selenate all the way to selenide. Indirect Conversion: Selenate (absorbed via sulfate transporters) is reduced to selenide for selenoprotein synthesis, likely via a multi-step process involving thioredoxin or glutathione systems, but selenite isn’t a confirmed intermediate. A speculated pathway: Studies suggest selenate reduction might involve APS reductase-like activity (borrowed from sulfur metabolism), but it bypasses selenite. For example, selenate-fed animals excrete selenite only after full reduction to selenide, then oxidation during excretion—not as a metabolic step.
Reverse Context and Excretion
Human selenium metabolism prioritizes selenide for selenophosphate (HSePO₃˛⁻) synthesis, used in selenocysteine (Sec) production for selenoproteins (e.g., GPx, TrxR). Excess selenium is methylated (e.g., to trimethylselenonium) or excreted as selenite in urine, but this selenite comes from selenide oxidation during excretion, not selenate reduction. No bidirectional selenite-selenate cycle exists.
Conclusion
No direct or indirect process in human biochemistry converts selenite to selenate—oxidation isn’t a goal. Selenate to selenite reduction also lacks evidence; selenate reduces to selenide, skipping selenite. Human selenium handling reduces both to selenide for selenoproteins or excretion, with no interconversion between these oxyanions. 701Endrun