Component
Lactoperoxidase enzyme family
Cross-species LPO family. Abstract-only records with unresolved preparation species do not assert the human isoform was tested.
15 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
Peroxide-preincubated LPO exposed to iodide yielded a crystal complex containing hypoiodite in its substrate channel.
Experimental context and source evidence
- experimental_model
- Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- The oxidized iodine product was observed structurally.
- primary_references
- Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 232–238
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft
## ki-lpo-product The oxidized iodine product was observed structurally. Peroxide-preincubated LPO exposed to iodide yielded a crystal complex containing hypoiodite in its substrate channel. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230
Complete structured claim and evidence
What acts on it
The LPO structure contains covalently attached heme; peroxide sits between its iron and distal His109.
Experimental context and source evidence
- experimental_model
- Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Iron-containing heme positions peroxide in the enzyme.
- primary_references
- Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 216–222
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft
## ki-lpo-heme Iron-containing heme positions peroxide in the enzyme. The LPO structure contains covalently attached heme; peroxide sits between its iron and distal His109. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461
Complete structured claim and evidence
Where it participates (unsigned role)
Replacing thiocyanate with iodide in the LPO/H2O2 system reduced adenovirus transduction.
Experimental context and source evidence
- experimental_model
- Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Changing the enzyme substrate changed antiviral activity.
- primary_references
- Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 72–78
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft
## ki-air-adeno Changing the enzyme substrate changed antiviral activity. Replacing thiocyanate with iodide in the LPO/H2O2 system reduced adenovirus transduction. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Complete structured claim and evidenceDifferentiated airway epithelia supplied sufficient peroxide for antiviral activity when LPO and iodide were added.
Experimental context and source evidence
- experimental_model
- Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Airway cells supplied the oxidant needed by the enzyme.
- primary_references
- Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 88–94
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft
## ki-air-peroxide Airway cells supplied the oxidant needed by the enzyme. Differentiated airway epithelia supplied sufficient peroxide for antiviral activity when LPO and iodide were added. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Complete structured claim and evidenceThe LPO/iodide/H2O2 system reduced RSV titre; the tested thiocyanate system did not inactivate RSV or adenovirus.
Experimental context and source evidence
- experimental_model
- Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Iodide and thiocyanate were not interchangeable against these viruses.
- primary_references
- Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 80–86
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. · source_derived_draft · unverified_draft
## ki-air-rsv Iodide and thiocyanate were not interchangeable against these viruses. The LPO/iodide/H2O2 system reduced RSV titre; the tested thiocyanate system did not inactivate RSV or adenovirus. Model: Primary airway epithelial cultures and human oral-KI exposure; separate experimental arms. Limitations: Culture antiviral activity and human secretion measurements do not establish prevention or treatment of human infection. Evidence location: Primary abstract Enhancement of respiratory mucosal antiviral defenses by the oxidation of iodide. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21441383/ · DOI 10.1165/rcmb.2010-0329oc
Complete structured claim and evidenceIodide substituted for thiocyanate in LPO/H2O2-dependent glutathione oxidation; chloride and bromide were ineffective substitutes.
Experimental context and source evidence
- experimental_model
- Purified biochemical reaction; GSH measured by amperometric titration.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- No demonstration that ordinary KI intake depletes human glutathione.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- This iodine chemistry can consume glutathione in a test system.
- primary_references
- Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN-/H2O2. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1324202/ · DOI 10.1016/0891-5849(92)90014-8
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 248–254
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified biochemical reaction; GSH measured by amperometric titration. · source_derived_draft · unverified_draft
## ki-gsh This iodine chemistry can consume glutathione in a test system. Iodide substituted for thiocyanate in LPO/H2O2-dependent glutathione oxidation; chloride and bromide were ineffective substitutes. Model: Purified biochemical reaction; GSH measured by amperometric titration. Limitations: No demonstration that ordinary KI intake depletes human glutathione. Evidence location: Primary abstract Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN-/H2O2. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1324202/ · DOI 10.1016/0891-5849(92)90014-8
Complete structured claim and evidenceInhibiting LPO activity increased lung lesions, RSV mRNA and antigen in the lamb experiment.
Experimental context and source evidence
- experimental_model
- Newborn and three-week-old lamb RSV experiments; oral KI given by intragastric gavage.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Animal disease model; no human antiviral efficacy established. LPO inhibition supports pathway involvement, not an exclusively LPO mechanism.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Blocking the enzyme weakened protection.
- primary_references
- Increased concentration of iodide in airway secretions is associated with reduced respiratory syncytial virus disease severity. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24053146/ · DOI 10.1165/rcmb.2012-0529oc
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 120–126
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Newborn and three-week-old lamb RSV experiments; oral KI given by intragastric gavage. · source_derived_draft · unverified_draft
## ki-lamb-lpo-block Blocking the enzyme weakened protection. Inhibiting LPO activity increased lung lesions, RSV mRNA and antigen in the lamb experiment. Model: Newborn and three-week-old lamb RSV experiments; oral KI given by intragastric gavage. Limitations: Animal disease model; no human antiviral efficacy established. LPO inhibition supports pathway involvement, not an exclusively LPO mechanism. Evidence location: Primary abstract Increased concentration of iodide in airway secretions is associated with reduced respiratory syncytial virus disease severity. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24053146/ · DOI 10.1165/rcmb.2012-0529oc
Complete structured claim and evidenceH2O2 formed LPO compound I with second-order rate constant (1.1 ± 0.1) × 10^7 M−1 s−1.
Experimental context and source evidence
- experimental_model
- Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Peroxide activates the enzyme before iodide oxidation.
- primary_references
- Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 184–190
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft
## ki-lpo-activate Peroxide activates the enzyme before iodide oxidation. H2O2 formed LPO compound I with second-order rate constant (1.1 ± 0.1) × 10^7 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Complete structured claim and evidenceHypoiodite occupied the distal heme cavity; ABTS activity experiments supported product inhibition.
Experimental context and source evidence
- experimental_model
- Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- The enzyme product can limit further enzyme activity.
- primary_references
- Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 240–246
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft
## ki-lpo-feedback The enzyme product can limit further enzyme activity. Hypoiodite occupied the distal heme cavity; ABTS activity experiments supported product inhibition. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase. · 2022 · https://pubmed.ncbi.nlm.nih.gov/34761444/ · DOI 10.1002/pro.4230
Complete structured claim and evidenceIodide reduced LPO compound I to native enzyme at (1.2 ± 0.04) × 10^8 M−1 s−1.
Experimental context and source evidence
- experimental_model
- Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Iodide supplies electrons to activated lactoperoxidase.
- primary_references
- Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 192–198
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft
## ki-lpo-iodide Iodide supplies electrons to activated lactoperoxidase. Iodide reduced LPO compound I to native enzyme at (1.2 ± 0.04) × 10^8 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Complete structured claim and evidenceThiocyanate reacted with LPO compound I at 2.0 × 10^8 M−1 s−1.
Experimental context and source evidence
- experimental_model
- Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Thiocyanate is another rapidly reacting substrate.
- primary_references
- Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 200–206
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft
## ki-lpo-scn Thiocyanate is another rapidly reacting substrate. Thiocyanate reacted with LPO compound I at 2.0 × 10^8 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
Complete structured claim and evidencePreincubating LPO with ammonium iodide decreased measured catalytic activity and stabilized a peroxide–iodide ternary complex.
Experimental context and source evidence
- experimental_model
- Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- Iodide can inhibit the enzyme under a different order of exposure.
- primary_references
- Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 224–230
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. · source_derived_draft · unverified_draft
## ki-lpo-substrate-block Iodide can inhibit the enzyme under a different order of exposure. Preincubating LPO with ammonium iodide decreased measured catalytic activity and stabilized a peroxide–iodide ternary complex. Model: Purified LPO crystallography and activity assays; ammonium iodide supplied the anion, not KI. Limitations: Structural/biochemical model; enzyme species not assigned from abstract. Cofactor chemistry does not establish dietary iron responsiveness. Evidence location: Primary abstract Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33882424/ · DOI 10.1016/j.jinorgbio.2021.111461
Complete structured claim and evidenceLPO/H2O2/iodide oxidized NADH to a product chemically distinct from NAD+, unlike the thiocyanate and bromide systems.
Experimental context and source evidence
- experimental_model
- Cell-free LPO/H2O2 reactions with nicotinamide nucleotides.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- The NADH reaction did not simply regenerate normal NAD+.
- primary_references
- The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 256–262
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. · source_derived_draft · unverified_draft
## ki-nadh The NADH reaction did not simply regenerate normal NAD+. LPO/H2O2/iodide oxidized NADH to a product chemically distinct from NAD+, unlike the thiocyanate and bromide systems. Model: Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. Limitations: Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva. Evidence location: Primary abstract The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791
Complete structured claim and evidenceNADPH was also oxidized under the LPO/H2O2/iodide conditions.
Experimental context and source evidence
- experimental_model
- Cell-free LPO/H2O2 reactions with nicotinamide nucleotides.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- The chemistry also reaches the NADPH reducing pool.
- primary_references
- The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 264–270
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. · source_derived_draft · unverified_draft
## ki-nadph The chemistry also reaches the NADPH reducing pool. NADPH was also oxidized under the LPO/H2O2/iodide conditions. Model: Cell-free LPO/H2O2 reactions with nicotinamide nucleotides. Limitations: Chemical oxidation is not evidence that supplementation drains niacin in vivo; the authors expected thiocyanate oxidation to predominate in milk/saliva. Evidence location: Primary abstract The oxidation of reduced nicotinamide nucleotides by hydrogen peroside in the presence of lactoperoxidase and thiocyanate, iodide or bromide. · 1970 · https://pubmed.ncbi.nlm.nih.gov/4317722/ · DOI 10.1042/bj1170791
Complete structured claim and evidenceSalivary hypoiodous acid increased after contrast exposure and its change correlated with iodine load.
Experimental context and source evidence
- experimental_model
- Paired saliva measurements in 40 coronary-angiography patients exposed to iodinated contrast.
- exposure_category
- Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
- limitations
- Contrast exposure is not oral KI; observational chemistry endpoints do not establish infection prevention or a safe effective supplement dose.
- nutrient_topic
- Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
- plain_language
- The saliva contained more of an oxidized iodine species.
- primary_references
- Excess iodine exposure acutely increases salivary iodide and antimicrobial hypoiodous acid concentrations in humans. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36463312/ · DOI 10.1038/s41598-022-23803-8
Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 168–174
AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Paired saliva measurements in 40 coronary-angiography patients exposed to iodinated contrast. · source_derived_draft · unverified_draft
## ki-saliva-hoi The saliva contained more of an oxidized iodine species. Salivary hypoiodous acid increased after contrast exposure and its change correlated with iodine load. Model: Paired saliva measurements in 40 coronary-angiography patients exposed to iodinated contrast. Limitations: Contrast exposure is not oral KI; observational chemistry endpoints do not establish infection prevention or a safe effective supplement dose. Evidence location: Primary abstract Excess iodine exposure acutely increases salivary iodide and antimicrobial hypoiodous acid concentrations in humans. · 2022 · https://pubmed.ncbi.nlm.nih.gov/36463312/ · DOI 10.1038/s41598-022-23803-8
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.