Superoxide radical anion

evidence_span

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experimental_model

Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays

exposure

Oxygen at 5 atmospheres absolute for 30 minutes, with L-NAME, a nitric oxide donor, or intravascular superoxide dismutase

limitations

Five atmospheres is well above therapeutic pressure and was chosen to study oxygen toxicity. The superoxide dismutase rescue is the key mechanistic step.

nutrient_topic

Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy

organism

Rat

plain_language

Superoxide destroys the molecule that keeps vessels relaxed, and removing superoxide removes the effect.

primary_references

[hbot-p11139368] Hyperbaric oxygen reduces cerebral blood flow by inactivating nitric oxide. (2000). https://pubmed.ncbi.nlm.nih.gov/11139368/ DOI: 10.1006/niox.2000.0313

tissue_or_cell_type

Brain

Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 166–177

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays · source_derived_draft · unverified_draft

### hbot-no-inactivation Brain nitric oxide metabolite levels fell by 31% and correlated with the fall in blood flow, while estimated hydroxyl radical production rose by 56%, and the blood-flow decrease was completely abolished by intravascular superoxide dismutase. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Superoxide destroys the molecule that keeps vessels relaxed, and removing superoxide removes the effect. organism: Rat tissue_or_cell_type: Brain experimental_model: Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays limitations: Five atmospheres is well above therapeutic pressure and was chosen to study oxygen toxicity. The superoxide dismutase rescue is the key mechanistic step. exposure: Oxygen at 5 atmospheres absolute for 30 minutes, with L-NAME, a nitric oxide donor, or intravascular superoxide dismutase evidence_span: {"source_cache": "artifacts/hbot-research/11139368.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9823a7f177483257b812d7c8c8e8052c3f04d6a7aa052876369c7c64b55668f3", "start_char": 0, "end_char": 1672, "text_sha256": "9823a7f177483257b812d7c8c8e8052c3f04d6a7aa052876369c7c64b55668f3"} [hbot-p11139368] Hyperbaric oxygen reduces cerebral blood flow by inactivating nitric oxide. (2000). https://pubmed.ncbi.nlm.nih.gov/11139368/ DOI: 10.1006/niox.2000.0313

evidence_access

Primary abstract and publisher methods/results

experimental_model

Cell-free mammalian TrxR study.

limitations

This does not show that lowering oxygen or adding antioxidants benefits patients.

nutrient_topic

Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin

plain_language

Oxygen chemistry changes the inhibitory response.

primary_references

Inhibition of Mammalian thioredoxin reductase by some flavonoids: implications for myricetin and quercetin anticancer activity. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16618767/ · DOI 10.1158/0008-5472.CAN-05-3310

Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 268–274

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free mammalian TrxR study. · source_derived_draft · unverified_draft

## myricetin-txnrd-oxygen Oxygen chemistry changes the inhibitory response. Superoxide enhanced myricetin-mediated TrxR inhibition, while anaerobic conditions attenuated it. Model: Cell-free mammalian TrxR study. Limitations: This does not show that lowering oxygen or adding antioxidants benefits patients. Evidence access: Primary abstract and publisher methods/results Inhibition of Mammalian thioredoxin reductase by some flavonoids: implications for myricetin and quercetin anticancer activity. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16618767/ · DOI 10.1158/0008-5472.CAN-05-3310

evidence_access

Primary abstract

experimental_model

Bovine enzyme assays.

limitations

Does not establish antioxidant benefit across tissues.

nutrient_topic

Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone

plain_language

Blocking the enzyme also reduced its radical output.

primary_references

Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123

Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 292–298

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Bovine enzyme assays. · source_derived_draft · unverified_draft

## luteolin-xo-superoxide Blocking the enzyme also reduced its radical output. Luteolin reduced superoxide production by purified bovine xanthine oxidase. Model: Bovine enzyme assays. Limitations: Does not establish antioxidant benefit across tissues. Evidence access: Primary abstract Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123

experimental_model

In-vitro polymorphonuclear leukocytes; tested drug concentrations reported as 10 micromolar–millimolar.

exposure_category

Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.

limitations

Assay effects do not identify a unique molecular target or establish universal antioxidant action.

nutrient_topic

Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide

plain_language

The effect did not extend to every oxidant.

primary_references

Effects of potassium iodide, colchicine and dapsone on the generation of polymorphonuclear leukocyte-derived oxygen intermediates. · 1982 · https://pubmed.ncbi.nlm.nih.gov/7104217/ · DOI 10.1111/j.1365-2133.1982.tb00340.x

Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 304–310

AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · In-vitro polymorphonuclear leukocytes; tested drug concentrations reported as 10 micromolar–millimolar. · source_derived_draft · unverified_draft

## ki-pmn-superoxide-null The effect did not extend to every oxidant. KI did not suppress superoxide generation in the same study. Model: In-vitro polymorphonuclear leukocytes; tested drug concentrations reported as 10 micromolar–millimolar. Limitations: Assay effects do not identify a unique molecular target or establish universal antioxidant action. Evidence location: Primary abstract Effects of potassium iodide, colchicine and dapsone on the generation of polymorphonuclear leukocyte-derived oxygen intermediates. · 1982 · https://pubmed.ncbi.nlm.nih.gov/7104217/ · DOI 10.1111/j.1365-2133.1982.tb00340.x

acting_entity

s-allylcysteine

dose

Assay-specific millimolar IC50 values

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC concentration series versus corresponding reference scavengers

experimental_model

Reactive-species scavenging systems

interpretation_status

Source-derived research curation; not independent primary verification

limitations

Assay potency is not an achieved human tissue concentration.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Cell-free chemical assays

plain_language

Direct chemistry has a measured concentration requirement.

primary_references

[17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002

route

In vitro

tissue_or_cell_type

Reactive-species scavenging systems

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 59–66

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reactive-species scavenging systems · source_derived_draft · unverified_draft

## s-allylcysteine-scavenging-superoxide Direct chemistry has a measured concentration requirement. SAC scavenged superoxide radical anion in the tested chemical system; IC50 was 14.49 mM. Model: Reactive-species scavenging systems Limitations: Assay potency is not an achieved human tissue concentration. Evidence access: Primary abstract [17576034] S-allylcysteine scavenges singlet oxygen and hypochlorous acid and protects LLC-PK(1) cells of potassium dichromate-induced toxicity. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17576034/ · DOI 10.1016/j.fct.2007.05.002 Structured context: {"organism": "Cell-free chemical assays", "tissue_or_cell_type": "Reactive-species scavenging systems", "dose": "Assay-specific millimolar IC50 values", "duration": "Not specified in accessed abstract", "route": "In vitro", "experimental_comparison": "SAC concentration series versus corresponding reference scavengers", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

evidence_span

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experimental_model

Recombinant human XDH variants with urate, superoxide and NO assays

exposure

Xanthine, oxygen and inorganic nitrite assays

limitations

The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

The enzyme can generate oxidants as well as carry out purine breakdown.

primary_references

[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

tissue_or_cell_type

Purified human enzyme

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 781–792

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft

### mo-xor-oxygen In its oxidase activity, XOR can generate superoxide and hydrogen peroxide rather than exclusively transferring electrons to NAD+. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme can generate oxidants as well as carry out purine breakdown. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

evidence_span

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experimental_model

ESR spin trapping, spectrophotometry and tissue-homogenate oxidation

exposure

Nasunin isolated from Chouja eggplant; 1 micromolar homogenate experiment

limitations

Homogenates do not establish brain entry or neuronal protection after oral intake. SOD-equivalent units are assay calibration, not SOD induction.

nutrient_topic

Nasunin research collection; topical membership is not evidence of a direct dietary effect. · Nasunin

organism

Cell-free chemistry and rat brain homogenates

plain_language

This chemical assay compares activity; it does not mean more SOD enzyme was made.

primary_references

[nasunin-p10100509] Antioxidant activity of nasunin, an anthocyanin in eggplant. (1998). https://pubmed.ncbi.nlm.nih.gov/10100509/

tissue_or_cell_type

Iron complex formation and lipid oxidation

Nasunin: identity, redox chemistry and nutrient connections (2026-09-17) · lines 549–560

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · ESR spin trapping, spectrophotometry and tissue-homogenate oxidation · source_derived_draft · unverified_draft

### nasunin-superoxide-scavenging ESR measured superoxide scavenging at 143 +/- 8 SOD-equivalent units per mg. Condition category: normal nutrient_topic: Nasunin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This chemical assay compares activity; it does not mean more SOD enzyme was made. organism: Cell-free chemistry and rat brain homogenates tissue_or_cell_type: Iron complex formation and lipid oxidation experimental_model: ESR spin trapping, spectrophotometry and tissue-homogenate oxidation limitations: Homogenates do not establish brain entry or neuronal protection after oral intake. SOD-equivalent units are assay calibration, not SOD induction. exposure: Nasunin isolated from Chouja eggplant; 1 micromolar homogenate experiment evidence_span: {"source_cache": "artifacts/nasunin-research/10100509.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c9b0aa305d8c03dd6b8fe8c1fae505dc50b3347a43c00387e01d4e36ecd04c09", "start_char": 0, "end_char": 1400, "text_sha256": "c9b0aa305d8c03dd6b8fe8c1fae505dc50b3347a43c00387e01d4e36ecd04c09"} [nasunin-p10100509] Antioxidant activity of nasunin, an anthocyanin in eggplant. (1998). https://pubmed.ncbi.nlm.nih.gov/10100509/

evidence_span

{"source_cache": "artifacts/sodium-research/32728214.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1", "start_char": 0, "end_char": 1533, "text_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1"}

experimental_model

Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays

exposure

Acute hypoxia and inhibition of mitochondrial sodium/calcium exchange

limitations

Mechanistic research under hypoxia, including multiple preparations. Do not infer that dietary salt drives this chain, that every tissue responds identically, or that ROS here proves disease.

nutrient_topic

Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium

organism

Human and mouse cells; additional rat vascular experiments in the paper

plain_language

A sodium-linked membrane effect contributed to a mitochondrial redox signal.

primary_references

[sodium-p32728214] Na+ controls hypoxic signalling by the mitochondrial respiratory chain. (2020). https://pubmed.ncbi.nlm.nih.gov/32728214/ DOI: 10.1038/s41586-020-2551-y

tissue_or_cell_type

Mitochondrial matrix and inner membrane

Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 811–822

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays · source_derived_draft · unverified_draft

### sodium-complex3-ros The pathway produced complex III superoxide; inhibiting mitochondrial sodium import blocked the response. Condition category: normal nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sodium-linked membrane effect contributed to a mitochondrial redox signal. organism: Human and mouse cells; additional rat vascular experiments in the paper tissue_or_cell_type: Mitochondrial matrix and inner membrane experimental_model: Acute-hypoxia cellular and mitochondrial experiments with ion imaging and respiratory/membrane assays limitations: Mechanistic research under hypoxia, including multiple preparations. Do not infer that dietary salt drives this chain, that every tissue responds identically, or that ROS here proves disease. exposure: Acute hypoxia and inhibition of mitochondrial sodium/calcium exchange evidence_span: {"source_cache": "artifacts/sodium-research/32728214.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1", "start_char": 0, "end_char": 1533, "text_sha256": "2780431aa362c99c816f986e923fd65ed0c0324e8c8674af8ff2a2f9367762c1"} [sodium-p32728214] Na+ controls hypoxic signalling by the mitochondrial respiratory chain. (2020). https://pubmed.ncbi.nlm.nih.gov/32728214/ DOI: 10.1038/s41586-020-2551-y

evidence_span

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experimental_model

Differentiated HL-60 neutrophil-like cells across normoxia, hypoxia, hyperoxia, pressure alone and hyperbaric oxygen

exposure

97.9% oxygen at 2.4 ATA for 90 minutes, with hyperbaric normoxia as a pressure control

limitations

A cell-line model of the neutrophil with a pressure control. The authors report that both hyperoxia and pressure contributed, without a consistent pattern.

nutrient_topic

Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy

organism

Human cell line

plain_language

The cells that kill bacteria did so more strongly after a session.

primary_references

[hbot-p23770209] Effects of hyperbaric oxygen treatment on antimicrobial function and apoptosis of differentiated HL-60 (neutrophil-like) cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23770209/ DOI: 10.1016/j.lfs.2013.06.003

tissue_or_cell_type

Neutrophil-like cells

Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 1037–1048

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Differentiated HL-60 neutrophil-like cells across normoxia, hypoxia, hyperoxia, pressure alone and hyperbaric oxygen · source_derived_draft · unverified_draft

### hbot-respiratory-burst-increase A single 90-minute exposure increased the respiratory burst activity of neutrophil-like cells after exposure, and phagocytosis of Staphylococcus aureus was also increased. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The cells that kill bacteria did so more strongly after a session. organism: Human cell line tissue_or_cell_type: Neutrophil-like cells experimental_model: Differentiated HL-60 neutrophil-like cells across normoxia, hypoxia, hyperoxia, pressure alone and hyperbaric oxygen limitations: A cell-line model of the neutrophil with a pressure control. The authors report that both hyperoxia and pressure contributed, without a consistent pattern. exposure: 97.9% oxygen at 2.4 ATA for 90 minutes, with hyperbaric normoxia as a pressure control evidence_span: {"source_cache": "artifacts/hbot-research/23770209.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1621131d902e359cb8c23a51c1d76596ddff036697818a1613e68b26095eed8a", "start_char": 0, "end_char": 1709, "text_sha256": "1621131d902e359cb8c23a51c1d76596ddff036697818a1613e68b26095eed8a"} [hbot-p23770209] Effects of hyperbaric oxygen treatment on antimicrobial function and apoptosis of differentiated HL-60 (neutrophil-like) cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23770209/ DOI: 10.1016/j.lfs.2013.06.003

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays

exposure

Oxygen at 5 atmospheres absolute for 30 minutes, with L-NAME, a nitric oxide donor, or intravascular superoxide dismutase

limitations

Five atmospheres is well above therapeutic pressure and was chosen to study oxygen toxicity. The superoxide dismutase rescue is the key mechanistic step.

nutrient_topic

Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy

organism

Rat

plain_language

Giving the enzyme that clears superoxide kept the vessels open.

primary_references

[hbot-p11139368] Hyperbaric oxygen reduces cerebral blood flow by inactivating nitric oxide. (2000). https://pubmed.ncbi.nlm.nih.gov/11139368/ DOI: 10.1006/niox.2000.0313

tissue_or_cell_type

Brain

trigger_kind

machinery_impairment Imported condition classification; unverified.

Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 179–190

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays · source_derived_draft · unverified_draft

### hbot-sod-rescue Administration of superoxide dismutase into the circulation before exposure completely abolished the decrease in regional cerebral blood flow at 5 ATA. Condition category: machinery_impairment nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Giving the enzyme that clears superoxide kept the vessels open. organism: Rat tissue_or_cell_type: Brain experimental_model: Regional cerebral blood flow measurement in rats with nitric oxide metabolite and hydroxyl radical assays limitations: Five atmospheres is well above therapeutic pressure and was chosen to study oxygen toxicity. The superoxide dismutase rescue is the key mechanistic step. exposure: Oxygen at 5 atmospheres absolute for 30 minutes, with L-NAME, a nitric oxide donor, or intravascular superoxide dismutase evidence_span: {"source_cache": "artifacts/hbot-research/11139368.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9823a7f177483257b812d7c8c8e8052c3f04d6a7aa052876369c7c64b55668f3", "start_char": 0, "end_char": 1672, "text_sha256": "9823a7f177483257b812d7c8c8e8052c3f04d6a7aa052876369c7c64b55668f3"} [hbot-p11139368] Hyperbaric oxygen reduces cerebral blood flow by inactivating nitric oxide. (2000). https://pubmed.ncbi.nlm.nih.gov/11139368/ DOI: 10.1006/niox.2000.0313

evidence_span

{"source_cache": "artifacts/hbot-research/6316150.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dc20323f9774c6c743e01f8bdbeedbc42b0ddac982f1e17d53a9591b87bf5379", "start_char": 0, "end_char": 867, "text_sha256": "dc20323f9774c6c743e01f8bdbeedbc42b0ddac982f1e17d53a9591b87bf5379"}

experimental_model

Refinement of the 2 angstrom crystal structure of copper, zinc superoxide dismutase with molecular surface analysis

exposure

Structural and mechanistic analysis of the active site

limitations

Structural chemistry. It explains why the enzyme needs its metals; it is not a statement about dietary copper or zinc.

nutrient_topic

Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy

organism

Bovine enzyme structure

plain_language

The copper atom itself is what takes and gives back the electron.

primary_references

[hbot-p6316150] Structure and mechanism of copper, zinc superoxide dismutase. (1983). https://pubmed.ncbi.nlm.nih.gov/6316150/ DOI: 10.1038/306284a0

tissue_or_cell_type

Purified enzyme

Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 491–502

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Refinement of the 2 angstrom crystal structure of copper, zinc superoxide dismutase with molecular surface analysis · source_derived_draft · unverified_draft

### hbot-sod1-copper-mechanism Copper, zinc superoxide dismutase catalyses the two-step dismutation of superoxide to molecular oxygen and hydrogen peroxide through alternate reduction and oxidation of the active-site copper, with a single complementary binding position for superoxide at the Cu(II) and the activity-important Arg141. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The copper atom itself is what takes and gives back the electron. organism: Bovine enzyme structure tissue_or_cell_type: Purified enzyme experimental_model: Refinement of the 2 angstrom crystal structure of copper, zinc superoxide dismutase with molecular surface analysis limitations: Structural chemistry. It explains why the enzyme needs its metals; it is not a statement about dietary copper or zinc. exposure: Structural and mechanistic analysis of the active site evidence_span: {"source_cache": "artifacts/hbot-research/6316150.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dc20323f9774c6c743e01f8bdbeedbc42b0ddac982f1e17d53a9591b87bf5379", "start_char": 0, "end_char": 867, "text_sha256": "dc20323f9774c6c743e01f8bdbeedbc42b0ddac982f1e17d53a9591b87bf5379"} [hbot-p6316150] Structure and mechanism of copper, zinc superoxide dismutase. (1983). https://pubmed.ncbi.nlm.nih.gov/6316150/ DOI: 10.1038/306284a0

experimental_model

Redox-controlled neutron structures of human SOD2

exposure

Redox-controlled Mn(III) and Mn(II) crystals

limitations

Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.

nutrient_topic

Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese

organism

Homo sapiens

plain_language

SOD2 removes superoxide; it produces hydrogen peroxide that requires further handling.

primary_references

[mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1

tissue_or_cell_type

Purified enzyme; mitochondrial-matrix protein

Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 446–456

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Redox-controlled neutron structures of human SOD2 · source_derived_draft · unverified_draft

### mn-enz-sod2-superoxide Human SOD2 uses a Mn(III)/Mn(II) cycle to convert superoxide into oxygen and hydrogen peroxide. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: SOD2 removes superoxide; it produces hydrogen peroxide that requires further handling. organism: Homo sapiens tissue_or_cell_type: Purified enzyme; mitochondrial-matrix protein experimental_model: Redox-controlled neutron structures of human SOD2 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Redox-controlled Mn(III) and Mn(II) crystals [mn-enz-33824320] Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. (2021). https://pubmed.ncbi.nlm.nih.gov/33824320/ DOI: 10.1038/s41467-021-22290-1

evidence_span

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experimental_model

Recombinant human XDH variants with urate, superoxide and NO assays

exposure

Xanthine, oxygen and inorganic nitrite assays

limitations

The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

One variant raised several outputs at once.

primary_references

[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

tissue_or_cell_type

Purified human enzyme

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 807–818

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft

### mo-xor-h1221r His1221Arg increased urate, superoxide and NO formation relative to wild type in xanthine-supplied assays. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: One variant raised several outputs at once. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

evidence_span

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experimental_model

Recombinant human XDH variants with urate, superoxide and NO assays

exposure

Xanthine, oxygen and inorganic nitrite assays

limitations

The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

Another variant changed the balance of products differently.

primary_references

[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

tissue_or_cell_type

Purified human enzyme

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 820–831

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft

### mo-xor-i703v Ile703Val increased urate and NO formation without increasing superoxide formation in the reported comparison. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another variant changed the balance of products differently. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

evidence_span

{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}

experimental_model

Recombinant human XDH variants with urate, superoxide and NO assays

exposure

Xanthine, oxygen and inorganic nitrite assays

limitations

The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

Changing the available electron acceptor changed the products.

primary_references

[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

tissue_or_cell_type

Purified human enzyme

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 794–805

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft

### mo-xor-nitrite Human XOR reduced nitrite to NO under the tested reducing conditions, and nitrite decreased XOR-driven superoxide production. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing the available electron acceptor changed the products. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864

evidence_access

Primary abstract

experimental_model

Human neutrophils after 400 or 600 mg/day for one week, or 400 mg/day for two weeks; ex-vivo binding and NECA challenges.

limitations

Adapted cells were challenged with an agonist; this is not the same as an immediate effect of caffeine, nor a clinical anti-inflammatory trial.

nutrient_topic

Caffeine collection; salts, coffee, species and coexposure contexts retain their identities. · Caffeine

plain_language

The immune-cell response was reversible and depended on the agonist challenge.

primary_references

Caffeine intake induces an alteration in human neutrophil A2A adenosine receptors. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16143823/ · DOI 10.1007/s00018-005-5312-z

Caffeine: receptors, metabolism, nutrient interactions, adaptation and discovery questions (2026-09-18) · lines 164–170

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human neutrophils after 400 or 600 mg/day for one week, or 400 mg/day for two weeks; ex-vivo binding and NECA challenges. · source_derived_draft · unverified_draft

## caf-neutrophil-superoxide The immune-cell response was reversible and depended on the agonist challenge. NECA-stimulated adapted neutrophils showed lower superoxide production; binding and functional changes returned to baseline after 48 hours withdrawal. Model: Human neutrophils after 400 or 600 mg/day for one week, or 400 mg/day for two weeks; ex-vivo binding and NECA challenges. Limitations: Adapted cells were challenged with an agonist; this is not the same as an immediate effect of caffeine, nor a clinical anti-inflammatory trial. Evidence access: Primary abstract Caffeine intake induces an alteration in human neutrophil A2A adenosine receptors. · 2005 · https://pubmed.ncbi.nlm.nih.gov/16143823/ · DOI 10.1007/s00018-005-5312-z