Component

Dopamine

Dopamine

13 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.

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.

Recorded relationships

What acts on it

  1. Expressed human DDC decarboxylated L-DOPA; added PLP enhanced the measured activity.

    Experimental context and source evidence
    experimental_model
    Human DDC expressed in monkey COS cells; enzyme assays
    exposure
    PLP addition to transfected COS-cell enzyme incubations.
    limitations
    An expression-system response is not proof that supplements increase brain monoamines.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Human DDC expressed in monkey COS cells
    plain_language
    B6 cofactor supports this monoamine-producing step.
    primary_references
    [sumi-1990-ddc] Characterization of recombinant human aromatic L-amino acid decarboxylase expressed in COS cells (1990). https://doi.org/10.1111/j.1471-4159.1990.tb04601.x DOI: 10.1111/j.1471-4159.1990.tb04601.x
    tissue_or_cell_type
    COS-cell expression system

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 999–1009

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human DDC expressed in monkey COS cells; enzyme assays · source_derived_draft · unverified_draft

    ### b6-neuro-ddc-dopamine Expressed human DDC decarboxylated L-DOPA; added PLP enhanced the measured activity. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: B6 cofactor supports this monoamine-producing step. organism: Human DDC expressed in monkey COS cells tissue_or_cell_type: COS-cell expression system experimental_model: Human DDC expressed in monkey COS cells; enzyme assays limitations: An expression-system response is not proof that supplements increase brain monoamines. exposure: PLP addition to transfected COS-cell enzyme incubations. [sumi-1990-ddc] Characterization of recombinant human aromatic L-amino acid decarboxylase expressed in COS cells (1990). https://doi.org/10.1111/j.1471-4159.1990.tb04601.x DOI: 10.1111/j.1471-4159.1990.tb04601.x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human DBH is the copper-enzyme step converting dopamine to norepinephrine; the study resolved its catalytic-core architecture.

    Human dopamine beta-hydroxylase / DBH → Norepinephrine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/27152332.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09", "start_char": 0, "end_char": 1325, "text_sha256": "984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09"}
    experimental_model
    Human DBH X-ray crystallography
    exposure
    Crystal structure at 2.9 angstrom resolution
    limitations
    Open and closed conformations were observed; the proposed catalytic alternation and fully occupied binuclear states require further evidence. Do not equate a structural model with proof of psychiatric effects from copper intake.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human protein
    plain_language
    Copper is part of the enzyme that converts one neurotransmitter into another.
    primary_references
    [copper-p27152332] The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution. (2016). https://pubmed.ncbi.nlm.nih.gov/27152332/ DOI: 10.1126/sciadv.1500980
    tissue_or_cell_type
    Purified dimeric enzyme

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1079–1090

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human DBH X-ray crystallography · source_derived_draft · unverified_draft

    ### copper-dbh-neurotransmitter-step Human DBH is the copper-enzyme step converting dopamine to norepinephrine; the study resolved its catalytic-core architecture. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Copper is part of the enzyme that converts one neurotransmitter into another. organism: Human protein tissue_or_cell_type: Purified dimeric enzyme experimental_model: Human DBH X-ray crystallography limitations: Open and closed conformations were observed; the proposed catalytic alternation and fully occupied binuclear states require further evidence. Do not equate a structural model with proof of psychiatric effects from copper intake. exposure: Crystal structure at 2.9 angstrom resolution evidence_span: {"source_cache": "artifacts/copper-research/27152332.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09", "start_char": 0, "end_char": 1325, "text_sha256": "984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09"} [copper-p27152332] The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution. (2016). https://pubmed.ncbi.nlm.nih.gov/27152332/ DOI: 10.1126/sciadv.1500980
    Complete structured claim and evidence
  2. Bacterial tyrosine decarboxylases converted levodopa to dopamine despite competing tyrosine or human decarboxylase inhibitors.

    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies.
    limitations
    Patient abundance associations and rat plasma effects are not proof that changing dietary tyrosine improves levodopa response.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Blocking the human enzyme may leave a microbial route active.
    primary_references
    Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 340–346

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies. · source_derived_draft · unverified_draft

    ## l-tyrosine-bacterial-drug Blocking the human enzyme may leave a microbial route active. Bacterial tyrosine decarboxylases converted levodopa to dopamine despite competing tyrosine or human decarboxylase inhibitors. Model: Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies. Limitations: Patient abundance associations and rat plasma effects are not proof that changing dietary tyrosine improves levodopa response. Evidence access: Primary abstract Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y
    Complete structured claim and evidence
  3. Combined phenylalanine/tyrosine depletion decreased dopamine-transient frequency without decreasing transient amplitude in freely moving rats.

    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Fast-scan cyclic voltammetry in a separate rat group from the tissue-content experiment.
    limitations
    The release endpoint is not a direct human measurement; the corrected norepinephrine endpoint is excluded. Correction record: The 2018 correction (PMID 30094500) reports an error in norepinephrine standard concentrations used for HPLC calibration. The correction abstract was inspected, but full notice content was unavailable; its complete quantitative scope remains unverified. This collection uses the tyrosine depletion and dopamine-transient findings and does not reuse the original norepinephrine concentration result. https://pubmed.ncbi.nlm.nih.gov/30094500/
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Less precursor can change release dynamics without simply emptying all dopamine stores.
    primary_references
    Acute phenylalanine/tyrosine depletion of phasic dopamine in the rat brain. · 2016 · https://pubmed.ncbi.nlm.nih.gov/26944052/ · DOI 10.1007/s00213-016-4259-0
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 388–394

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Fast-scan cyclic voltammetry in a separate rat group from the tissue-content experiment. · source_derived_draft · unverified_draft

    ## l-tyrosine-rat-dopamine-transients Less precursor can change release dynamics without simply emptying all dopamine stores. Combined phenylalanine/tyrosine depletion decreased dopamine-transient frequency without decreasing transient amplitude in freely moving rats. Model: Fast-scan cyclic voltammetry in a separate rat group from the tissue-content experiment. Limitations: The release endpoint is not a direct human measurement; the corrected norepinephrine endpoint is excluded. Correction record: The 2018 correction (PMID 30094500) reports an error in norepinephrine standard concentrations used for HPLC calibration. The correction abstract was inspected, but full notice content was unavailable; its complete quantitative scope remains unverified. This collection uses the tyrosine depletion and dopamine-transient findings and does not reuse the original norepinephrine concentration result. https://pubmed.ncbi.nlm.nih.gov/30094500/ Evidence access: Primary abstract Acute phenylalanine/tyrosine depletion of phasic dopamine in the rat brain. · 2016 · https://pubmed.ncbi.nlm.nih.gov/26944052/ · DOI 10.1007/s00213-016-4259-0
    Complete structured claim and evidence
  4. Tartrazine inhibited dopamine sulfation in human liver cytosol.

    Tartrazine → Dopamine sulfation by human liver cytosol source_derived_draftungraded
    Experimental context and source evidence
    dose
    Tartrazine in an additive-inhibition panel; concentration and substrate amounts not in abstract
    duration
    Assay interval not specified in accessed abstract
    evidence_access
    Primary PubMed abstract; unrecovered method details explicitly retained.
    evidence_scope
    literature_reviewed; source-specific experimental curation
    experimental_model
    Human liver cytosolic preparations
    limitations
    A functional sulfation assay does not demonstrate direct SULT1A3 binding or altered human brain dopamine. Ethinyloestradiol findings for other additives are not transferred to tartrazine.
    nutrient_topic
    Tartrazine food-colorant chapter; nutrient, drug and peptide interactions retain their models and limits. · Tartrazine
    organism
    Human liver cytosolic preparations
    plain_language
    Tartrazine inhibited dopamine sulfation in human liver cytosol.
    primary_references
    Common food additives are potent inhibitors of human liver 17 alpha-ethinyloestradiol and dopamine sulphotransferases. (1993). https://pubmed.ncbi.nlm.nih.gov/8250957/ DOI: 10.1016/0006-2952(93)90575-h
    route
    In vitro cytosolic enzyme assay
    tissue
    Dopamine sulfation

    Tartrazine: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 259–268

    Original AI-assisted curation of eighteen primary studies. Study-specific citations, negative findings and limitations retained. Not publisher full text. · supports · Human liver cytosolic preparations · source_derived_draft · unverified_draft

    ## tartrazine-dopamine-sulfation Tartrazine inhibited dopamine sulfation in human liver cytosol. Model/species: Human liver cytosolic preparations Tissue: Dopamine sulfation Exposure: Tartrazine in an additive-inhibition panel; concentration and substrate amounts not in abstract Route: In vitro cytosolic enzyme assay Duration: Assay interval not specified in accessed abstract Limits: A functional sulfation assay does not demonstrate direct SULT1A3 binding or altered human brain dopamine. Ethinyloestradiol findings for other additives are not transferred to tartrazine. Primary reference: Common food additives are potent inhibitors of human liver 17 alpha-ethinyloestradiol and dopamine sulphotransferases. (1993). https://pubmed.ncbi.nlm.nih.gov/8250957/ DOI: 10.1016/0006-2952(93)90575-h Access: Primary PubMed abstract; unrecovered method details explicitly retained.
    Complete structured claim and evidence
  5. Theanine protected SH-SY5Y cells against the injury produced by dopamine plus copper.

    L-Theanine → Dopamine-associated cultured-cell injury source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/theanine-research/39499422.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4", "start_char": 0, "end_char": 1871, "text_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4"}
    experimental_model
    Cell-free oxidation and cultured-cell injury assays
    exposure
    Dopamine with and without copper; theanine concentration-ratio experiments
    limitations
    High experimental substrate ratios; no human copper-depletion, Parkinson disease treatment or systemic chelation conclusion. Cellular protection does not establish effective brain exposure.
    nutrient_topic
    L-Theanine research collection; topical membership is not evidence of a direct dietary effect. · L-Theanine
    organism
    Human SH-SY5Y cell line and chemical systems
    plain_language
    Cell survival was measured separately from the chemical oxidation assay.
    primary_references
    [theanine-p39499422] L-Theanine Effectively Protects Against Copper-Facilitated Dopamine Oxidation: Implication for Relieving Dopamine Overflow-Associated Neurotoxicities. (2025). https://pubmed.ncbi.nlm.nih.gov/39499422/ DOI: 10.1007/s12035-024-04601-x
    tissue_or_cell_type
    Copper-facilitated dopamine oxidation

    L-Theanine: metabolism, neural signaling, nutrient connections and human outcomes (2026-09-17) · lines 744–755

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell-free oxidation and cultured-cell injury assays · source_derived_draft · unverified_draft

    ### theanine-copper-cell-protection Theanine protected SH-SY5Y cells against the injury produced by dopamine plus copper. Condition category: normal nutrient_topic: L-Theanine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cell survival was measured separately from the chemical oxidation assay. organism: Human SH-SY5Y cell line and chemical systems tissue_or_cell_type: Copper-facilitated dopamine oxidation experimental_model: Cell-free oxidation and cultured-cell injury assays limitations: High experimental substrate ratios; no human copper-depletion, Parkinson disease treatment or systemic chelation conclusion. Cellular protection does not establish effective brain exposure. exposure: Dopamine with and without copper; theanine concentration-ratio experiments evidence_span: {"source_cache": "artifacts/theanine-research/39499422.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4", "start_char": 0, "end_char": 1871, "text_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4"} [theanine-p39499422] L-Theanine Effectively Protects Against Copper-Facilitated Dopamine Oxidation: Implication for Relieving Dopamine Overflow-Associated Neurotoxicities. (2025). https://pubmed.ncbi.nlm.nih.gov/39499422/ DOI: 10.1007/s12035-024-04601-x
    Complete structured claim and evidence
  6. Theanine suppressed copper-facilitated dopamine oxidation; the authors attributed this to copper chelation.

    L-Theanine → Copper-facilitated dopamine oxidation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/theanine-research/39499422.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4", "start_char": 0, "end_char": 1871, "text_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4"}
    experimental_model
    Cell-free oxidation and cultured-cell injury assays
    exposure
    Dopamine with and without copper; theanine concentration-ratio experiments
    limitations
    High experimental substrate ratios; no human copper-depletion, Parkinson disease treatment or systemic chelation conclusion. Cellular protection does not establish effective brain exposure.
    nutrient_topic
    L-Theanine research collection; topical membership is not evidence of a direct dietary effect. · L-Theanine
    organism
    Human SH-SY5Y cell line and chemical systems
    plain_language
    Copper changed the chemistry of dopamine oxidation, and theanine interfered with that chemistry in the assay.
    primary_references
    [theanine-p39499422] L-Theanine Effectively Protects Against Copper-Facilitated Dopamine Oxidation: Implication for Relieving Dopamine Overflow-Associated Neurotoxicities. (2025). https://pubmed.ncbi.nlm.nih.gov/39499422/ DOI: 10.1007/s12035-024-04601-x
    tissue_or_cell_type
    Copper-facilitated dopamine oxidation

    L-Theanine: metabolism, neural signaling, nutrient connections and human outcomes (2026-09-17) · lines 731–742

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell-free oxidation and cultured-cell injury assays · source_derived_draft · unverified_draft

    ### theanine-copper-dopamine-oxidation Theanine suppressed copper-facilitated dopamine oxidation; the authors attributed this to copper chelation. Condition category: normal nutrient_topic: L-Theanine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Copper changed the chemistry of dopamine oxidation, and theanine interfered with that chemistry in the assay. organism: Human SH-SY5Y cell line and chemical systems tissue_or_cell_type: Copper-facilitated dopamine oxidation experimental_model: Cell-free oxidation and cultured-cell injury assays limitations: High experimental substrate ratios; no human copper-depletion, Parkinson disease treatment or systemic chelation conclusion. Cellular protection does not establish effective brain exposure. exposure: Dopamine with and without copper; theanine concentration-ratio experiments evidence_span: {"source_cache": "artifacts/theanine-research/39499422.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4", "start_char": 0, "end_char": 1871, "text_sha256": "abb7a869056bc8c43d6792b2a4ff9a1b15738facf454daeb3f92df383932b9c4"} [theanine-p39499422] L-Theanine Effectively Protects Against Copper-Facilitated Dopamine Oxidation: Implication for Relieving Dopamine Overflow-Associated Neurotoxicities. (2025). https://pubmed.ncbi.nlm.nih.gov/39499422/ DOI: 10.1007/s12035-024-04601-x
    Complete structured claim and evidence
  7. Strychnine reduced the theanine-induced dopamine response in rat striatum.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/theanine-research/18196445.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "59fdaf94d59c2f4b2981c29cd2981c043351aae1299a59a19e29979076957839", "start_char": 0, "end_char": 1118, "text_sha256": "59fdaf94d59c2f4b2981c29cd2981c043351aae1299a59a19e29979076957839"}
    experimental_model
    In-vivo striatal microdialysis with receptor antagonists
    exposure
    Local brain theanine administration; glycine and AMPA antagonists
    limitations
    Direct brain dosing bypasses oral absorption and blood-brain-barrier transport. Antagonist sensitivity identifies pathway involvement, not necessarily direct theanine binding.
    nutrient_topic
    L-Theanine research collection; topical membership is not evidence of a direct dietary effect. · L-Theanine
    organism
    Conscious rats
    plain_language
    The glycine-receptor pathway participated in the dopamine response.
    primary_references
    [theanine-p18196445] Theanine, gamma-glutamylethylamide, a unique amino acid in tea leaves, modulates neurotransmitter concentrations in the brain striatum interstitium in conscious rats. (2009). https://pubmed.ncbi.nlm.nih.gov/18196445/ DOI: 10.1007/s00726-007-0020-7
    tissue_or_cell_type
    Striatal extracellular neurotransmitters

    L-Theanine: metabolism, neural signaling, nutrient connections and human outcomes (2026-09-17) · lines 380–391

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In-vivo striatal microdialysis with receptor antagonists · source_derived_draft · unverified_draft

    ### theanine-glycine-dopamine Strychnine reduced the theanine-induced dopamine response in rat striatum. Condition category: normal nutrient_topic: L-Theanine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The glycine-receptor pathway participated in the dopamine response. organism: Conscious rats tissue_or_cell_type: Striatal extracellular neurotransmitters experimental_model: In-vivo striatal microdialysis with receptor antagonists limitations: Direct brain dosing bypasses oral absorption and blood-brain-barrier transport. Antagonist sensitivity identifies pathway involvement, not necessarily direct theanine binding. exposure: Local brain theanine administration; glycine and AMPA antagonists evidence_span: {"source_cache": "artifacts/theanine-research/18196445.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "59fdaf94d59c2f4b2981c29cd2981c043351aae1299a59a19e29979076957839", "start_char": 0, "end_char": 1118, "text_sha256": "59fdaf94d59c2f4b2981c29cd2981c043351aae1299a59a19e29979076957839"} [theanine-p18196445] Theanine, gamma-glutamylethylamide, a unique amino acid in tea leaves, modulates neurotransmitter concentrations in the brain striatum interstitium in conscious rats. (2009). https://pubmed.ncbi.nlm.nih.gov/18196445/ DOI: 10.1007/s00726-007-0020-7
    Complete structured claim and evidence
  8. Ascorbate is the presumed in vivo reductant of dopamine beta-monooxygenase; the one-electron reductant ferrocyanide was nearly as kinetically competent, while dopamine as sole reductant reduced enzymic copper in a rate-limiting step 40-fold slower than with ascorbate, and the reductant binds at a site physically distinct from the substrate site.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/cold-research/3676254.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e929132eed0f1c94ab0bdbef6e31bca7ecbed222cf9b585e17a1cfae7e93c82a", "start_char": 0, "end_char": 1648, "text_sha256": "e929132eed0f1c94ab0bdbef6e31bca7ecbed222cf9b585e17a1cfae7e93c82a"}
    experimental_model
    Steady-state kinetics of dopamine beta-monooxygenase with structurally distinct reductants
    exposure
    Ascorbate, ferrocyanide or dopamine itself as the reducing agent, with deuterium isotope effects
    limitations
    A kinetic comparison identifying ascorbate as the presumed physiological reductant and locating a separate binding site for it. Truncated abstract; the reductant site is inferred from kinetics and modelling.
    nutrient_topic
    Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Cold water immersion
    organism
    Bovine enzyme
    plain_language
    Vitamin C is what hands the enzyme back its electrons, and without it the reaction crawls.
    primary_references
    [cold-p3676254] Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction. (1987). https://pubmed.ncbi.nlm.nih.gov/3676254/ DOI: 10.1021/bi00391a013
    tissue_or_cell_type
    Purified enzyme

    Cold water immersion: cold sensing, heat production, the catecholamine axis and what repeated exposure changes (2026-09-19) · lines 585–596

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Steady-state kinetics of dopamine beta-monooxygenase with structurally distinct reductants · source_derived_draft · unverified_draft

    ### cold-ascorbate-reductant Ascorbate is the presumed in vivo reductant of dopamine beta-monooxygenase; the one-electron reductant ferrocyanide was nearly as kinetically competent, while dopamine as sole reductant reduced enzymic copper in a rate-limiting step 40-fold slower than with ascorbate, and the reductant binds at a site physically distinct from the substrate site. Condition category: normal nutrient_topic: Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Vitamin C is what hands the enzyme back its electrons, and without it the reaction crawls. organism: Bovine enzyme tissue_or_cell_type: Purified enzyme experimental_model: Steady-state kinetics of dopamine beta-monooxygenase with structurally distinct reductants limitations: A kinetic comparison identifying ascorbate as the presumed physiological reductant and locating a separate binding site for it. Truncated abstract; the reductant site is inferred from kinetics and modelling. exposure: Ascorbate, ferrocyanide or dopamine itself as the reducing agent, with deuterium isotope effects evidence_span: {"source_cache": "artifacts/cold-research/3676254.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e929132eed0f1c94ab0bdbef6e31bca7ecbed222cf9b585e17a1cfae7e93c82a", "start_char": 0, "end_char": 1648, "text_sha256": "e929132eed0f1c94ab0bdbef6e31bca7ecbed222cf9b585e17a1cfae7e93c82a"} [cold-p3676254] Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction. (1987). https://pubmed.ncbi.nlm.nih.gov/3676254/ DOI: 10.1021/bi00391a013
    Complete structured claim and evidence
  9. Dopamine beta-hydroxylase specifically binds 8 moles of copper per mole of tetramer, confirmed by radiolabel, atomic absorption, NMR and EPR titration, and catalytic rate increased with copper up to that ratio and was constant thereafter, so this stoichiometry is required for maximal activity.

    Copper → Dopamine beta-hydroxylase catalytic turnover source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/cold-research/6323422.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dac85ce0ad7c7d5994b97d55b129050a0e7ca8bf96943578d272054db6a07a62", "start_char": 0, "end_char": 1346, "text_sha256": "dac85ce0ad7c7d5994b97d55b129050a0e7ca8bf96943578d272054db6a07a62"}
    experimental_model
    Copper titration of bovine adrenal dopamine beta-hydroxylase followed by NMR, EPR and inhibitor kinetics
    exposure
    Titration with copper and measurement of catalytic rate
    limitations
    Stoichiometry measured three independent ways. It establishes how much copper the enzyme needs, not how much copper a person needs.
    nutrient_topic
    Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Cold water immersion
    organism
    Bovine enzyme
    plain_language
    The enzyme that turns dopamine into noradrenaline needs exactly eight copper atoms to work fully.
    primary_references
    [cold-p6323422] Kinetic and spectroscopic studies of the interaction of copper with dopamine beta-hydroxylase. (1984). https://pubmed.ncbi.nlm.nih.gov/6323422/ DOI: 10.1016/s0021-9258(17)43105-x
    tissue_or_cell_type
    Adrenal medulla enzyme

    Cold water immersion: cold sensing, heat production, the catecholamine axis and what repeated exposure changes (2026-09-19) · lines 559–570

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Copper titration of bovine adrenal dopamine beta-hydroxylase followed by NMR, EPR and inhibitor kinetics · source_derived_draft · unverified_draft

    ### cold-dbh-copper-stoichiometry Dopamine beta-hydroxylase specifically binds 8 moles of copper per mole of tetramer, confirmed by radiolabel, atomic absorption, NMR and EPR titration, and catalytic rate increased with copper up to that ratio and was constant thereafter, so this stoichiometry is required for maximal activity. Condition category: normal nutrient_topic: Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The enzyme that turns dopamine into noradrenaline needs exactly eight copper atoms to work fully. organism: Bovine enzyme tissue_or_cell_type: Adrenal medulla enzyme experimental_model: Copper titration of bovine adrenal dopamine beta-hydroxylase followed by NMR, EPR and inhibitor kinetics limitations: Stoichiometry measured three independent ways. It establishes how much copper the enzyme needs, not how much copper a person needs. exposure: Titration with copper and measurement of catalytic rate evidence_span: {"source_cache": "artifacts/cold-research/6323422.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dac85ce0ad7c7d5994b97d55b129050a0e7ca8bf96943578d272054db6a07a62", "start_char": 0, "end_char": 1346, "text_sha256": "dac85ce0ad7c7d5994b97d55b129050a0e7ca8bf96943578d272054db6a07a62"} [cold-p6323422] Kinetic and spectroscopic studies of the interaction of copper with dopamine beta-hydroxylase. (1984). https://pubmed.ncbi.nlm.nih.gov/6323422/ DOI: 10.1016/s0021-9258(17)43105-x
    Complete structured claim and evidence
  10. Glutamate co-entry increased vesicular acidification in the study, supporting the pH gradient used for monoamine storage.

    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Rodent synaptic-vesicle acidification assays; glutamate compared with chloride.
    limitations
    The preparation does not show that glutamate supplements increase human dopamine.
    nutrient_topic
    L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
    plain_language
    One transmitter can influence storage of another through shared vesicle chemistry.
    primary_references
    Vesicular glutamate transport promotes dopamine storage and glutamate corelease in vivo. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20223200/ · DOI 10.1016/j.neuron.2010.02.012

    L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 314–320

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rodent synaptic-vesicle acidification assays; glutamate compared with chloride. · source_derived_draft · unverified_draft

    ## glutamate-glutamate-vesicle-acidification One transmitter can influence storage of another through shared vesicle chemistry. Glutamate co-entry increased vesicular acidification in the study, supporting the pH gradient used for monoamine storage. Model: Rodent synaptic-vesicle acidification assays; glutamate compared with chloride. Limitations: The preparation does not show that glutamate supplements increase human dopamine. Evidence access: Primary full text Vesicular glutamate transport promotes dopamine storage and glutamate corelease in vivo. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20223200/ · DOI 10.1016/j.neuron.2010.02.012
    Complete structured claim and evidence
  11. Dopamine-neuron Slc17a6 deletion reduced dopamine stores in ventral-striatal projections and reduced cocaine-stimulated locomotor responses while sparing baseline motor behavior.

    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Mouse conditional knockout with tissue dopamine and behavioral measurements.
    limitations
    Multiple downstream effects coexist; this does not prove every dopamine neuron or behavior depends equally on VGLUT2.
    nutrient_topic
    L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
    plain_language
    Removing the glutamate-loading route changed another transmitter system in a specific circuit.
    primary_references
    Vesicular glutamate transport promotes dopamine storage and glutamate corelease in vivo. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20223200/ · DOI 10.1016/j.neuron.2010.02.012
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 322–328

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse conditional knockout with tissue dopamine and behavioral measurements. · source_derived_draft · unverified_draft

    ## glutamate-vglut2-dopamine-stores Removing the glutamate-loading route changed another transmitter system in a specific circuit. Dopamine-neuron Slc17a6 deletion reduced dopamine stores in ventral-striatal projections and reduced cocaine-stimulated locomotor responses while sparing baseline motor behavior. Model: Mouse conditional knockout with tissue dopamine and behavioral measurements. Limitations: Multiple downstream effects coexist; this does not prove every dopamine neuron or behavior depends equally on VGLUT2. Evidence access: Primary full text Vesicular glutamate transport promotes dopamine storage and glutamate corelease in vivo. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20223200/ · DOI 10.1016/j.neuron.2010.02.012
    Complete structured claim and evidence
  12. Ethanol preferentially stimulated dopamine release in the nucleus accumbens of freely moving rats.

    Ethanol → Dopamine release in the nucleus accumbens source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/alcohol-research/3761194.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca", "start_char": 0, "end_char": 1539, "text_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca"}
    experimental_model
    In vivo microdialysis in freely moving rats
    exposure
    Ethanol administration with regional dopamine measurement
    limitations
    A reward-pathway measurement in freely moving animals. Dopamine release is a correlate of reinforcement, not a measure of liking or dependence.
    nutrient_topic
    Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
    organism
    Rat
    plain_language
    Alcohol raises dopamine in the brain region that marks things as worth repeating.
    primary_references
    [alcohol-p3761194] Preferential stimulation of dopamine release in the nucleus accumbens of freely moving rats by ethanol. (1986). https://pubmed.ncbi.nlm.nih.gov/3761194/ DOI: 10.1016/s0022-3565(25)23929-5
    tissue_or_cell_type
    Nucleus accumbens

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 423–434

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vivo microdialysis in freely moving rats · source_derived_draft · unverified_draft

    ### alcohol-accumbens-dopamine Ethanol preferentially stimulated dopamine release in the nucleus accumbens of freely moving rats. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol raises dopamine in the brain region that marks things as worth repeating. organism: Rat tissue_or_cell_type: Nucleus accumbens experimental_model: In vivo microdialysis in freely moving rats limitations: A reward-pathway measurement in freely moving animals. Dopamine release is a correlate of reinforcement, not a measure of liking or dependence. exposure: Ethanol administration with regional dopamine measurement evidence_span: {"source_cache": "artifacts/alcohol-research/3761194.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca", "start_char": 0, "end_char": 1539, "text_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca"} [alcohol-p3761194] Preferential stimulation of dopamine release in the nucleus accumbens of freely moving rats by ethanol. (1986). https://pubmed.ncbi.nlm.nih.gov/3761194/ DOI: 10.1016/s0022-3565(25)23929-5
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards