Component

Human dopamine beta-hydroxylase / DBH

Human dopamine beta-hydroxylase / DBH. Species, exposure and limitations are retained in each linked claim.

5 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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 it acts on

  1. Human DBH displayed open and closed active-site conformations; the closed structure placed its two copper-binding sites about 4–5 angstroms apart.

    Human dopamine beta-hydroxylase / DBH → Copper 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
    The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study.
    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 1092–1103

    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-copper-site-conformations Human DBH displayed open and closed active-site conformations; the closed structure placed its two copper-binding sites about 4–5 angstroms apart. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study. 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. 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

Where it participates (unsigned role)

  1. Pathogenic CYB561 variants in four patients accompanied very low norepinephrine and epinephrine despite normal plasma DBH activity; impaired intravesicular ascorbate support was the proposed functional block.

    Human cytochrome b561 / CYB561 → Human CYB561-dependent vesicular catecholamine synthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Two human families; genetic analysis with supporting Cyb561 knockout mouse results.
    limitations
    The human defect and mouse corroboration are distinct evidence; ordinary dietary vitamin C deficiency was not the intervention.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    A normal blood enzyme test can miss a cofactor problem inside a vesicle.
    primary_references
    Mutations in CYB561 Causing a Novel Orthostatic Hypotension Syndrome. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29343526/ · DOI 10.1161/CIRCRESAHA.117.311949
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 52–58

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Two human families; genetic analysis with supporting Cyb561 knockout mouse results. · source_derived_draft · unverified_draft

    ## l-tyrosine-cyb-vesicle A normal blood enzyme test can miss a cofactor problem inside a vesicle. Pathogenic CYB561 variants in four patients accompanied very low norepinephrine and epinephrine despite normal plasma DBH activity; impaired intravesicular ascorbate support was the proposed functional block. Model: Two human families; genetic analysis with supporting Cyb561 knockout mouse results. Limitations: The human defect and mouse corroboration are distinct evidence; ordinary dietary vitamin C deficiency was not the intervention. Evidence access: Primary abstract Mutations in CYB561 Causing a Novel Orthostatic Hypotension Syndrome. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29343526/ · DOI 10.1161/CIRCRESAHA.117.311949
    Complete structured claim and evidence

  2. Chromaffin granules must shuttle reducing equivalents inward to re-reduce ascorbate oxidised during noradrenaline synthesis: tyramine-driven turnover oxidised intragranular ascorbate with a stoichiometry of octopamine synthesised to ascorbate oxidised near unity, 95% inhibited by the enzyme inhibitor disulfiram, and abolished or reversed by extragranular ascorbate, while labelled ascorbate showed no transmembrane transport of the vitamin itself.

    Cytosolic ascorbate pool → Reduced ascorbate inside the chromaffin granule source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/cold-research/3949732.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9db1233389aeb375adfd655ea04f39ccb05e22773f367aaa1292bb21698242e1", "start_char": 0, "end_char": 2000, "text_sha256": "9db1233389aeb375adfd655ea04f39ccb05e22773f367aaa1292bb21698242e1"}
    experimental_model
    Intact bovine chromaffin granules undergoing dopamine beta-hydroxylase turnover with labelled ascorbate
    exposure
    Tyramine- or dopamine-stimulated turnover with extragranular ascorbate
    limitations
    An in vitro demonstration in intact granules. Ascorbate itself does not cross the membrane, which is precisely why a shuttle is required.
    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
    plain_language
    The vitamin cannot cross into the vesicle, so the cell passes electrons across the membrane instead.
    primary_references
    [cold-p3949732] Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes. (1986). https://pubmed.ncbi.nlm.nih.gov/3949732/ DOI: 10.1016/s0021-9258(17)35819-2
    tissue_or_cell_type
    Adrenal chromaffin granules

    Cold water immersion: cold sensing, heat production, the catecholamine axis and what repeated exposure changes (2026-09-19) · lines 598–609

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Intact bovine chromaffin granules undergoing dopamine beta-hydroxylase turnover with labelled ascorbate · source_derived_draft · unverified_draft

    ### cold-ascorbate-shuttle Chromaffin granules must shuttle reducing equivalents inward to re-reduce ascorbate oxidised during noradrenaline synthesis: tyramine-driven turnover oxidised intragranular ascorbate with a stoichiometry of octopamine synthesised to ascorbate oxidised near unity, 95% inhibited by the enzyme inhibitor disulfiram, and abolished or reversed by extragranular ascorbate, while labelled ascorbate showed no transmembrane transport of the vitamin itself. 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 vitamin cannot cross into the vesicle, so the cell passes electrons across the membrane instead. organism: Bovine tissue_or_cell_type: Adrenal chromaffin granules experimental_model: Intact bovine chromaffin granules undergoing dopamine beta-hydroxylase turnover with labelled ascorbate limitations: An in vitro demonstration in intact granules. Ascorbate itself does not cross the membrane, which is precisely why a shuttle is required. exposure: Tyramine- or dopamine-stimulated turnover with extragranular ascorbate evidence_span: {"source_cache": "artifacts/cold-research/3949732.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9db1233389aeb375adfd655ea04f39ccb05e22773f367aaa1292bb21698242e1", "start_char": 0, "end_char": 2000, "text_sha256": "9db1233389aeb375adfd655ea04f39ccb05e22773f367aaa1292bb21698242e1"} [cold-p3949732] Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes. (1986). https://pubmed.ncbi.nlm.nih.gov/3949732/ DOI: 10.1016/s0021-9258(17)35819-2
    Complete structured claim and evidence

  3. 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

In the sources

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

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