Component

Bovine dopamine beta-hydroxylase

Bovine adrenal-medullary dopamine beta-hydroxylase used in biochemical studies.

4 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

Where it participates (unsigned role)

  1. Blumberg et al. found little average coordination change after ascorbate reduction: four nitrogen ligands best fit both forms, at 1.97 angstrom oxidized and 2.05 angstrom reduced; they found no sulfur or chlorine ligation and explicitly opposed the earlier interpretation.

    L-Ascorbate → Ascorbate-reduced bovine dopamine beta-hydroxylase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS
    exposure
    Purified oxidized versus ascorbate-reduced bovine DBH; bulk X-ray absorption/EXAFS interpretation.
    limitations
    The abstract permits N/O ligation generally; four nitrogens was its best fit. Historical bulk spectroscopy, not a review of all later structural evidence or current consensus.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus
    plain_language
    The later study agreed that copper was reduced but interpreted the surrounding atoms differently.
    primary_references
    [blumberg1989] X-ray absorption spectroscopic study of the active copper sites in dopamine beta-hydroxylase. (1989). https://pubmed.ncbi.nlm.nih.gov/2703478/ DOI: 10.1016/s0021-9258(18)83307-5
    tissue_or_cell_type
    Adrenal-medullary enzyme preparation

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 950–961

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS · source_derived_draft · unverified_draft

    ### vc-enzyme-dbh-coordination-blumberg-interpretation Blumberg et al. found little average coordination change after ascorbate reduction: four nitrogen ligands best fit both forms, at 1.97 angstrom oxidized and 2.05 angstrom reduced; they found no sulfur or chlorine ligation and explicitly opposed the earlier interpretation. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: The later study agreed that copper was reduced but interpreted the surrounding atoms differently. organism: Bos taurus tissue_or_cell_type: Adrenal-medullary enzyme preparation experimental_model: Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS limitations: The abstract permits N/O ligation generally; four nitrogens was its best fit. Historical bulk spectroscopy, not a review of all later structural evidence or current consensus. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Purified oxidized versus ascorbate-reduced bovine DBH; bulk X-ray absorption/EXAFS interpretation. [blumberg1989] X-ray absorption spectroscopic study of the active copper sites in dopamine beta-hydroxylase. (1989). https://pubmed.ncbi.nlm.nih.gov/2703478/ DOI: 10.1016/s0021-9258(18)83307-5
    Complete structured claim and evidence

  2. Scott et al. interpreted the ascorbate-reduced bovine DBH spectrum as a decrease from roughly four to two N/O ligands plus a sulfur-containing ligand at 2.30 angstrom, compared with the oxidized enzyme.

    L-Ascorbate → Ascorbate-reduced bovine dopamine beta-hydroxylase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS
    exposure
    Purified oxidized versus ascorbate-reduced bovine DBH; bulk X-ray absorption/EXAFS interpretation.
    limitations
    Historical average EXAFS interpretation explicitly challenged by Blumberg1989; not an endorsed ligand assignment or a claim about human dietary copper.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus
    plain_language
    This study proposed that reducing the copper also changed which nearby atoms coordinated it.
    primary_references
    [scott1988] The copper sites of dopamine beta-hydroxylase: an X-ray absorption spectroscopic study. (1988). https://pubmed.ncbi.nlm.nih.gov/3179263/ DOI: 10.1021/bi00415a005
    tissue_or_cell_type
    Adrenal-medullary enzyme preparation

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 937–948

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS · source_derived_draft · unverified_draft

    ### vc-enzyme-dbh-coordination-scott-interpretation Scott et al. interpreted the ascorbate-reduced bovine DBH spectrum as a decrease from roughly four to two N/O ligands plus a sulfur-containing ligand at 2.30 angstrom, compared with the oxidized enzyme. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: This study proposed that reducing the copper also changed which nearby atoms coordinated it. organism: Bos taurus tissue_or_cell_type: Adrenal-medullary enzyme preparation experimental_model: Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS limitations: Historical average EXAFS interpretation explicitly challenged by Blumberg1989; not an endorsed ligand assignment or a claim about human dietary copper. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Purified oxidized versus ascorbate-reduced bovine DBH; bulk X-ray absorption/EXAFS interpretation. [scott1988] The copper sites of dopamine beta-hydroxylase: an X-ray absorption spectroscopic study. (1988). https://pubmed.ncbi.nlm.nih.gov/3179263/ DOI: 10.1021/bi00415a005
    Complete structured claim and evidence

  3. Ascorbate reduced enzyme-bound copper in purified bovine dopamine beta-hydroxylase from Cu(II) to Cu(I), as examined by X-ray absorption spectroscopy.

    L-Ascorbate → Ascorbate-reduced bovine dopamine beta-hydroxylase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS
    exposure
    Ascorbate reduction of purified Cu(II)-DBH to Cu(I)-DBH.
    limitations
    Purified bovine enzyme, not a dietary copper-status measurement. Scott 1988 and Blumberg 1989 disagree on the detailed coordination change and heavy-atom ligation; this record retains only the shared Cu(II)-to-Cu(I) redox conclusion.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus
    plain_language
    Vitamin C supplies reducing power to copper held inside this neurotransmitter enzyme.
    primary_references
    [scott1988] The copper sites of dopamine beta-hydroxylase: an X-ray absorption spectroscopic study. (1988). https://pubmed.ncbi.nlm.nih.gov/3179263/ DOI: 10.1021/bi00415a005 [blumberg1989] X-ray absorption spectroscopic study of the active copper sites in dopamine beta-hydroxylase. (1989). https://pubmed.ncbi.nlm.nih.gov/2703478/ DOI: 10.1016/s0021-9258(18)83307-5
    tissue_or_cell_type
    Adrenal-medullary enzyme preparation

    Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 793–805

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS · source_derived_draft · unverified_draft

    ### vc-enzyme-dbh-copper-reduction Ascorbate reduced enzyme-bound copper in purified bovine dopamine beta-hydroxylase from Cu(II) to Cu(I), as examined by X-ray absorption spectroscopy. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C supplies reducing power to copper held inside this neurotransmitter enzyme. organism: Bos taurus tissue_or_cell_type: Adrenal-medullary enzyme preparation experimental_model: Bovine dopamine beta-hydroxylase X-ray absorption and EXAFS limitations: Purified bovine enzyme, not a dietary copper-status measurement. Scott 1988 and Blumberg 1989 disagree on the detailed coordination change and heavy-atom ligation; this record retains only the shared Cu(II)-to-Cu(I) redox conclusion. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Ascorbate reduction of purified Cu(II)-DBH to Cu(I)-DBH. [scott1988] The copper sites of dopamine beta-hydroxylase: an X-ray absorption spectroscopic study. (1988). https://pubmed.ncbi.nlm.nih.gov/3179263/ DOI: 10.1021/bi00415a005 [blumberg1989] X-ray absorption spectroscopic study of the active copper sites in dopamine beta-hydroxylase. (1989). https://pubmed.ncbi.nlm.nih.gov/2703478/ DOI: 10.1016/s0021-9258(18)83307-5
    Complete structured claim and evidence

  4. Coupling bovine DBH tyramine hydroxylation to semidehydroascorbate reductase identified semidehydroascorbate as the immediate enzymic oxidation product of ascorbate.

    L-Ascorbate → Ascorbyl radical source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing.
    experimental_model
    Purified bovine DBH coupled to rat-liver or Neurospora semidehydroascorbate reductase
    exposure
    Tyramine beta-hydroxylation with ascorbate; coupled pyridine-nucleotide oxidation and radical recycling assays.
    limitations
    Heterologous reductase-coupled assay; radical dismutation can subsequently produce DHA, so immediate product and net redox balance must be distinguished.
    nutrient_topic
    Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
    organism
    Bos taurus; Rattus norvegicus; Neurospora crassa
    plain_language
    This copper enzyme takes single electrons from vitamin C, leaving an ascorbyl radical that can be recycled.
    primary_references
    [dbh1981] Mechanism of dopamine-beta-hydroxylation. Semidehydroascorbate as the enzyme oxidation product of ascorbate. (1981). https://pubmed.ncbi.nlm.nih.gov/6451628/ DOI: 10.1016/S0021-9258(19)69620-1
    tissue_or_cell_type
    Bovine adrenal-medullary enzyme plus heterologous reductase preparations

    Vitamin C: mechanisms, deficiency 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 · Purified bovine DBH coupled to rat-liver or Neurospora semidehydroascorbate reductase · source_derived_draft · unverified_draft

    ### vc-enzyme-dbh-radical-product Coupling bovine DBH tyramine hydroxylation to semidehydroascorbate reductase identified semidehydroascorbate as the immediate enzymic oxidation product of ascorbate. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: This copper enzyme takes single electrons from vitamin C, leaving an ascorbyl radical that can be recycled. organism: Bos taurus; Rattus norvegicus; Neurospora crassa tissue_or_cell_type: Bovine adrenal-medullary enzyme plus heterologous reductase preparations experimental_model: Purified bovine DBH coupled to rat-liver or Neurospora semidehydroascorbate reductase limitations: Heterologous reductase-coupled assay; radical dismutation can subsequently produce DHA, so immediate product and net redox balance must be distinguished. cross_nutrient: Vitamin C chemistry in collagen, modified-lysine/carnitine metabolism or copper-dependent peptide/catecholamine processing. exposure: Tyramine beta-hydroxylation with ascorbate; coupled pyridine-nucleotide oxidation and radical recycling assays. [dbh1981] Mechanism of dopamine-beta-hydroxylation. Semidehydroascorbate as the enzyme oxidation product of ascorbate. (1981). https://pubmed.ncbi.nlm.nih.gov/6451628/ DOI: 10.1016/S0021-9258(19)69620-1
    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.

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