Component
Ascorbate-reduced bovine dopamine beta-hydroxylase
DBH preparation with enzyme-bound Cu(I), experimentally distinguished from its Cu(II) form.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
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.
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 evidenceScott 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.
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 evidenceAscorbate reduced enzyme-bound copper in purified bovine dopamine beta-hydroxylase from Cu(II) to Cu(I), as examined by X-ray absorption spectroscopy.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.