Component

Human adrenodoxin / FDX1

Human adrenodoxin / FDX1

6 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 adrenodoxin supported CYP27B1 activity in reconstituted vesicles; varying adrenodoxin changed apparent kinetic parameters for calcifediol hydroxylation.

    Human adrenodoxin / FDX1 → Vitamin D 1-alpha-hydroxylase / CYP27B1 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved.
    experimental_model
    Human CYP27B1/FDX1/FDXR kinetic reconstitution
    exposure
    FDX1 1-30 micromolar; 2-min incubations with calcifediol; Table 4.
    limitations
    The experiment varies intact FDX1, not dietary iron. Reciprocal changes of apparent Km and turnover prevent interpreting FDX1 level as a universal limiting factor.
    nutrient
    Vitamin D2 and D3 · Vitamin D2 and D3
    nutrient_topic
    Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3
    organism
    Homo sapiens proteins
    plain_language
    An iron-sulfur electron carrier supports the final D3 activation step.
    primary_references
    [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    tissue_or_cell_type
    reconstituted mitochondrial membrane

    Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 452–465

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CYP27B1/FDX1/FDXR kinetic reconstitution · source_derived_draft · unverified_draft

    ### vd-act-fdx1-cyp27b1 Human adrenodoxin supported CYP27B1 activity in reconstituted vesicles; varying adrenodoxin changed apparent kinetic parameters for calcifediol hydroxylation. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An iron-sulfur electron carrier supports the final D3 activation step. organism: Homo sapiens proteins tissue_or_cell_type: reconstituted mitochondrial membrane experimental_model: Human CYP27B1/FDX1/FDXR kinetic reconstitution limitations: The experiment varies intact FDX1, not dietary iron. Reciprocal changes of apparent Km and turnover prevent interpreting FDX1 level as a universal limiting factor. exposure: FDX1 1-30 micromolar; 2-min incubations with calcifediol; Table 4. cross_nutrient: true evidence_location: Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved. nutrient: Vitamin D2 and D3 [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    Complete structured claim and evidence

  2. Human [2Fe-2S] ferredoxin FDX1 supplied electrons for MMAB-dependent adenosylcobalamin synthesis in the FDXR/NADPH reconstitution.

    Human adrenodoxin / FDX1 → Human ATP:cob(I)alamin adenosyltransferase / MMAB source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Abstract and indexed primary Results, Figure 3
    experimental_model
    Purified human proteins
    exposure
    FDX1, FDXR and NADPH with MMAB, cob(II)alamin and ATP
    limitations
    Biochemically competent donor; exclusivity or necessity in living humans was not tested.
    nutrient_topic
    Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
    organism
    Homo sapiens
    plain_language
    In the purified human system, an iron-sulfur electron carrier supported B12 activation.
    primary_references
    [gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163
    tissue_or_cell_type
    Purified protein assay

    Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1005–1017

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human proteins · source_derived_draft · unverified_draft

    ### fdx1-supports-mmab Human [2Fe-2S] ferredoxin FDX1 supplied electrons for MMAB-dependent adenosylcobalamin synthesis in the FDXR/NADPH reconstitution. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: In the purified human system, an iron-sulfur electron carrier supported B12 activation. organism: Homo sapiens tissue_or_cell_type: Purified protein assay experimental_model: Purified human proteins limitations: Biochemically competent donor; exclusivity or necessity in living humans was not tested. exposure: FDX1, FDXR and NADPH with MMAB, cob(II)alamin and ATP cross_nutrient: true evidence_location: Abstract and indexed primary Results, Figure 3 [gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163
    Complete structured claim and evidence

What acts on it

  1. The active human CYP27B1 reconstitution supplied human adrenodoxin reductase and NADPH upstream of human adrenodoxin.

    Human ferredoxin reductase / FDXR → Human adrenodoxin / FDX1 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved.
    experimental_model
    Human protein reconstitution and substrate turnover
    exposure
    0.4 micromolar FDXR, 15 micromolar FDX1 and 50 micromolar NADPH; Experimental procedures.
    limitations
    This record reports the supported redox chain; FDXR omission or dietary niacin/riboflavin intervention was not reported in the extracted experiment.
    nutrient
    Vitamin D2 and D3 · Vitamin D2 and D3
    nutrient_topic
    Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3
    organism
    Homo sapiens proteins
    plain_language
    A reductase feeds the electron carrier used during vitamin D activation.
    primary_references
    [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    tissue_or_cell_type
    mitochondrial redox-partner assay

    Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 467–480

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human protein reconstitution and substrate turnover · source_derived_draft · unverified_draft

    ### vd-act-fdxr-cyp27b1-system The active human CYP27B1 reconstitution supplied human adrenodoxin reductase and NADPH upstream of human adrenodoxin. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A reductase feeds the electron carrier used during vitamin D activation. organism: Homo sapiens proteins tissue_or_cell_type: mitochondrial redox-partner assay experimental_model: Human protein reconstitution and substrate turnover limitations: This record reports the supported redox chain; FDXR omission or dietary niacin/riboflavin intervention was not reported in the extracted experiment. exposure: 0.4 micromolar FDXR, 15 micromolar FDX1 and 50 micromolar NADPH; Experimental procedures. cross_nutrient: true evidence_location: Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved. nutrient: Vitamin D2 and D3 [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human CYP27B1 1alpha-hydroxylated 25-hydroxyvitamin D2 in phospholipid vesicles; low-substrate catalytic efficiency was similar to that measured for calcifediol.

    Vitamin D 1-alpha-hydroxylase / CYP27B1 → 1-alpha,25-Dihydroxyvitamin D2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_location
    Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved.
    experimental_model
    Partially purified human CYP27B1 membrane assay
    exposure
    5-40 nM CYP27B1; 15 micromolar FDX1, 0.4 micromolar FDXR, 50 micromolar NADPH; 2 min at 37 C. Table 5/Figure 6A.
    limitations
    D2 kinetic data came from one experiment; results do not establish human dosing equivalence.
    nutrient
    Vitamin D2 and D3 · Vitamin D2 and D3
    nutrient_topic
    Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3
    organism
    Homo sapiens proteins
    plain_language
    CYP27B1 completes activation of the D2 precursor.
    primary_references
    [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    tissue_or_cell_type
    reconstituted inner-mitochondrial-membrane model

    Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 437–450

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Partially purified human CYP27B1 membrane assay · source_derived_draft · unverified_draft

    ### vd-act-cyp27b1-d2 Human CYP27B1 1alpha-hydroxylated 25-hydroxyvitamin D2 in phospholipid vesicles; low-substrate catalytic efficiency was similar to that measured for calcifediol. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP27B1 completes activation of the D2 precursor. organism: Homo sapiens proteins tissue_or_cell_type: reconstituted inner-mitochondrial-membrane model experimental_model: Partially purified human CYP27B1 membrane assay limitations: D2 kinetic data came from one experiment; results do not establish human dosing equivalence. exposure: 5-40 nM CYP27B1; 15 micromolar FDX1, 0.4 micromolar FDXR, 50 micromolar NADPH; 2 min at 37 C. Table 5/Figure 6A. cross_nutrient: false evidence_location: Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved. nutrient: Vitamin D2 and D3 [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x
    Complete structured claim and evidence

  2. Engineered LplA restored lipoylation in MECR-, BOLA3-, FDX1-, LIAS- and LIPT1-knockout cell models.

    Engineered bacterial LplA targeted to mammalian mitochondria → Mitochondrial protein lipoylation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/ala-research/39547509.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c914532ce06cd71fa946c3aa27935a85d94827215c74ae076a0eebb80ebb45bd", "start_char": 0, "end_char": 1884, "text_sha256": "c914532ce06cd71fa946c3aa27935a85d94827215c74ae076a0eebb80ebb45bd"}
    experimental_model
    Engineered bacterial ligase in human knockout cells and a modeled patient allele
    exposure
    Mitochondrially targeted engineered LplA expression
    limitations
    Experimental genetic engineering, not ordinary supplementation and not a treated-patient efficacy trial.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human cells with bacterial enzyme engineering
    plain_language
    Adding a new enzyme created a route that free supplementation alone did not supply.
    primary_references
    [ala-p39547509] Engineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency. (2024). https://pubmed.ncbi.nlm.nih.gov/39547509/ DOI: 10.1016/j.jbc.2024.107995
    tissue_or_cell_type
    Lipoylation-null cell models and K562 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 559–570

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Engineered bacterial ligase in human knockout cells and a modeled patient allele · source_derived_draft · unverified_draft

    ### ala-lpla-lipoylation-rescue Engineered LplA restored lipoylation in MECR-, BOLA3-, FDX1-, LIAS- and LIPT1-knockout cell models. Condition category: machinery_impairment nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding a new enzyme created a route that free supplementation alone did not supply. organism: Human cells with bacterial enzyme engineering tissue_or_cell_type: Lipoylation-null cell models and K562 cells experimental_model: Engineered bacterial ligase in human knockout cells and a modeled patient allele limitations: Experimental genetic engineering, not ordinary supplementation and not a treated-patient efficacy trial. exposure: Mitochondrially targeted engineered LplA expression evidence_span: {"source_cache": "artifacts/ala-research/39547509.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c914532ce06cd71fa946c3aa27935a85d94827215c74ae076a0eebb80ebb45bd", "start_char": 0, "end_char": 1884, "text_sha256": "c914532ce06cd71fa946c3aa27935a85d94827215c74ae076a0eebb80ebb45bd"} [ala-p39547509] Engineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency. (2024). https://pubmed.ncbi.nlm.nih.gov/39547509/ DOI: 10.1016/j.jbc.2024.107995
    Complete structured claim and evidence

  3. R186Q human MMAB showed no detectable adenosylcobalamin synthesis with FDX1/FDXR/NADPH, although a strong chemical reductant supported activity.

    Human MMAB p.Arg186Gln → Human MMAB adenosylcobalamin synthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    true
    evidence_location
    Abstract and indexed primary Results, Figure 3
    experimental_model
    Purified human MMAB R186Q
    exposure
    R186Q variant; FDX1/FDXR/NADPH versus titanium(III)citrate
    limitations
    Detection-limited in-vitro activity; not proof of zero activity in every tissue.
    nutrient_topic
    Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
    organism
    Homo sapiens
    plain_language
    This MMAB variant failed in the ferredoxin assay; the result depended on the electron donor.
    primary_references
    [gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163
    tissue_or_cell_type
    Purified protein assay
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1019–1031

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MMAB R186Q · source_derived_draft · unverified_draft

    ### mmab-r186q-fdx-system-fails R186Q human MMAB showed no detectable adenosylcobalamin synthesis with FDX1/FDXR/NADPH, although a strong chemical reductant supported activity. Condition category: machinery_impairment nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This MMAB variant failed in the ferredoxin assay; the result depended on the electron donor. organism: Homo sapiens tissue_or_cell_type: Purified protein assay experimental_model: Purified human MMAB R186Q limitations: Detection-limited in-vitro activity; not proof of zero activity in every tissue. exposure: R186Q variant; FDX1/FDXR/NADPH versus titanium(III)citrate cross_nutrient: true evidence_location: Abstract and indexed primary Results, Figure 3 [gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163
    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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