Component

Human ferrochelatase / FECH

Human ferrochelatase / FECH

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

What it acts on

  1. The human ferrochelatase homodimer contained two uniquely coordinated, nitric-oxide-sensitive [2Fe-2S] clusters.

    Human ferrochelatase / FECH → [2Fe-2S] iron-sulfur cluster source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"}
    experimental_model
    Human ferrochelatase crystal structure
    exposure
    2.0 angstrom structure and biochemical catalytic interpretation
    limitations
    Purified enzyme; cluster structure is not a human dietary-iron threshold.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human enzyme
    plain_language
    The enzyme that inserts iron also carries its own iron-sulfur cofactors.
    primary_references
    [iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152
    tissue_or_cell_type
    Mitochondrial membrane-associated enzyme

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 524–535

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human ferrochelatase crystal structure · source_derived_draft · unverified_draft

    ### iron-fech-clusters The human ferrochelatase homodimer contained two uniquely coordinated, nitric-oxide-sensitive [2Fe-2S] clusters. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme that inserts iron also carries its own iron-sulfur cofactors. organism: Human enzyme tissue_or_cell_type: Mitochondrial membrane-associated enzyme experimental_model: Human ferrochelatase crystal structure limitations: Purified enzyme; cluster structure is not a human dietary-iron threshold. exposure: 2.0 angstrom structure and biochemical catalytic interpretation evidence_span: {"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"} [iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152
    Complete structured claim and evidence

  2. Human ferrochelatase inserts ferrous iron into protoporphyrin to form heme.

    Human ferrochelatase / FECH → Protoporphyrin IX source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"}
    experimental_model
    Human ferrochelatase crystal structure
    exposure
    2.0 angstrom structure and biochemical catalytic interpretation
    limitations
    Purified enzyme; cluster structure is not a human dietary-iron threshold.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human enzyme
    plain_language
    The last step places an iron atom inside the finished heme ring.
    primary_references
    [iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152
    tissue_or_cell_type
    Mitochondrial membrane-associated enzyme

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 511–522

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human ferrochelatase crystal structure · source_derived_draft · unverified_draft

    ### iron-fech-heme Human ferrochelatase inserts ferrous iron into protoporphyrin to form heme. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The last step places an iron atom inside the finished heme ring. organism: Human enzyme tissue_or_cell_type: Mitochondrial membrane-associated enzyme experimental_model: Human ferrochelatase crystal structure limitations: Purified enzyme; cluster structure is not a human dietary-iron threshold. exposure: 2.0 angstrom structure and biochemical catalytic interpretation evidence_span: {"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"} [iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152
    Complete structured claim and evidence

What acts on it

  1. PIH treatment lowered FECH protein without lowering FECH mRNA in human liver-cell models.

    Pyridoxal isonicotinoyl hydrazone → Human ferrochelatase / FECH source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    B6-drug conjugation connects to iron-sensitive heme machinery.
    experimental_model
    Cell-free chemistry, primary human hepatocytes and HepG2/C3A cells
    exposure
    100 micromolar PIH for 16 hours in the initial HepG2/C3A comparison; 24-hour PIH dose-response assays.
    limitations
    Direct destruction of the FECH iron-sulfur cluster was not demonstrated.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    A drug-B6 conjugate affected a heme-making enzyme.
    primary_references
    [brewer-2019-isoniazid] The Isoniazid Metabolites Hydrazine and Pyridoxal Isonicotinoyl Hydrazone Modulate Heme Biosynthesis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6390808/ DOI: 10.1093/toxsci/kfy294
    tissue_or_cell_type
    Primary human hepatocytes and HepG2/C3A cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1296–1307

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell-free chemistry, primary human hepatocytes and HepG2/C3A cells · source_derived_draft · unverified_draft

    ### b6-neuro-pih-fech-protein PIH treatment lowered FECH protein without lowering FECH mRNA in human liver-cell models. Condition category: machinery_impairment nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A drug-B6 conjugate affected a heme-making enzyme. organism: Homo sapiens tissue_or_cell_type: Primary human hepatocytes and HepG2/C3A cells experimental_model: Cell-free chemistry, primary human hepatocytes and HepG2/C3A cells limitations: Direct destruction of the FECH iron-sulfur cluster was not demonstrated. exposure: 100 micromolar PIH for 16 hours in the initial HepG2/C3A comparison; 24-hour PIH dose-response assays. cross_nutrient: B6-drug conjugation connects to iron-sensitive heme machinery. [brewer-2019-isoniazid] The Isoniazid Metabolites Hydrazine and Pyridoxal Isonicotinoyl Hydrazone Modulate Heme Biosynthesis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6390808/ DOI: 10.1093/toxsci/kfy294
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Ferrochelatase protein abundance increased in patient-derived cells, while its catalytic activity was drastically reduced.

    Human mitochondrial glutaredoxin 5 / GLRX5 → Ferrochelatase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/30660387.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e", "start_char": 0, "end_char": 1625, "text_sha256": "ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e"}
    experimental_model
    Patient-derived cell biochemistry and variant structural analysis
    exposure
    Compound-heterozygous GLRX5 variants
    limitations
    One patient; reduced succinyl-CoA contribution to ALAS2 dysfunction was proposed, not definitively isolated.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human GLRX5-deficient patient
    plain_language
    More enzyme protein did not mean more working enzyme.
    primary_references
    [iron-p30660387] GLRX5 mutations impair heme biosynthetic enzymes ALA synthase 2 and ferrochelatase in Human congenital sideroblastic anemia. (2019). https://pubmed.ncbi.nlm.nih.gov/30660387/ DOI: 10.1016/j.ymgme.2018.12.012
    tissue_or_cell_type
    Lymphoblastoid and CD34-positive cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1070–1081

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient-derived cell biochemistry and variant structural analysis · source_derived_draft · unverified_draft

    ### iron-glrx5-fech Ferrochelatase protein abundance increased in patient-derived cells, while its catalytic activity was drastically reduced. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: More enzyme protein did not mean more working enzyme. organism: Human GLRX5-deficient patient tissue_or_cell_type: Lymphoblastoid and CD34-positive cells experimental_model: Patient-derived cell biochemistry and variant structural analysis limitations: One patient; reduced succinyl-CoA contribution to ALAS2 dysfunction was proposed, not definitively isolated. exposure: Compound-heterozygous GLRX5 variants evidence_span: {"source_cache": "artifacts/iron-research/30660387.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e", "start_char": 0, "end_char": 1625, "text_sha256": "ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e"} [iron-p30660387] GLRX5 mutations impair heme biosynthetic enzymes ALA synthase 2 and ferrochelatase in Human congenital sideroblastic anemia. (2019). https://pubmed.ncbi.nlm.nih.gov/30660387/ DOI: 10.1016/j.ymgme.2018.12.012
    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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