Component

Human mitochondrial glutaredoxin 5 / GLRX5

Human mitochondrial glutaredoxin 5 / GLRX5. Species, exposure and limitations are retained in each linked claim.

8 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. GLRX5-associated cases showed deficient protein lipoylation and glycine-cleavage activity with elevated glycine.

    Human mitochondrial glutaredoxin 5 / GLRX5 → Glycine accumulation in lipoylation disorders source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/ala-research/24334290.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2", "start_char": 0, "end_char": 2342, "text_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2"}
    experimental_model
    Variant nonketotic hyperglycinemia cohort and cell complementation
    exposure
    LIAS, BOLA3 or GLRX5 variants; lipoate and mitochondrially targeted lipoate in cells
    limitations
    Phenotypes varied; respiratory-chain function was preserved in this series, unlike some other Fe-S disorders.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human
    plain_language
    A cofactor-assembly defect can mimic a defect in the glycine-cleavage enzymes themselves.
    primary_references
    [ala-p24334290] Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5. (2014). https://pubmed.ncbi.nlm.nih.gov/24334290/ DOI: 10.1093/brain/awt328
    tissue_or_cell_type
    Eight genetically explained patients within an eleven-person group
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 533–544

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Variant nonketotic hyperglycinemia cohort and cell complementation · source_derived_draft · unverified_draft

    ### ala-glrx5-glycine-failure GLRX5-associated cases showed deficient protein lipoylation and glycine-cleavage activity with elevated glycine. Condition category: machinery_impairment nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cofactor-assembly defect can mimic a defect in the glycine-cleavage enzymes themselves. organism: Human tissue_or_cell_type: Eight genetically explained patients within an eleven-person group experimental_model: Variant nonketotic hyperglycinemia cohort and cell complementation limitations: Phenotypes varied; respiratory-chain function was preserved in this series, unlike some other Fe-S disorders. exposure: LIAS, BOLA3 or GLRX5 variants; lipoate and mitochondrially targeted lipoate in cells evidence_span: {"source_cache": "artifacts/ala-research/24334290.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2", "start_char": 0, "end_char": 2342, "text_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2"} [ala-p24334290] Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5. (2014). https://pubmed.ncbi.nlm.nih.gov/24334290/ DOI: 10.1093/brain/awt328
    Complete structured claim and evidence

  2. Apo-GLRX5 reduced glutathione mixed disulfides about 100 times more slowly than GLRX2.

    Human mitochondrial glutaredoxin 5 / GLRX5 → Human glutaredoxin 2 / GLRX2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"}
    experimental_model
    Crystallography, solution oligomers and biochemical assays
    exposure
    Iron-sulfur/GSH complex and disulfide assays
    limitations
    The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GLRX5
    plain_language
    Related glutaredoxins are not functionally interchangeable.
    primary_references
    [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    tissue_or_cell_type
    Purified holo and apo protein

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 801–812

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, solution oligomers and biochemical assays · source_derived_draft · unverified_draft

    ### glutathione-glrx5-disulfide-rate Apo-GLRX5 reduced glutathione mixed disulfides about 100 times more slowly than GLRX2. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Related glutaredoxins are not functionally interchangeable. organism: Human GLRX5 tissue_or_cell_type: Purified holo and apo protein experimental_model: Crystallography, solution oligomers and biochemical assays limitations: The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy. exposure: Iron-sulfur/GSH complex and disulfide assays evidence_span: {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"} [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    Complete structured claim and evidence

  3. ALAS2 activity was altered in the GLRX5-deficient cells; a problem in succinyl-CoA supply was proposed as a contributor.

    Human mitochondrial glutaredoxin 5 / GLRX5 → Human erythroid aminolevulinate synthase 2 / ALAS2 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
    A mitochondrial assembly defect may also limit the starting materials used early in heme synthesis.
    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 1083–1094

    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-alas2 ALAS2 activity was altered in the GLRX5-deficient cells; a problem in succinyl-CoA supply was proposed as a contributor. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: A mitochondrial assembly defect may also limit the starting materials used early in heme synthesis. 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

  4. Patient-derived cells showed reduced glutathione and aconitase activity, damaged/depleted mitochondrial DNA, lower complex I/IV activities and lower ATP content.

    Human mitochondrial glutaredoxin 5 / GLRX5 → ATP 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
    The defect extended beyond red-cell pigment to mitochondrial energy handling.
    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 1096–1107

    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-energy Patient-derived cells showed reduced glutathione and aconitase activity, damaged/depleted mitochondrial DNA, lower complex I/IV activities and lower ATP content. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The defect extended beyond red-cell pigment to mitochondrial energy handling. 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

  5. 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

Where it participates (unsigned role)

  1. BOLA3 did not directly enhance Fe-S cluster transfer from NFU1 or GLRX5 to LIAS in the purified assay.

    Human BOLA3 → LIAS catalytic turnover source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/36281303.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f", "start_char": 0, "end_char": 1732, "text_sha256": "29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f"}
    experimental_model
    Purified human LIAS turnover and cluster-transfer assays
    exposure
    LIAS with candidate iron-sulfur cluster donors
    limitations
    Cell-free transfer distinguishes direct donor activity from upstream functions in intact cells.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human recombinant proteins
    plain_language
    A protein can be essential in cells without stimulating this isolated transfer step.
    primary_references
    [ala-p36281303] In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. (2022). https://pubmed.ncbi.nlm.nih.gov/36281303/ DOI: 10.1021/acsbiomedchemau.2c00020
    tissue_or_cell_type
    Mitochondrial lipoyl synthesis machinery

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 338–349

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

    ### ala-bola3-direct-assay-null BOLA3 did not directly enhance Fe-S cluster transfer from NFU1 or GLRX5 to LIAS in the purified assay. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A protein can be essential in cells without stimulating this isolated transfer step. organism: Human recombinant proteins tissue_or_cell_type: Mitochondrial lipoyl synthesis machinery experimental_model: Purified human LIAS turnover and cluster-transfer assays limitations: Cell-free transfer distinguishes direct donor activity from upstream functions in intact cells. exposure: LIAS with candidate iron-sulfur cluster donors evidence_span: {"source_cache": "artifacts/ala-research/36281303.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f", "start_char": 0, "end_char": 1732, "text_sha256": "29a716d2027786ee1eefa5380aca1ddc035ec330409162f3d4e61db20015780f"} [ala-p36281303] In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. (2022). https://pubmed.ncbi.nlm.nih.gov/36281303/ DOI: 10.1021/acsbiomedchemau.2c00020
    Complete structured claim and evidence

  2. Neither lipoate nor mitochondrially targeted lipoate corrected the studied cellular lipoylation deficiency.

    Lipoic acid → 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/24334290.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2", "start_char": 0, "end_char": 2342, "text_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2"}
    experimental_model
    Variant nonketotic hyperglycinemia cohort and cell complementation
    exposure
    LIAS, BOLA3 or GLRX5 variants; lipoate and mitochondrially targeted lipoate in cells
    limitations
    Phenotypes varied; respiratory-chain function was preserved in this series, unlike some other Fe-S disorders.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human
    plain_language
    Delivering the molecule nearer mitochondria was still insufficient in these models.
    primary_references
    [ala-p24334290] Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5. (2014). https://pubmed.ncbi.nlm.nih.gov/24334290/ DOI: 10.1093/brain/awt328
    tissue_or_cell_type
    Eight genetically explained patients within an eleven-person group
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 546–557

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Variant nonketotic hyperglycinemia cohort and cell complementation · source_derived_draft · unverified_draft

    ### ala-variant-lipoate-no-rescue Neither lipoate nor mitochondrially targeted lipoate corrected the studied cellular lipoylation deficiency. Condition category: machinery_impairment nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Delivering the molecule nearer mitochondria was still insufficient in these models. organism: Human tissue_or_cell_type: Eight genetically explained patients within an eleven-person group experimental_model: Variant nonketotic hyperglycinemia cohort and cell complementation limitations: Phenotypes varied; respiratory-chain function was preserved in this series, unlike some other Fe-S disorders. exposure: LIAS, BOLA3 or GLRX5 variants; lipoate and mitochondrially targeted lipoate in cells evidence_span: {"source_cache": "artifacts/ala-research/24334290.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2", "start_char": 0, "end_char": 2342, "text_sha256": "2d6f134f9da5ac532fac9c58757e80a0b51c9912f8ddbec39eb81d1e81ccbfb2"} [ala-p24334290] Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5. (2014). https://pubmed.ncbi.nlm.nih.gov/24334290/ DOI: 10.1093/brain/awt328
    Complete structured claim and evidence

  3. Each GLRX5-bound [2Fe-2S] cluster was ligated by two protein Cys67 thiols and two GSH cysteine thiols.

    GSH → Human GLRX5 [2Fe-2S]-glutathione complex source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"}
    experimental_model
    Crystallography, solution oligomers and biochemical assays
    exposure
    Iron-sulfur/GSH complex and disulfide assays
    limitations
    The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GLRX5
    plain_language
    Glutathione is part of the cluster-binding structure, not only an antioxidant.
    primary_references
    [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    tissue_or_cell_type
    Purified holo and apo protein

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 788–799

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, solution oligomers and biochemical assays · source_derived_draft · unverified_draft

    ### glutathione-glrx5-gsh-ligand Each GLRX5-bound [2Fe-2S] cluster was ligated by two protein Cys67 thiols and two GSH cysteine thiols. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione is part of the cluster-binding structure, not only an antioxidant. organism: Human GLRX5 tissue_or_cell_type: Purified holo and apo protein experimental_model: Crystallography, solution oligomers and biochemical assays limitations: The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy. exposure: Iron-sulfur/GSH complex and disulfide assays evidence_span: {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"} [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    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.

    Evidence, AI assistance and curation standards