Component

LIAS radical-SAM [4Fe-4S] site

LIAS radical-SAM [4Fe-4S] site. Species, exposure and limitations are retained in each linked claim.

3 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 acts on it

  1. EPR comparisons supported auxiliary-cluster insertion before radical-SAM-cluster insertion during the tested LIAS reconstitution.

    LIAS auxiliary [4Fe-4S] site → LIAS radical-SAM [4Fe-4S] site source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"}
    experimental_model
    Recombinant human LIAS cluster reconstitution, EPR and LC-MS
    exposure
    [2Fe-2S]-loaded ISCU or ISCA2 donors
    limitations
    In vitro donor capacity does not establish a unique physiological donor or exclude other routes.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human proteins
    plain_language
    The experimental rebuild suggested an order for loading the two sites.
    primary_references
    [ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598
    tissue_or_cell_type
    Two LIAS iron-sulfur sites

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 403–414

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human LIAS cluster reconstitution, EPR and LC-MS · source_derived_draft · unverified_draft

    ### ala-cluster-order EPR comparisons supported auxiliary-cluster insertion before radical-SAM-cluster insertion during the tested LIAS reconstitution. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The experimental rebuild suggested an order for loading the two sites. organism: Human proteins tissue_or_cell_type: Two LIAS iron-sulfur sites experimental_model: Recombinant human LIAS cluster reconstitution, EPR and LC-MS limitations: In vitro donor capacity does not establish a unique physiological donor or exclude other routes. exposure: [2Fe-2S]-loaded ISCU or ISCA2 donors evidence_span: {"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"} [ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598
    Complete structured claim and evidence

  2. An NFU1-ISCA1 heterodimer delivers a [4Fe-4S] cluster to the radical-SAM site of LIAS.

    Human NFU1-ISCA1 complex → LIAS radical-SAM [4Fe-4S] site source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/35343688.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689", "start_char": 0, "end_char": 670, "text_sha256": "62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689"}
    experimental_model
    Recombinant protein interaction and cluster-insertion analysis
    exposure
    NFU1-ISCA1 donor complex
    limitations
    Loading the radical-SAM site is distinct from recycling the auxiliary sulfur-donor site.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human proteins
    plain_language
    A separate assembly route equips the radical-generating site.
    primary_references
    [ala-p35343688] Protein-Interaction Affinity Gradient Drives [4Fe-4S] Cluster Insertion in Human Lipoyl Synthase. (2022). https://pubmed.ncbi.nlm.nih.gov/35343688/ DOI: 10.1021/jacs.1c13626
    tissue_or_cell_type
    LIAS radical-SAM site

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 364–375

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant protein interaction and cluster-insertion analysis · source_derived_draft · unverified_draft

    ### ala-nfu1-isca1-radical-site An NFU1-ISCA1 heterodimer delivers a [4Fe-4S] cluster to the radical-SAM site of LIAS. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate assembly route equips the radical-generating site. organism: Human proteins tissue_or_cell_type: LIAS radical-SAM site experimental_model: Recombinant protein interaction and cluster-insertion analysis limitations: Loading the radical-SAM site is distinct from recycling the auxiliary sulfur-donor site. exposure: NFU1-ISCA1 donor complex evidence_span: {"source_cache": "artifacts/ala-research/35343688.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689", "start_char": 0, "end_char": 670, "text_sha256": "62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689"} [ala-p35343688] Protein-Interaction Affinity Gradient Drives [4Fe-4S] Cluster Insertion in Human Lipoyl Synthase. (2022). https://pubmed.ncbi.nlm.nih.gov/35343688/ DOI: 10.1021/jacs.1c13626
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. LIAS has distinct radical-SAM and auxiliary [4Fe-4S] clusters; the latter supplies sulfur during lipoyl synthesis.

    Lipoic acid synthetase / LIAS → [4Fe-4S] iron-sulfur cluster 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
    Two iron-sulfur clusters perform different jobs in the same enzyme.
    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 299–310

    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-lias-two-clusters LIAS has distinct radical-SAM and auxiliary [4Fe-4S] clusters; the latter supplies sulfur during lipoyl synthesis. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two iron-sulfur clusters perform different jobs in the same enzyme. 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

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