Component

Human cysteine desulfurase / NFS1

Human cysteine desulfurase / NFS1. Identity is distinct from its gene and experimentally modified states; see each claim for organism and scope.

5 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. FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells.

    Human cysteine desulfurase / NFS1 → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"}
    experimental_model
    HeLa localization/FRET and split-EGFP; purified protein complementation
    exposure
    Cell fractionation, immunodetection and protein interaction
    limitations
    Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens; separate Neurospora crassa complementation
    plain_language
    Sulfur delivery to the molybdenum pathway also occurs outside mitochondria.
    primary_references
    [mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
    tissue_or_cell_type
    Human cytosol and purified proteins

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 378–389

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HeLa localization/FRET and split-EGFP; purified protein complementation · source_derived_draft · unverified_draft

    ### mo-nfs1-cytosol FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sulfur delivery to the molybdenum pathway also occurs outside mitochondria. organism: Homo sapiens; separate Neurospora crassa complementation tissue_or_cell_type: Human cytosol and purified proteins experimental_model: HeLa localization/FRET and split-EGFP; purified protein complementation limitations: Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria. exposure: Cell fractionation, immunodetection and protein interaction evidence_span: {"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"} [mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
    Complete structured claim and evidence

  2. Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.

    Human cysteine desulfurase / NFS1 → L-Cysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"}
    experimental_model
    Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays
    exposure
    L-cysteine sulfur-donor assays
    limitations
    Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human proteins expressed in Escherichia coli
    plain_language
    Cysteine supplies sulfur that becomes part of the molybdenum cofactor.
    primary_references
    [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    tissue_or_cell_type
    Purified proteins

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 352–363

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays · source_derived_draft · unverified_draft

    ### mo-nfs1-sulfur Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cysteine supplies sulfur that becomes part of the molybdenum cofactor. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified proteins experimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays limitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013. exposure: L-cysteine sulfur-donor assays evidence_span: {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"} [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    Complete structured claim and evidence

  3. The NFS1-containing desulfurase complex structure resolved a solvent-exposed PLP cofactor and an unusual substrate-channel architecture.

    Human cysteine desulfurase / NFS1 → PLP source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"}
    experimental_model
    Crystallography, electron microscopy, kinetics and cell studies
    exposure
    SDA-complex structural analysis
    limitations
    Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex
    plain_language
    The sulfur-supplying machinery for iron-sulfur clusters also uses a vitamin B6-derived cofactor.
    primary_references
    [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    tissue_or_cell_type
    Mitochondrial Fe-S assembly machinery

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1148–1159

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, electron microscopy, kinetics and cell studies · source_derived_draft · unverified_draft

    ### iron-nfs1-plp The NFS1-containing desulfurase complex structure resolved a solvent-exposed PLP cofactor and an unusual substrate-channel architecture. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur-supplying machinery for iron-sulfur clusters also uses a vitamin B6-derived cofactor. organism: Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex tissue_or_cell_type: Mitochondrial Fe-S assembly machinery experimental_model: Crystallography, electron microscopy, kinetics and cell studies limitations: Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested. exposure: SDA-complex structural analysis evidence_span: {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"} [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    Complete structured claim and evidence

  4. The NFS1–ISD11–ACP core associates with ISCU, frataxin and ferredoxin to support Fe-S cluster biosynthesis.

    Human cysteine desulfurase / NFS1 → Iron-sulfur cluster biosynthesis and assembly source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"}
    experimental_model
    Crystallography, electron microscopy, kinetics and cell studies
    exposure
    SDA-complex structural analysis
    limitations
    Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex
    plain_language
    Iron needs an assembly system and a sulfur supply before it becomes a working iron-sulfur cofactor.
    primary_references
    [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    tissue_or_cell_type
    Mitochondrial Fe-S assembly machinery

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1161–1172

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, electron microscopy, kinetics and cell studies · source_derived_draft · unverified_draft

    ### iron-sda-assembly The NFS1–ISD11–ACP core associates with ISCU, frataxin and ferredoxin to support Fe-S cluster biosynthesis. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron needs an assembly system and a sulfur supply before it becomes a working iron-sulfur cofactor. organism: Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex tissue_or_cell_type: Mitochondrial Fe-S assembly machinery experimental_model: Crystallography, electron microscopy, kinetics and cell studies limitations: Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested. exposure: SDA-complex structural analysis evidence_span: {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"} [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. In the recombinant hybrid NFS1–ISD11–ACP structure, the phosphopantetheine-linked acyl group of E. coli ACP occupies the hydrophobic core of human ISD11.

    Escherichia coli acylated phosphopantetheinyl-AcpP → Human ISD11 / LYRM4 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_location
    Abstract; primary Results: Identification of the ACP–Lipid–ISD11 Motif
    experimental_model
    Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure
    exposure
    Coexpression and structural analysis; no nutrient restriction.
    limitations
    This is not an all-human ACP structure. The bound PLP and acyl-ACP show cofactor coexistence; dietary B6/B5 dependency or repletion was not tested. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens proteins; Escherichia coli ACP
    plain_language
    The CoA-derived carrier arm holds a fatty-acid chain that helps form the iron–sulfur complex interface.
    primary_references
    [b5-met-cory2017] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    tissue_or_cell_type
    Purified recombinant Fe–S assembly subcomplex

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 935–947

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure · source_derived_draft · unverified_draft

    ### b5-met-acyl-acp-isd11-interface In the recombinant hybrid NFS1–ISD11–ACP structure, the phosphopantetheine-linked acyl group of E. coli ACP occupies the hydrophobic core of human ISD11. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The CoA-derived carrier arm holds a fatty-acid chain that helps form the iron–sulfur complex interface. organism: Homo sapiens proteins; Escherichia coli ACP tissue_or_cell_type: Purified recombinant Fe–S assembly subcomplex experimental_model: Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure limitations: This is not an all-human ACP structure. The bound PLP and acyl-ACP show cofactor coexistence; dietary B6/B5 dependency or repletion was not tested. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Coexpression and structural analysis; no nutrient restriction. cross_nutrient: true evidence_location: Abstract; primary Results: Identification of the ACP–Lipid–ISD11 Motif [b5-met-cory2017] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
    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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