Component

Human MOCS3 sulfur-loaded persulfide state

Human MOCS3 sulfur-loaded persulfide state. Species, exposure and limitations are retained in each linked claim.

2 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

Where it participates (unsigned role)

  1. Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it.

    Human NFS1 sulfur-loaded persulfide state → Human adenylyltransferase and sulfurtransferase / MOCS3 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
    The sulfur handoff uses identifiable proteins, not a free-floating mineral pool.
    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 365–376

    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-mocs3-transfer Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur handoff uses identifiable proteins, not a free-floating mineral pool. 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

  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

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