Component

Carbon monoxide

Carbon monoxide. 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 it acts on

  1. Carbon monoxide-mediated oxidative stress causes chemical alterations in myelin basic protein, which initiates an adaptive immunological response leading to a functional deficit, and poisoned rats do not improve in a radial maze.

    Carbon monoxide → Myelin basic protein source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/16325878.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6e0360f0f818602bdcf74234be1b33779b854e82daadfdd69e78ad24eaa5953f", "start_char": 0, "end_char": 1115, "text_sha256": "6e0360f0f818602bdcf74234be1b33779b854e82daadfdd69e78ad24eaa5953f"}
    experimental_model
    Rat model of carbon monoxide poisoning with myelin basic protein chemistry, immunology and maze testing
    exposure
    Hyperbaric oxygen given after carbon monoxide poisoning
    limitations
    An immunological mechanism in a rat model. The treatment prevented the functional deficit without eliminating all the chemical changes, which is the informative dissociation.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Rat
    plain_language
    The gas changes a brain protein enough that the immune system starts attacking it.
    primary_references
    [hbot-p16325878] Hyperbaric oxygen reduces delayed immune-mediated neuropathology in experimental carbon monoxide toxicity. (2006). https://pubmed.ncbi.nlm.nih.gov/16325878/ DOI: 10.1016/j.taap.2005.10.006
    tissue_or_cell_type
    Brain and immune system

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 1076–1087

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat model of carbon monoxide poisoning with myelin basic protein chemistry, immunology and maze testing · source_derived_draft · unverified_draft

    ### hbot-mbp-immune-mechanism Carbon monoxide-mediated oxidative stress causes chemical alterations in myelin basic protein, which initiates an adaptive immunological response leading to a functional deficit, and poisoned rats do not improve in a radial maze. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The gas changes a brain protein enough that the immune system starts attacking it. organism: Rat tissue_or_cell_type: Brain and immune system experimental_model: Rat model of carbon monoxide poisoning with myelin basic protein chemistry, immunology and maze testing limitations: An immunological mechanism in a rat model. The treatment prevented the functional deficit without eliminating all the chemical changes, which is the informative dissociation. exposure: Hyperbaric oxygen given after carbon monoxide poisoning evidence_span: {"source_cache": "artifacts/hbot-research/16325878.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6e0360f0f818602bdcf74234be1b33779b854e82daadfdd69e78ad24eaa5953f", "start_char": 0, "end_char": 1115, "text_sha256": "6e0360f0f818602bdcf74234be1b33779b854e82daadfdd69e78ad24eaa5953f"} [hbot-p16325878] Hyperbaric oxygen reduces delayed immune-mediated neuropathology in experimental carbon monoxide toxicity. (2006). https://pubmed.ncbi.nlm.nih.gov/16325878/ DOI: 10.1016/j.taap.2005.10.006
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The authors suggest that increased sequestration of iron as a consequence of induced heme oxygenase-1 might be involved in the adaptive protection, and that induction of DNA damage is not the trigger for it.

    Human heme oxygenase 1 / HMOX1 → Availability of free transition metals inside the cell source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/11023535.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "19b770dff3d327e2dd6d49180686f9823624190ab5693c28b88adcfaf703f14d", "start_char": 0, "end_char": 1576, "text_sha256": "19b770dff3d327e2dd6d49180686f9823624190ab5693c28b88adcfaf703f14d"}
    experimental_model
    Comet assay in lymphocytes of volunteers before and after hyperbaric oxygen, with enzyme expression measurement
    exposure
    100% oxygen at 2.5 ATA for three 20-minute periods
    limitations
    A human exposure study with a within-subject design. The iron-sequestration explanation is the authors’ inference from the pattern of protection, not a direct measurement of free iron.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human
    plain_language
    The proposed protection is locking away the iron that would otherwise turn peroxide into a more dangerous radical.
    primary_references
    [hbot-p11023535] Induction of heme oxygenase-1 and adaptive protection against the induction of DNA damage after hyperbaric oxygen treatment. (2000). https://pubmed.ncbi.nlm.nih.gov/11023535/ DOI: 10.1093/carcin/21.10.1795
    tissue_or_cell_type
    Circulating lymphocytes

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 322–333

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Comet assay in lymphocytes of volunteers before and after hyperbaric oxygen, with enzyme expression measurement · source_derived_draft · unverified_draft

    ### hbot-iron-sequestration-hypothesis The authors suggest that increased sequestration of iron as a consequence of induced heme oxygenase-1 might be involved in the adaptive protection, and that induction of DNA damage is not the trigger for it. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The proposed protection is locking away the iron that would otherwise turn peroxide into a more dangerous radical. organism: Human tissue_or_cell_type: Circulating lymphocytes experimental_model: Comet assay in lymphocytes of volunteers before and after hyperbaric oxygen, with enzyme expression measurement limitations: A human exposure study with a within-subject design. The iron-sequestration explanation is the authors’ inference from the pattern of protection, not a direct measurement of free iron. exposure: 100% oxygen at 2.5 ATA for three 20-minute periods evidence_span: {"source_cache": "artifacts/hbot-research/11023535.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "19b770dff3d327e2dd6d49180686f9823624190ab5693c28b88adcfaf703f14d", "start_char": 0, "end_char": 1576, "text_sha256": "19b770dff3d327e2dd6d49180686f9823624190ab5693c28b88adcfaf703f14d"} [hbot-p11023535] Induction of heme oxygenase-1 and adaptive protection against the induction of DNA damage after hyperbaric oxygen treatment. (2000). https://pubmed.ncbi.nlm.nih.gov/11023535/ DOI: 10.1093/carcin/21.10.1795
    Complete structured claim and evidence

  2. Heme oxygenase oxidatively cleaves heme to biliverdin with release of iron and carbon monoxide.

    Human heme oxygenase 1 / HMOX1 → Heme source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/15049686.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "76bcb8ae12316350b1161f32c1633e2b5c752fcbf7e158940385b354ee3452d2", "start_char": 0, "end_char": 1167, "text_sha256": "76bcb8ae12316350b1161f32c1633e2b5c752fcbf7e158940385b354ee3452d2"}
    experimental_model
    Product-bound human HO-1 structure
    exposure
    Biliverdin-bound structure compared with heme-bound enzyme
    limitations
    Product release interpretation from structure; no in-vivo flux measurement.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Human enzyme
    plain_language
    Breaking open heme makes its iron available for reuse.
    primary_references
    [iron-p15049686] Crystal structure of human heme oxygenase-1 in a complex with biliverdin. (2004). https://pubmed.ncbi.nlm.nih.gov/15049686/ DOI: 10.1021/bi035451l
    tissue_or_cell_type
    Purified heme oxygenase-1

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 576–587

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Product-bound human HO-1 structure · source_derived_draft · unverified_draft

    ### iron-heme-oxygenase Heme oxygenase oxidatively cleaves heme to biliverdin with release of iron and carbon monoxide. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Breaking open heme makes its iron available for reuse. organism: Human enzyme tissue_or_cell_type: Purified heme oxygenase-1 experimental_model: Product-bound human HO-1 structure limitations: Product release interpretation from structure; no in-vivo flux measurement. exposure: Biliverdin-bound structure compared with heme-bound enzyme evidence_span: {"source_cache": "artifacts/iron-research/15049686.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "76bcb8ae12316350b1161f32c1633e2b5c752fcbf7e158940385b354ee3452d2", "start_char": 0, "end_char": 1167, "text_sha256": "76bcb8ae12316350b1161f32c1633e2b5c752fcbf7e158940385b354ee3452d2"} [iron-p15049686] Crystal structure of human heme oxygenase-1 in a complex with biliverdin. (2004). https://pubmed.ncbi.nlm.nih.gov/15049686/ DOI: 10.1021/bi035451l
    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