Biliverdin: molecular mechanisms & dependencies

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.

Human evidence only

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)

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
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

The events it takes part in

A mechanism often involves more than two components. These are the full events, with every participant and its role.

Situations it appears in

Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

Open hypotheses

Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.

This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

Biliverdin