Component
Reversible oxygen binding by hemoglobin
Reversible oxygen binding by hemoglobin. Species, exposure and limitations are retained in each linked claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
Oxyhemoglobin structures resolved hydrogen bonding between the oxygen ligand and distal histidine in both alpha and beta subunits.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/iron-research/16765986.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "177ab81c08f82c99c81c69d1cb582e52216234e290066ae5aa380a887fb0e38c", "start_char": 0, "end_char": 1284, "text_sha256": "177ab81c08f82c99c81c69d1cb582e52216234e290066ae5aa380a887fb0e38c"}
- experimental_model
- High-resolution crystallographic comparison
- exposure
- 1.25 angstrom structural refinement
- limitations
- Structural oxygen-ligand geometry, not a supplementation or oxygen-delivery clinical trial.
- nutrient_topic
- Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
- organism
- Human hemoglobin A
- plain_language
- Hemoglobin holds oxygen at carefully organized heme sites so oxygen binding can be controlled.
- primary_references
- [iron-p16765986] 1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. (2006). https://pubmed.ncbi.nlm.nih.gov/16765986/ DOI: 10.1016/j.jmb.2006.05.036
- tissue_or_cell_type
- Purified oxy-, deoxy- and carbonmonoxyhemoglobin
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 537–548
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · High-resolution crystallographic comparison · source_derived_draft · unverified_draft
### iron-hemoglobin-oxygen-site Oxyhemoglobin structures resolved hydrogen bonding between the oxygen ligand and distal histidine in both alpha and beta subunits. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Hemoglobin holds oxygen at carefully organized heme sites so oxygen binding can be controlled. organism: Human hemoglobin A tissue_or_cell_type: Purified oxy-, deoxy- and carbonmonoxyhemoglobin experimental_model: High-resolution crystallographic comparison limitations: Structural oxygen-ligand geometry, not a supplementation or oxygen-delivery clinical trial. exposure: 1.25 angstrom structural refinement evidence_span: {"source_cache": "artifacts/iron-research/16765986.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "177ab81c08f82c99c81c69d1cb582e52216234e290066ae5aa380a887fb0e38c", "start_char": 0, "end_char": 1284, "text_sha256": "177ab81c08f82c99c81c69d1cb582e52216234e290066ae5aa380a887fb0e38c"} [iron-p16765986] 1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. (2006). https://pubmed.ncbi.nlm.nih.gov/16765986/ DOI: 10.1016/j.jmb.2006.05.036
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.