Component
Diiron catalytic center
Diiron catalytic center. Species, exposure and limitations are retained in each linked claim.
2 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 it acts on
Human MIOX contains a diiron catalytic center involved in oxygen-dependent inositol cleavage.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/inositol-research/18364358.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19", "start_char": 0, "end_char": 1004, "text_sha256": "9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19"}
- experimental_model
- Human enzyme crystallography and catalytic analysis
- exposure
- Diiron center and inhibitor-bound structure
- limitations
- Catabolism of inositol is not evidence that humans synthesize vitamin C from it; the crystal ligand was an inhibitor.
- nutrient_topic
- Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
- organism
- Homo sapiens
- plain_language
- Two iron atoms are part of this breakdown enzyme, linking inositol metabolism to iron chemistry.
- primary_references
- [ino-p18364358] Structural and biophysical characterization of human myo-inositol oxygenase. (2008). https://pubmed.ncbi.nlm.nih.gov/18364358/ DOI: 10.1074/jbc.m800348200
- tissue_or_cell_type
- Purified MIOX
Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 470–481
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme crystallography and catalytic analysis · source_derived_draft · unverified_draft
### ino-miox-iron Human MIOX contains a diiron catalytic center involved in oxygen-dependent inositol cleavage. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two iron atoms are part of this breakdown enzyme, linking inositol metabolism to iron chemistry. organism: Homo sapiens tissue_or_cell_type: Purified MIOX experimental_model: Human enzyme crystallography and catalytic analysis limitations: Catabolism of inositol is not evidence that humans synthesize vitamin C from it; the crystal ligand was an inhibitor. exposure: Diiron center and inhibitor-bound structure evidence_span: {"source_cache": "artifacts/inositol-research/18364358.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19", "start_char": 0, "end_char": 1004, "text_sha256": "9992644d489f26782d7ef0a70dc13ec5ca48e2b660a011173fba8e0d4e43ae19"} [ino-p18364358] Structural and biophysical characterization of human myo-inositol oxygenase. (2008). https://pubmed.ncbi.nlm.nih.gov/18364358/ DOI: 10.1074/jbc.m800348200
Complete structured claim and evidence
Where it participates (unsigned role)
COQ7 hydroxylation assays consumed NADH in a substrate-dependent manner.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"}
- experimental_model
- Purified reconstructed COQ metabolon with short-chain substrates
- exposure
- Enzyme combinations, methyl donors, reductants and metal additions
- limitations
- Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.
- nutrient_topic
- Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
- organism
- Reconstructed ancestral tetrapod proteins
- plain_language
- Niacin-derived reducing power also feeds a later synthesis step.
- primary_references
- [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
- tissue_or_cell_type
- Stepwise CoQ head-group assembly
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 723–734
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft
### coq10-coq7-nadh COQ7 hydroxylation assays consumed NADH in a substrate-dependent manner. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Niacin-derived reducing power also feeds a later synthesis step. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 23488, "end_char": 27391, "text_sha256": "7147c9d517477cd7bbec4a155e5f13bc733d294380975977eba11b64517047f3"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z
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.