Component
The high-spin Fe(IV)-oxo reaction intermediate of a 2-oxoglutarate dioxygenase
The high-spin Fe(IV)-oxo reaction intermediate of a 2-oxoglutarate dioxygenase. 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
A prolyl-4-hydroxylase, a functional homologue of human 2-oxoglutarate-dependent dioxygenases with essential roles in collagen biosynthesis and oxygen sensing, accumulated a C-H-cleaving high-spin Fe(IV)-oxo intermediate with a large substrate deuterium kinetic isotope effect on its decay.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/hbot-research/17003127.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8c7def7926cf3f7a38d874fe22494fa3b72477ed41bdd2baee407cab4ea0d96d", "start_char": 0, "end_char": 1302, "text_sha256": "8c7def7926cf3f7a38d874fe22494fa3b72477ed41bdd2baee407cab4ea0d96d"}
- experimental_model
- Stopped-flow, optical absorption and Mossbauer spectroscopy of a prolyl-4-hydroxylase reaction
- exposure
- Catalysis with saturating substrates and deuterated substrate
- limitations
- Spectroscopy on a functional homologue, not the human enzyme. It identifies the chemical intermediate that does the work.
- 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
- Bacterial enzyme homologous to the human enzymes
- plain_language
- The iron atom briefly becomes a highly reactive form that rips a hydrogen off the target carbon.
- primary_references
- [hbot-p17003127] Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. (2006). https://pubmed.ncbi.nlm.nih.gov/17003127/ DOI: 10.1073/pnas.0604005103
- tissue_or_cell_type
- Purified enzyme
Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 894–905
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stopped-flow, optical absorption and Mossbauer spectroscopy of a prolyl-4-hydroxylase reaction · source_derived_draft · unverified_draft
### hbot-fe-iv-intermediate A prolyl-4-hydroxylase, a functional homologue of human 2-oxoglutarate-dependent dioxygenases with essential roles in collagen biosynthesis and oxygen sensing, accumulated a C-H-cleaving high-spin Fe(IV)-oxo intermediate with a large substrate deuterium kinetic isotope effect on its decay. 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 iron atom briefly becomes a highly reactive form that rips a hydrogen off the target carbon. organism: Bacterial enzyme homologous to the human enzymes tissue_or_cell_type: Purified enzyme experimental_model: Stopped-flow, optical absorption and Mossbauer spectroscopy of a prolyl-4-hydroxylase reaction limitations: Spectroscopy on a functional homologue, not the human enzyme. It identifies the chemical intermediate that does the work. exposure: Catalysis with saturating substrates and deuterated substrate evidence_span: {"source_cache": "artifacts/hbot-research/17003127.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8c7def7926cf3f7a38d874fe22494fa3b72477ed41bdd2baee407cab4ea0d96d", "start_char": 0, "end_char": 1302, "text_sha256": "8c7def7926cf3f7a38d874fe22494fa3b72477ed41bdd2baee407cab4ea0d96d"} [hbot-p17003127] Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. (2006). https://pubmed.ncbi.nlm.nih.gov/17003127/ DOI: 10.1073/pnas.0604005103
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.