Deoxyribonucleotide synthesis: 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

What acts on it

Human RRM2 radical-center tyrosine mutations abolished the detectable stable radical and ribonucleotide-reductase activity in the tested assays.
Human ribonucleotide reductase small subunit RRM2 → Deoxyribonucleotide synthesis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/iron-research/16373698.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc", "start_char": 0, "end_char": 1165, "text_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc"}
experimental_model
Mutagenesis, EPR and catalytic assays
exposure
Conserved tyrosine mutations around the diiron center
limitations
Purified enzyme mechanisms; no recommendation to increase dietary iron for DNA synthesis.
nutrient_topic
Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
organism
Human RRM2 and RRM2B proteins
plain_language
DNA building-block synthesis needs a functioning iron/radical enzyme system.
primary_references
[iron-p16373698] A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases. (2005). https://pubmed.ncbi.nlm.nih.gov/16373698/ DOI: 10.1158/1535-7163.mct-05-0273
tissue_or_cell_type
Ribonucleotide reductase small subunits
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1174–1185
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mutagenesis, EPR and catalytic assays · source_derived_draft · unverified_draft
### iron-rrm2-iron-radical Human RRM2 radical-center tyrosine mutations abolished the detectable stable radical and ribonucleotide-reductase activity in the tested assays. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: DNA building-block synthesis needs a functioning iron/radical enzyme system. organism: Human RRM2 and RRM2B proteins tissue_or_cell_type: Ribonucleotide reductase small subunits experimental_model: Mutagenesis, EPR and catalytic assays limitations: Purified enzyme mechanisms; no recommendation to increase dietary iron for DNA synthesis. exposure: Conserved tyrosine mutations around the diiron center evidence_span: {"source_cache": "artifacts/iron-research/16373698.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc", "start_char": 0, "end_char": 1165, "text_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc"} [iron-p16373698] A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases. (2005). https://pubmed.ncbi.nlm.nih.gov/16373698/ DOI: 10.1158/1535-7163.mct-05-0273
Complete structured claim and evidence
The corresponding conserved-tyrosine perturbation also disabled the radical and catalytic activity of the human p53R2/RRM2B system.
Human p53-inducible ribonucleotide reductase small subunit / RRM2B → Deoxyribonucleotide synthesis source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/iron-research/16373698.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc", "start_char": 0, "end_char": 1165, "text_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc"}
experimental_model
Mutagenesis, EPR and catalytic assays
exposure
Conserved tyrosine mutations around the diiron center
limitations
Purified enzyme mechanisms; no recommendation to increase dietary iron for DNA synthesis.
nutrient_topic
Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
organism
Human RRM2 and RRM2B proteins
plain_language
The related small subunit is recorded separately so its role is not lost inside a generic enzyme label.
primary_references
[iron-p16373698] A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases. (2005). https://pubmed.ncbi.nlm.nih.gov/16373698/ DOI: 10.1158/1535-7163.mct-05-0273
tissue_or_cell_type
Ribonucleotide reductase small subunits
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1187–1198
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mutagenesis, EPR and catalytic assays · source_derived_draft · unverified_draft
### iron-rrm2b-iron-radical The corresponding conserved-tyrosine perturbation also disabled the radical and catalytic activity of the human p53R2/RRM2B system. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The related small subunit is recorded separately so its role is not lost inside a generic enzyme label. organism: Human RRM2 and RRM2B proteins tissue_or_cell_type: Ribonucleotide reductase small subunits experimental_model: Mutagenesis, EPR and catalytic assays limitations: Purified enzyme mechanisms; no recommendation to increase dietary iron for DNA synthesis. exposure: Conserved tyrosine mutations around the diiron center evidence_span: {"source_cache": "artifacts/iron-research/16373698.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc", "start_char": 0, "end_char": 1165, "text_sha256": "0d3e9b3d6c8961f94af38195eab5b0b3180c321da1c7ca75ae956036a60b16cc"} [iron-p16373698] A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases. (2005). https://pubmed.ncbi.nlm.nih.gov/16373698/ DOI: 10.1158/1535-7163.mct-05-0273
Complete structured claim and evidence

Where it participates (unsigned role)

Recovery of thioredoxin reductase activity over four days paralleled the return of the cells to a normal rate of growth, and the authors conclude that full activity of TrxR1, required for production of deoxyribonucleotides for DNA synthesis, is essential for normal growth of oxygen-challenged cells.
Thioredoxin reductase catalytic activity → Human lens epithelial cell growth source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
experimental_model
Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
exposure
99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
limitations
Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
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 cells
plain_language
The cells could not start dividing again until that enzyme came back.
primary_references
[hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
tissue_or_cell_type
Lens epithelium
trigger_kind
machinery_impairment Imported condition classification; unverified.
Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 400–411
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft
### hbot-trxr-growth-requirement Recovery of thioredoxin reductase activity over four days paralleled the return of the cells to a normal rate of growth, and the authors conclude that full activity of TrxR1, required for production of deoxyribonucleotides for DNA synthesis, is essential for normal growth of oxygen-challenged cells. Condition category: machinery_impairment 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 cells could not start dividing again until that enzyme came back. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
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.

Deoxyribonucleotide synthesis