Component
PRDX3
Cysteine-based peroxide reductase regenerated by thioredoxin; not a selenoprotein.
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
PRDX3 consumes hydrogen peroxide, forming water within the mitochondrial thioredoxin circuit.
Experimental context and source evidence
- cell_type
- cardiac mitochondria
- experimental_model
- Peroxide and redox measurements
- limitations
- Other mitochondrial peroxide defenses also contribute.
- organism
- mouse and guinea pig
Selenium: literature corrections and mechanism additions · lines 630–640
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Peroxide and redox measurements · secondary_verified · secondary_verified
## prdx3-reduces-mitochondrial-peroxide The relay ends in peroxide removal. PRDX3 consumes hydrogen peroxide, forming water within the mitochondrial thioredoxin circuit. Organism: mouse and guinea pig Cell type: cardiac mitochondria Experimental model: Peroxide and redox measurements Limitations: Other mitochondrial peroxide defenses also contribute. Primary reference: [Thioredoxin Reductase-2 Is Essential for Keeping Low Levels of H2O2 Emission from Isolated Heart Mitochondria](https://pubmed.ncbi.nlm.nih.gov/21832082/)
Complete structured claim and evidence
What acts on it
Reduced TXN2 regenerates the peroxide-reducing form of PRDX3.
Experimental context and source evidence
- cell_type
- cardiac mitochondria
- experimental_model
- Redox-state measurements
- limitations
- TXN2 and PRDX3 are not selenoproteins.
- organism
- mouse and guinea pig
Selenium: literature corrections and mechanism additions · lines 618–628
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Redox-state measurements · secondary_verified · secondary_verified
## txn2-regenerates-prdx3 Thioredoxin recharges a mitochondrial peroxide-removal enzyme. Reduced TXN2 regenerates the peroxide-reducing form of PRDX3. Organism: mouse and guinea pig Cell type: cardiac mitochondria Experimental model: Redox-state measurements Limitations: TXN2 and PRDX3 are not selenoproteins. Primary reference: [Thioredoxin Reductase-2 Is Essential for Keeping Low Levels of H2O2 Emission from Isolated Heart Mitochondria](https://pubmed.ncbi.nlm.nih.gov/21832082/)
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.