Component
Ergothioneine-copper(I) complex
Context-specific entity; species, compartment and exposure are stated on each 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
Ergothioneine at 0.1-1 mM protected DNA and albumin against 0.1 mM copper with ascorbate or peroxide.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Cell-free copper/ascorbate and copper/peroxide systems.
- limitations
- Exposure and free-metal speciation limit extrapolation.
- nutrient_topic
- Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
- plain_language
- Binding the catalyst can protect several targets.
- primary_references
- Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t
Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 128–134
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free copper/ascorbate and copper/peroxide systems. · source_derived_draft · unverified_draft
## ergothioneine-copper-oxidation Binding the catalyst can protect several targets. Ergothioneine at 0.1-1 mM protected DNA and albumin against 0.1 mM copper with ascorbate or peroxide. Model: Cell-free copper/ascorbate and copper/peroxide systems. Limitations: Exposure and free-metal speciation limit extrapolation. Evidence access: Primary abstract Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t
Complete structured claim and evidence
Where it participates (unsigned role)
Ergothioneine bound copper(I), rather than copper(II), and formed a redox-inactive complex in the tested chemical systems.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Spectroscopy and competition against histidine/phenanthroline.
- limitations
- This is not demonstrated copper depletion in humans.
- nutrient_topic
- Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
- plain_language
- Copper oxidation state matters for binding.
- primary_references
- Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t
Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 120–126
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Spectroscopy and competition against histidine/phenanthroline. · source_derived_draft · unverified_draft
## ergothioneine-copper-binding Copper oxidation state matters for binding. Ergothioneine bound copper(I), rather than copper(II), and formed a redox-inactive complex in the tested chemical systems. Model: Spectroscopy and competition against histidine/phenanthroline. Limitations: This is not demonstrated copper depletion in humans. Evidence access: Primary abstract Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t
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.