Component
The thioredoxin reductase C-terminal Gly-Cys-SeCys-Gly redox centre
The thioredoxin reductase C-terminal Gly-Cys-SeCys-Gly redox centre. 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.
Where it participates (unsigned role)
Mammalian thioredoxin reductase carries an essential selenocysteine in the conserved C-terminal sequence Gly-Cys-SeCys-Gly, forming a selenenylsulfide between Cys497 and SeCys498 that becomes a selenolthiol on reduction, alongside a separate Cys59-Cys64 disulfide identical to the glutathione reductase active site.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/hbot-research/10801974.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3", "start_char": 0, "end_char": 1719, "text_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3"}
- experimental_model
- Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase
- exposure
- Oxidised and NADPH-reduced enzyme states
- limitations
- Enzyme chemistry on purified protein. It establishes the selenium-containing active site; it is not a statement about selenium intake.
- 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
- Rat and human enzyme
- plain_language
- The enzyme’s working end is built from a selenium amino acid paired with a cysteine.
- primary_references
- [hbot-p10801974] Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. (2000). https://pubmed.ncbi.nlm.nih.gov/10801974/ DOI: 10.1073/pnas.100114897
- 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 452–463
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase · source_derived_draft · unverified_draft
### hbot-trxr-selenocysteine-site Mammalian thioredoxin reductase carries an essential selenocysteine in the conserved C-terminal sequence Gly-Cys-SeCys-Gly, forming a selenenylsulfide between Cys497 and SeCys498 that becomes a selenolthiol on reduction, alongside a separate Cys59-Cys64 disulfide identical to the glutathione reductase active site. 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 enzyme’s working end is built from a selenium amino acid paired with a cysteine. organism: Rat and human enzyme tissue_or_cell_type: Purified enzyme experimental_model: Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase limitations: Enzyme chemistry on purified protein. It establishes the selenium-containing active site; it is not a statement about selenium intake. exposure: Oxidised and NADPH-reduced enzyme states evidence_span: {"source_cache": "artifacts/hbot-research/10801974.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3", "start_char": 0, "end_char": 1719, "text_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3"} [hbot-p10801974] Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. (2000). https://pubmed.ncbi.nlm.nih.gov/10801974/ DOI: 10.1073/pnas.100114897
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.