Component
Aquocobalamin
Water-ligated cobalt(III) cobalamin; acid-base partner of hydroxocobalamin, kept chemically distinct.
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 acts on it
Purified human CblC/MMACHC supported GSH-dependent reduction of aquocobalamin to cob(II)alamin efficiently under anaerobic conditions; the human reaction was oxygen-sensitive.
Experimental context and source evidence
- cross_nutrient
- true
- evidence_location
- Abstract; indexed primary Results summary
- experimental_model
- Purified human MMACHC; oxygen-controlled biochemical assay
- exposure
- GSH and specified B12 form under anaerobic versus aerobic conditions
- limitations
- Abstract-level extraction; stronger aerobic activity of the C. elegans enzyme must not be attributed to human MMACHC.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Glutathione could supply reducing power, but oxygen strongly affected this human-protein reaction.
- primary_references
- [li-2014-gsh-electron] Glutathione-dependent one-electron transfer reactions catalyzed by a B12 trafficking protein (2014). https://pubmed.ncbi.nlm.nih.gov/24742678/ DOI: 10.1074/jbc.M114.567339
- tissue_or_cell_type
- Cell-free assay
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 781–793
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MMACHC; oxygen-controlled biochemical assay · source_derived_draft · unverified_draft
### b12-human-gsh-reduction Purified human CblC/MMACHC supported GSH-dependent reduction of aquocobalamin to cob(II)alamin efficiently under anaerobic conditions; the human reaction was oxygen-sensitive. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione could supply reducing power, but oxygen strongly affected this human-protein reaction. organism: Homo sapiens tissue_or_cell_type: Cell-free assay experimental_model: Purified human MMACHC; oxygen-controlled biochemical assay limitations: Abstract-level extraction; stronger aerobic activity of the C. elegans enzyme must not be attributed to human MMACHC. exposure: GSH and specified B12 form under anaerobic versus aerobic conditions cross_nutrient: true evidence_location: Abstract; indexed primary Results summary [li-2014-gsh-electron] Glutathione-dependent one-electron transfer reactions catalyzed by a B12 trafficking protein (2014). https://pubmed.ncbi.nlm.nih.gov/24742678/ DOI: 10.1074/jbc.M114.567339
Complete structured claim and evidenceReduced, full-length human MMADHC bound free aquocobalamin in vitro with a reported KD of 1.0 +/- 0.4 micromolar and formed a base-on thiolato-cob(III)alamin species.
Experimental context and source evidence
- cross_nutrient
- false
- evidence_location
- Abstract; indexed Results: CblD binds H2OCbl and forms a complex with CblC
- experimental_model
- Human full-length recombinant MMADHC binding assay
- exposure
- Reduction of cysteines followed by removal of excess DTT; free aquocobalamin
- limitations
- Slow binding and micromolar affinity make free aquocobalamin capture an uncertain physiological route; older no-binding results were condition-sensitive.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- MMADHC could bind this B12 form directly under the preparation conditions.
- primary_references
- [li-2020-co-s] An Interprotein Co-S Coordination Complex in the B12-Trafficking Pathway (2020). https://pubmed.ncbi.nlm.nih.gov/32871076/ DOI: 10.1021/jacs.0c06590
- tissue_or_cell_type
- Cell-free assay
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 893–905
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human full-length recombinant MMADHC binding assay · source_derived_draft · unverified_draft
### b12-mmad-free-aquo-binding Reduced, full-length human MMADHC bound free aquocobalamin in vitro with a reported KD of 1.0 +/- 0.4 micromolar and formed a base-on thiolato-cob(III)alamin species. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: MMADHC could bind this B12 form directly under the preparation conditions. organism: Homo sapiens tissue_or_cell_type: Cell-free assay experimental_model: Human full-length recombinant MMADHC binding assay limitations: Slow binding and micromolar affinity make free aquocobalamin capture an uncertain physiological route; older no-binding results were condition-sensitive. exposure: Reduction of cysteines followed by removal of excess DTT; free aquocobalamin cross_nutrient: false evidence_location: Abstract; indexed Results: CblD binds H2OCbl and forms a complex with CblC [li-2020-co-s] An Interprotein Co-S Coordination Complex in the B12-Trafficking Pathway (2020). https://pubmed.ncbi.nlm.nih.gov/32871076/ DOI: 10.1021/jacs.0c06590
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.