Vitamin B12 (Methylcobalamin)
Methylcobalamin is one of the two coenzyme forms of cobalamin found in mammalian biochemistry, the other being adenosylcobalamin. All cobalamins are built around a corrin ring holding a central cobalt atom, and what distinguishes the forms is the upper axial ligand on that cobalt. In methylcobalamin it is a methyl group; in cyanocobalamin, the synthetic form used in most fortification chemistry, it is a cyanide ion, which is stable but is not a coenzyme and must be converted before it is biochemically active.
That distinction is the reason methylcobalamin is stocked separately as a reference material. A cobalt-carbon bond is unusual in biology, and it is the only organometallic bond in mammalian enzymology. It is also deliberately weak, and the chemistry of B12-dependent enzymes turns on how the protein manipulates that weakness. Methylcobalamin is the cofactor of methionine synthase, where the methyl group is transferred intact rather than homolysed, which makes it the non-radical member of the pair.
Technical Specifications
| Property | Specification |
|---|---|
| Product Name | Vitamin B12 (methylcobalamin) |
| Synonyms | Mecobalamin, methyl-B12, MeCbl |
| CAS Number | 13422-55-4 |
| Molecular Formula | C₆₃H₉₁CoN₁₃O₁₄P |
| Molecular Weight | 1344.38 g/mol |
| Chemical Class | Cobalamin; organometallic cobalt corrinoid |
| Axial Ligand | Methyl (upper); dimethylbenzimidazole (lower) |
| Appearance | Dark red solution, supplied in a 20 mL vial |
| Solubility Profile | Aqueous solution; markedly light-sensitive |
| Solution Base | Deionized Water, Benzyl Alcohol |
Research Applications & Mechanism of Action
Methylcobalamin functions as the methyl carrier for methionine synthase, which transfers a methyl group from 5-methyltetrahydrofolate to homocysteine to give methionine. That single reaction is the junction between the folate cycle and the methionine cycle, so cobalamin availability constrains one-carbon metabolism as a whole, including the supply of S-adenosylmethionine for downstream methylation.
The structural literature on B12-dependent enzymes is the more mechanistically informative body of work. Crystallography of these enzymes showed that the cobalt-nitrogen bond to the protein histidine is unusually long compared with free cobalamin, which is interpreted as the protein deliberately weakening the metal-carbon bond to favour the reactive species. The enzyme, in other words, does chemistry to its own cofactor.
Primary fields of in vitro and preclinical laboratory investigation include:
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Enzyme Cofactor Assays: Reconstituting methionine synthase and related cobalamin-dependent enzymes to measure activity as a function of cofactor form.
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One-Carbon Metabolism: Tracking homocysteine, methionine and S-adenosylmethionine pools in cell-free and cultured systems.
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Organometallic Spectroscopy: Using the characteristic corrinoid absorbance and the cobalt oxidation state as spectroscopic handles for binding and photolysis studies.
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Cofactor Form Comparison: Benchmarking methylcobalamin against cyanocobalamin, hydroxocobalamin and adenosylcobalamin in the same assay.
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Analytical Reference Work: A defined corrinoid standard for chromatographic and mass-spectrometric method development.
Selected Research Literature
Peer-reviewed structural and enzymological literature indexed on PubMed, provided for scientific context only. Nothing here describes or implies a use for this material.
- Mancia F, Keep NH, Nakagawa A, et al. How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution. Structure. 1996;4(3):339-350. doi:10.1016/s0969-2126(96)00037-8
- Reitzer R, Gruber K, Jogl G, et al. Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights. Structure. 1999;7(8):891-902. doi:10.1016/s0969-2126(99)80116-6
Assay note. The cobalt-carbon bond is photolabile. Methylcobalamin solutions lose the methyl ligand under ordinary laboratory lighting, converting to hydroxocobalamin, and an unexplained loss of cofactor activity is more often a lighting problem than a chemistry one. Amber glassware and low light during preparation are the difference between measuring the compound and measuring its photolysis product.
Analytical Documentation
Purity, identity, and composition vary by manufacturing lot. Kimera Chems does not publish a single fixed purity figure for this item; refer to the batch-specific Certificate of Analysis (COA) issued for the lot received, which reflects third-party analytical testing for that lot. Contact us if a COA for your lot is required.
Storage & Handling
Store at controlled room temperature. Do not refrigerate or freeze. Cold storage may cause the solution to cloud or precipitate. If this occurs, return to room temperature and mix until clear.
Storage guidance is a house recommendation. Analytical documentation is per-lot release testing.
Related Research Compounds
Research Use Disclaimer
Research Use Only Disclaimer: This product is developed and distributed strictly as a Research Use Only (RUO) laboratory reference chemical intended exclusively for non-clinical analytical and scientific investigation. It is not an FDA-approved drug, medical treatment, dietary supplement, or food ingredient, and is strictly prohibited for human or animal consumption. Kimera Chems supplies this research material solely to qualified institutions and professional investigators for authorized laboratory research.
