39580
5,6-Dimethylbenzimidazole
purum, ≥99.0% (NT)
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About This Item
Empirical Formula (Hill Notation):
C9H10N2
CAS Number:
Molecular Weight:
146.19
Beilstein:
116595
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
grade
purum
Assay
≥99.0% (NT)
mp
202-205 °C (lit.)
202-205 °C
SMILES string
Cc1cc2nc[nH]c2cc1C
InChI
1S/C9H10N2/c1-6-3-8-9(4-7(6)2)11-5-10-8/h3-5H,1-2H3,(H,10,11)
InChI key
LJUQGASMPRMWIW-UHFFFAOYSA-N
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Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Peter J Anderson et al.
Journal of bacteriology, 190(4), 1160-1171 (2007-11-06)
Corrinoid (vitamin B12-like) cofactors contain various alpha-axial ligands, including 5,6-dimethylbenzimidazole (DMB) or adenine. The bacterium Salmonella enterica produces the corrin ring only under anaerobic conditions, but it can form "complete" corrinoids aerobically by importing an "incomplete" corrinoid, such as cobinamide
Ruibing Wang et al.
Dalton transactions (Cambridge, England : 2003), (18)(18), 3584-3589 (2009-04-22)
Cucurbit[7]uril (CB[7]) forms very stable complexes with the alpha-axial 5,6-dimethylbenzimidazole (alpha-DMB) nucleotide base when dissociated from the Co(III) center in vitamin B(12) (CNCbl, K(CB[7]) = (7.5 +/- 0.5) x 10(4) dm(3) mol(-1)) and coenzyme B(12) (AdoCbl, K(CB[7]) = (3.02 +/-
Xiao-Lei Wang et al.
Journal of the American Chemical Society, 133(11), 4079-4091 (2011-02-25)
BluB is a distinct flavin destructase that catalyzes a complex oxygen-dependent conversion of reduced flavin mononucleotide (FMNH(2)) to form 5,6-dimethylbenzimidazole (DMB), the lower ligand of vitamin B(12). The catalyzed mechanism remains a challenge due to the discrepancy between the complexity
Finding the final pieces of the vitamin B12 biosynthetic jigsaw.
Martin J Warren
Proceedings of the National Academy of Sciences of the United States of America, 103(13), 4799-4800 (2006-03-29)
Pseudo-B12 joins the cofactor family.
Michiko E Taga et al.
Journal of bacteriology, 190(4), 1157-1159 (2007-12-18)
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