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Chemical Compound Review

Dimedazol     5,6-dimethyl-1H-benzoimidazole

Synonyms: Dimesol, Dimezol, Dimedazole, PubChem7550, Dimezol base, ...
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Disease relevance of Dimedazole


High impact information on Dimedazole

  • These structures reveal that the B12 cofactor undergoes a major conformational change on binding to the apoenzymes of methionine synthase and methylmalonyl-coenzyme A mutase: The dimethylbenzimidazole ligand to the cobalt is displaced by a histidine residue from the protein [6].
  • Two mutants that lead to severe impairment (mut0) are Gly-630 --> Glu and Gly-703 --> Arg, which map to the binding site for the dimethylbenzimidazole nucleotide substituent of adenosylcobalamin [7].
  • In vivo data showed that the lack of cobC function blocks the synthesis of cobalamin from its precursors cobinamide and 5,6-dimethylbenzimidazole, i.e. it prevents the assembly of the nucleotide loop of cobalamin [8].
  • These measurements can be used to estimate the influence of the dimethylbenzimidazole ligand on both the thermodynamics and kinetics of methyl transfer between methyltetrahydrofolate and cob(I)alamin or cob(I)inamide [9].
  • Dimethylbenzimidazole contributes approximately 0.6 kcal/mol of stabilization for the forward reaction and approximately 2.2 kcal/mol of destabilization for the reverse reaction [9].

Chemical compound and disease context of Dimedazole


Biological context of Dimedazole


Anatomical context of Dimedazole


Associations of Dimedazole with other chemical compounds

  • Free dimethylbenzimidazole axial base-on cob(II)alamin was formed by photolysis of the corresponding adenosylcobalamin and cryotrapped in glycerol-aqueous glass [16].
  • These experiments reveal that one molecule of glycine is incorporated into 5,6-dimethylbenzimidazole moiety of vitamin B12 in a regiospecific manner [10].
  • Spectroscopic data show that the dimethylbenzimidazole group trans to the NO(2)(-) ligand is protonated and partially dechelated at pH 1, by which a reaction with NO is induced [17].
  • (15)N superhyperfine splitting in the EPR signals of the low-spin Co(2+) of B(12r), bound in the active site of EAL, indicates that the dimethylbenzimidazole moiety of the cofactor contributes the lower axial ligand consistent with "base-on" binding of coenzyme B(12) to EAL [18].
  • Examination of the role of base-off cobalamin species (where the 5,6-dimethylbenzimidazole ligand coordinated to cobalt is detached by protonation of the imidazole nitrogen) in differentiation between homolytic and heterolytic cobalt-carbon bond cleavage mechanisms is a primary step in better understanding B12-dependent enzyme catalysis [19].

Gene context of Dimedazole


Analytical, diagnostic and therapeutic context of Dimedazole


  1. Human vitamin B12 absorption measurement by accelerator mass spectrometry using specifically labeled (14)C-cobalamin. Carkeet, C., Dueker, S.R., Lango, J., Buchholz, B.A., Miller, J.W., Green, R., Hammock, B.D., Roth, J.R., Anderson, P.J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Sinorhizobium meliloti bluB is necessary for production of 5,6-dimethylbenzimidazole, the lower ligand of B12. Campbell, G.R., Taga, M.E., Mistry, K., Lloret, J., Anderson, P.J., Roth, J.R., Walker, G.C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Binding of Cob(II)alamin to the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii. Identification of dimethylbenzimidazole as the axial ligand. Lawrence, C.C., Gerfen, G.J., Samano, V., Nitsche, R., Robins, M.J., Rétey, J., Stubbe, J. J. Biol. Chem. (1999) [Pubmed]
  4. Biosynthesis of vitamin B12. Formation of free 5,6-dimethylbenzimidazole and alpha-ribazole from riboflavin by Propionibacterium freudenreichii. Hörig, J., Renz, P. FEBS Lett. (1977) [Pubmed]
  5. The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli. Lawrence, J.G., Roth, J.R. J. Bacteriol. (1995) [Pubmed]
  6. Structure-based perspectives on B12-dependent enzymes. Ludwig, M.L., Matthews, R.G. Annu. Rev. Biochem. (1997) [Pubmed]
  7. Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Drennan, C.L., Matthews, R.G., Rosenblatt, D.S., Ledley, F.D., Fenton, W.A., Ludwig, M.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. O'Toole, G.A., Trzebiatowski, J.R., Escalante-Semerena, J.C. J. Biol. Chem. (1994) [Pubmed]
  9. Cobalamin-dependent methionine synthase: probing the role of the axial base in catalysis of methyl transfer between methyltetrahydrofolate and exogenous cob(I)alamin or cob(I)inamide. Dorweiler, J.S., Finke, R.G., Matthews, R.G. Biochemistry (2003) [Pubmed]
  10. Biosynthesis of vitamin B12 in anaerobic bacteria. Mode of incorporation of glycine into the 5,6-dimethylbenzimidazole moiety in Eubacterium limosum. Lamm, L., Heckmann, G., Renz, P. Eur. J. Biochem. (1982) [Pubmed]
  11. Biosynthesis of vitamin B12 in anaerobic bacteria--experiments with Eubacterium limosum on the transformation of 5-hydroxy-6-methyl-benzimidazole, its nucleoside, its cobamide, and of 5-hydroxybenzimidazolylcobamide in vitamin B12. Schulze, B., Vogler, B., Renz, P. Eur. J. Biochem. (1998) [Pubmed]
  12. The end of the cob operon: evidence that the last gene (cobT) catalyzes synthesis of the lower ligand of vitamin B12, dimethylbenzimidazole. Chen, P., Ailion, M., Weyand, N., Roth, J. J. Bacteriol. (1995) [Pubmed]
  13. O-demethylase from Ap6tobacterium dehalogenans--cloning, sequencing, and active expression of the gene encoding the corrinoid protein. Kaufmann, F., Wohlfarth, G., Diekert, G. Eur. J. Biochem. (1998) [Pubmed]
  14. Antagonism of the lethal effects of cyanide by a synthetic water-soluble cobalt(III) porphyrin compound. McGuinn, W.D., Baxter, L., Pei, L., Petrikovics, I., Cannon, E.P., Way, J.L. Fundamental and applied toxicology : official journal of the Society of Toxicology. (1994) [Pubmed]
  15. Biosynthesis of vitamin B-12. Part I. Role of the ribosomal proteins in vitamin B-12 biosynthesis. Pezacka, E., Walerych, W. Biochim. Biophys. Acta (1981) [Pubmed]
  16. Identification of dimethylbenzimidazole axial coordination and characterization of (14)N superhyperfine and nuclear quadrupole coupling in Cob(II)alamin bound to ethanolamine deaminase in a catalytically-engaged substrate radical-Cobalt(II) biradical state. Ke, S.C., Torrent, M., Museav, D.G., Morokuma, K., Warncke, K. Biochemistry (1999) [Pubmed]
  17. Nitrite impurities are responsible for the reaction observed between vitamin B12 and nitric oxide in acidic aqueous solution. Roncaroli, F., Shubina, T.E., Clark, T., van Eldik, R. Inorganic chemistry. (2006) [Pubmed]
  18. Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B(12). Abend, A., Bandarian, V., Nitsche, R., Stupperich, E., Rétey, J., Reed, G.H. Arch. Biochem. Biophys. (1999) [Pubmed]
  19. Temperature dependent coordination effects in base-off adenosyl and methylcobalamin by X-ray edge spectroscopy. Wirt, M.D., Chance, M.R. J. Inorg. Biochem. (1993) [Pubmed]
  20. The cobT gene of Salmonella typhimurium encodes the NaMN: 5,6-dimethylbenzimidazole phosphoribosyltransferase responsible for the synthesis of N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole, an intermediate in the synthesis of the nucleotide loop of cobalamin. Trzebiatowski, J.R., O'Toole, G.A., Escalante-Semerena, J.C. J. Bacteriol. (1994) [Pubmed]
  21. Preparation, properties and biological activities of succinyl derivatives of vitamin B12. Toraya, T., Ohashi, K., Ueno, H., Fukui, S. Bioinorganic chemistry. (1975) [Pubmed]
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