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Curr Opin Chem Biol. 1998 Oct;2(5):650-5.

The function of adenosylcobalamin in the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii.

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Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.


Ribonucleoside triphosphate reductase from Lactobacillus leichmannii catalyzes the reduction of nucleotides to deoxynucleotides and uses adenosylcobalamin as a cofactor. A transient protein-based thiyl radical is essential for catalysis. Studies directed toward the elucidation of the function of adenosylcobalamin during catalysis have shown that formation of the thiyl radical and 5'-deoxyadenosine occurs in a concerted fashion with C-Co bond homolysis, that the homolysis is entropically and not enthalpically driven, that the dimethylbenzimidazole moiety of adenosylcobalamin is the axial ligand during catalysis, and that the C-Co bond is reformed after every turnover.

[Indexed for MEDLINE]

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