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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1982 Jun;79(11):3480–3484. doi: 10.1073/pnas.79.11.3480

Synthesis and biological activity of a profluorescent analogue of coenzyme B12.

M S Rosendahl, G M Omann, N J Leonard
PMCID: PMC346444  PMID: 7048307

Abstract

We describe here the synthesis and chemical properties of linear(lin)-benzoadenosylcobalamin, a coenzyme B12 analogue that has a laterally extended nucleoside in the upper axial position. It is an effective competitive inhibitor of ribonucleotide reductase from Lactobacillus leichmannii. lin-Benzoadenosylcobalamin is nonfluorescent in solution but, on homolytic (light) or heterolytic (acid, cyanide) cleavage of the carbon-cobalt bond, forms fluorescent products. In addition, fluorescence is detectable on binding of the coenzyme analogue to ribonucleotide reductase, and the observed fluorescence polarization of the lin-benzoadenosyl moiety indicates that it is bound loosely to the enzyme when the coenzyme is partially dissociated.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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