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Abstract
Recently the amide-oxygen has been suggested to participate in the formation of the corrin ring of vitamin B12. To confirm this hypothesis, 17O-labeled aminolevulinic acid (ALA) was prepared and administered to Propionibacterium shermanii. The isolated vitamin B12 showed only broad 17O signals in the oxygen-17 nuclear magnetic resonance (17O-NMR) spectrum. However, distinct isotope-shifted peaks were observed in the 13C-NMR spectrum of vitamin B12 isolated after incorporation of [1-13C:1,4-18O2]ALA. Of these shifted peaks, one peak (C27) showed very low intensity. This indicates that dilution of 18O occurred at the acetyl chain of the A ring of vitamin B12. This result supports the assumption that the lactone formation of the A ring promotes the ring contraction, as proposed by Eschenmoser.
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