Biosynthesis of riboflavin: mechanism of formation of the ribitylamino linkage
- 23 February 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (4) , 1117-1120
- https://doi.org/10.1021/bi00404a006
Abstract
Feeding experiments with Ashbya gossypii followed by NMR analysis of the resulting riboflavin showed incorporation of deuterium from D-[2-2H]ribose at C-2'' and from D-[1-2H]ribose in the pro-R position at C-1'' of the ribityl side chain. The results rule out an Amadori rearrangement mechanism for the reduction of the ribosylamino to the ribitylamino linkage and point to formation of a Schiff base that is reduced stereospecifically opposite to the fact from which the oxygen has departed. As prerequisite for the analysis, the 1H NMR signals for the pro-R and pro-S hydrogens at C-1'' of 6,7-dimethyl-8-ribityllumazine and riboflavin and its tetraacetate were assigned with the aid of synthetic stereospecifically deuteriated samples.This publication has 8 references indexed in Scilit:
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