Biosynthesis of riboflavin: mechanism of formation of the ribitylamino linkage

Journal Article · Tue Feb 23 00:00:00 EST 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00404a006· OSTI ID:5272366

Keller, P J; Van, Q L; Kim, S U; Bown, D H; Chen, H C; Kohnle, A; Bacher, A; Floss, H G

Feeding experiments with Ashbya gossypii followed by NMR analysis of the resulting riboflavin showed incorporation of deuterium from D-(2-/sup 2/H)ribose at C-2' and from D-(1-/sup 2/H) 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 face from which the oxygen has departed. As prerequisite for the analysis, the /sup 1/H 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.

• Research Organization: Ohio State Univ., Columbus (USA)
• OSTI ID: 5272366
• Journal Information: Biochemistry; (United States), Vol. 27:4
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
DEUTERIUM COMPOUNDS
UPTAKE
RIBOFLAVIN
BIOSYNTHESIS
NUCLEAR MAGNETIC RESONANCE
PROTONS
SCHIFF BASES
BARYONS
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
IMINES
MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
RESONANCE
SYNTHESIS
VITAMIN B GROUP
VITAMINS
550201* - Biochemistry- Tracer Techniques