An N1-hydrogen bonding model for flavin coenzyme.
A model flavin possessing a specific hydrogen bond to the N1-position has been synthesized. The redox potential has been measured in aqueous buffer and found to be shifted +21 mV as compared to a similar flavin lacking this hydrogen bond. The reaction of the N1-hydrogen-bonding model with sulfite and 1-benzyl-dihydronicotinamide were examined and compared with the non-hydrogen-bonded flavin. The N1-hydrogen bond did not accelerate the rate of sulfite ion or hydride addition to N5, however the N5-sulfite complex was stabilized by nearly 4-fold over a non-hydrogen-bonding model. The model flavins were also studied computationally.
Guo
Fengli
F
Department of Chemistry and Center for Molecular Toxicology, Vanderbilt University, VU Station B 351822, Nashville, TN 37235-1822, USA.
Chang
Bryan H
BH
Rizzo
Carmelo J
CJ
D003067:Coenzymes / Q000737:chemistry*; D005415:Flavins / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular
D003067:Coenzymes; D005415:Flavins