3909-32-8Relevant academic research and scientific papers
The use of immobilized enzymes in organic synthesis. Part 8. Oxidation of 1-aryl-3-carbamoylpyridinium chlorides by rabbit liver aldehyde oxidase and bovine milk xanthine oxidase
Angelino, S. A. G. F.,Buurman, D. J.,Plas, H. C. van der,Mueller, F.
, p. 331 - 336 (2007/10/02)
Oxidation of 1-aryl-3-carbamoylpyridinium chlorides with immobilized rabbit liver aldehyde oxidase gave predominantly 1-aryl-1,6-dihydro-6-oxo-3-pyridinecarboxamides, together with the corresponding 1-aryl-1,4-dihydro-4-oxo-3-pyridinecarboxamides.In general, the site of oxidation by this enzyme is determined by steric factors.The rate of oxidation by free aldehyde oxidase is very sensitive to electronic effects.A more electron-withdrawing aryl substituent increases the reaction rate for oxidation to 6-oxo product.Consequently, a positive ρ value of about 3.6 was calculated for free aldehyde oxidase.Oxidation of these compounds by bovinr milk xanthine oxidase yielded mainly 4-oxo products.Preparative-scale reactions with both free and immobilized xanthine oxidase gave low product yields.The oxidation rate of free xanthine oxidase is only slightly affected by substituents in the aryl group.
