87384-49-4

Upstream product

• 53406-00-1 3-carbamoyl-1-(2,4-dinitrophenyl)pyridinium chloride 
• 104-94-9 4-methoxy-aniline 

Downstream Products

• 87384-63-2 1-(4-methoxy-phenyl)-4-oxo-1,4-dihydro-pyridine-3-carboxylic acid amide 
• 87413-02-3 1-(para-methoxylphenyl)-1,4-dihydronicotinamide 

Relevant academic research and scientific papers

Thermodynamics and kinetics of the hydride-transfer cycles for 1-aryl-1,4-dihydronicotinamide and its 1,2-dihydroisomer

Five 1-(p-substituted phenyl)-1,4-dihydronicotinamides (GPNAH-1,4-H 2) and five 1-(p-substituted phenyl)-1,2-dihydronicotinamides (GPNAH-1,2-H2) were synthesized, which were used to mimic NAD(P)H coenzyme and its 1,2-dihydroisomer re

An old but simple and efficient method to elucidate the oxidation mechanism of NAD(P)H model 1-aryl-1,4-dihydronicotinamides by cations 2-methyl-5-nitroisoquinolium, tropylium, and xanthylium in aqueous solution

Cations 2-methyl-5-mitroisoquinplinium (IQ+), tropylium (T+), and xanthylium (Xn+) were treated by an NAD(P)H model 1-(p-substituted phenyl)-1.4-dihydronicotinamide series (1) in buffered aqueous solution to give the corresponding reduced products by accepting hydride. Effects of the 4-substituents of 1 on the reaction rates were investigated. Hammett's linear free energy relationship analysis on the three reactions of 1 provides the reaction constants of -0.48, -2.2, and -1.4 with IQ+, T+, and Xn+ as the hydride acceptors, respectively. Comparison of the present reactions with the reaction examples whose mechanisms are well-known, such as the reaction of 1 with a one-electron oxidant Fe(CN)6-3, shows that the active site of 1 in the oxidation with IQ+ is at the 4-position on the dihydropyridine ring but that the active site of 1 in the oxidations with T+ and Xn+ is at the 1-position, which is in agreement with the results from the Bronsted-type linear analysis and the relation studies of the logarithm of the second-order rate constants with the oxidation potentials of the hydride donors. According to the dependence of the reaction mechanism on the active site of 1, a conclusion can be made that the reaction of 1 with IQ+ proceeds by direct one-step hydride transfer mechanism, but the reactions of 1 with T+ and Xn+ would take place via multistep hydride transfer mechanism initiated by one-electron transfer.

REACTIVITY OF BIOLOGICALLY IMPORTANT REDUCED PYRIDINES V. RELATIVE IMPORTANCE OF ELECTRON VERSUS PROTON LOSS IN FERRICYANIDE-MEDIATED OXIDATION OF DIHYDRONICOTINAMIDES

Kinetics of ferricyanide-mediated oxidation of various 1-(4-substituted phenyl)-1,4-dihydronicotinamides were studied assuming either a rate determining initial electron loss or a rate determining proton loss following a rapid pre-equilibrium step.Values

POLAROGRAPHIC REDUCTION OF p-SUBSTITUTED 1-PHENYL-3-AMINOCARBONYLPYRIDINIUM SALTS

The substitution effect of different groups (H, NO2, COOH, Br, Cl, NHCOCH3, CH3, OCH3, OH, and N(C2H5)2) on the polarographic behaviour of p-substituted 1-phenyl-3-aminocarbonylpyridinium cations has been investigated, in particular on their half-wave pot

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

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.