Pyridine coenzymes

Upon preincubation with urea, various 3- or 4-substituted N-methylpyridinium salts form charge-transfer complexes with tryptophan containing proteins such as, L-chymotrypsin and lysozyme. The complexes were studied by using the difference spectrophotometric technique. The fluorescence examination showed that tryptophyl residues in protein molecules are engaged in the complex formation process. The complex formation reactions proceed at a considerable rate. The stopped-flow method was used to determine the pseudo first order rate constants. A linear dependence of the pseudo first order rate constants with the donor concentration was found. The second order rate constants were obtained by dividing the mean value of the pseudo first order rate constants by the initial donor concentration for each run. The linear dependence of second order rate constants with the electron affinity of the acceptors can serve as a criterion for the formation of charge-transfer complexes.

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Pyridine coenzymes

Cited by 14 publications

References 11 publications

Pyridine coenzymes. VII. Catalysis of the hydration of the reduced form by iodoaromatic compounds

Pyridine coenzymes. VII. Catalysis of the hydration of the reduced form by iodoaromatic compounds

Intramolecular charge‐transfer interaction between the oxidized and reduced forms of nicotinamide in a polymeric system. NAD coenzyme model

The kinetics of complex formation of tryptophan containing proteins with pyridinium salts

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