A general method for the electrochemical evaluation of the bimolecular rate constant in enzyme catalyzed reaction kinetics

A general working curve in terms of the ratio of the kinetic limiting current of bioelectrocatalysis to the diffusion-controlled current recorded in the absence of the enzyme reaction versus the k[E] (k=bimolecular rate constant, [E]=enzyme concentration) group at high concentration of the substrate and at very low mediator concentration was constructed. The curve allows one to evaluate the bimolecular catalytic constant for one- or two-electron mediator from voltammetric data recorded at a fixed scan rate

The use of cyclic voltammetric measurements for the determination of kinetic constants in enzyme-based electrocatalysis. The case of the redox mediated dihydronicotinamide adenine dinucleotide oxidation catalysed by flavoproteins

On the basis of simulated voltammetric curves used as testing data, practical methods to extract the bimolecular rate constant for a mediated enzymatic catalysis with an excess of the substrate are examined. The evaluation criteria are the simplicity of treatment and the agreement between the expected and the obtained values of the rate constants. The results obtained indicate that the different approaches examined are equivalent