Myoglobin kinetic parameters

The single potential step chronoabsorptometry technique has been employed to determine the heterogeneous electron transfer kinetic parameters of myoglobin [36], horse heart cytochrome c [37] and soluble spinach ferredoxin [38]. In every case, the chronoabsorptometric data were analysed according to the irreversible model (the reverse reaction is ignored). The error associated with the use of this model for the kinetic analysis of these systems is most pronounced at low overpotentials, long transient times, and large reaction rates. 

Edmund E. Bowden conducted potential step chronoabsorptometry experiments on the reaction of myoglobin at modified gold minigrid electrodes [40]. Although these experiments were very reproducible, the heterogeneous electron transfer kinetic parameters raised concerns, namely, the rate constant was very low (k° = 3.9 X 10-11 cm/s) and alpha was high (a = 0.88). These issues became muted as the work progressed, as will be discussed below. 

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