Enzyme-like kinetics of ferryloxy myoglobin formation in films on electrodes in microemulsions

Covalently linked films of the ferric heme protein myoglobin and poly-L-lysine graphite electrodes reacted with tert-butylhydroperoxide (tBuOOH) to form ferryloxy protein species according to Michaelis-Menten enzyme kinetics. Apparent kinetic constants are most likely governed by acidity-controlled protein conformations and their binding with tBuOOH in the intermediate protein-substrate complex.