Human myeloperoxidase catalyzes an oscillating peroxidase-oxidase reaction

We have studied the peroxidase-oxidase reaction catalyzed by human myeloperoxidase in an open system where both substrates-molecular oxygen and NADH-are supplied continuously to the reaction mixture. The reaction shows oscillatory kinetics at pH values around 5, provided that the reaction medium in addition to the enzyme and the substrates also contains an aromatic electron mediator such as melatonin or 4-hydroxybenzoic acid and chloride ions at concentrations >1mM.

The experimental findings can be simulated by a detailed model of the reaction. The results are important for our understanding of oxidant production in neutrophils.