Hydrogen Peroxide → Iodide Ion

Participants

Reaction Steps

In a second set of experiments, glucose oxidase (D-glucose:oxygen 1-oxidoreductase; EC 1.1.3.4) (1 mg/ml) and horseradish peroxidase (donor:hydrogen-peroxide oxidoreductase; EC 1.11.1.7) (0.5 mg/ml) made up in 10 mM sodium phosphate buffer, 150 mM NaCl, pH 7.4, was loaded into the inner reservoir of the mechanical device. The device ring was closed and rinsed under distilled water. The device was then placed in a beaker containing approximately 20 ml 150 mM potassium iodide and 100 mg/ml glucose made up in distilled water. No formation of elemental iodine, evident by the appearance of the yellow triiodide complex, occurred in the external medium even after leaving the ring submerged in the solution over a period of approximately 8 hours. At the end of the experiment, the ring was squeezed about its outer circumference to distort its shape into an ellipsoid. This latter operation triggered the appearance of triiodide in the external medium (verified as elemental iodine by chloroform extraction and identification of its characteristic violet color in chloroform), indicating that egress of glucose oxidase and horseradish peroxidase had occurred as a result of distortion of the ring, presenting the enzymes formerly contained within the inner reservoir to the substrates in the external medium. This allows for elemental iodine to be formed via oxidation of glucose and subsequent peroxidation of iodide in the external medium.

Provenance & Evidence