The mechanism of azide activation of polyphenol oxidase II from tobacco.

Abstract

So far, azide has been consistently reported to act as an inhibitor of metal enzymes, especially copper proteins. The present work shows that azide can also act as an activator of polyphenol oxidase II (PPO II) from tobacco leaves. From the square-wave voltammetry of native PPO II, peroxide-PPO II complex and azide-PPO II complex, the reduction of nitro blue tetrazolium by the enzymes and activation of PPO II by peroxide it follows that the binding of azide to PPO II induces the formation of CuO(2)(2-)Cu in the active site of PPO II from CuO(2)(-)Cu in native PPO II. The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator.