How do enzymes activate oxygen without inactivating themselves?

Abstract

Detailed analyses of the oxidative half-reactions of glucose oxidase and soybean lipoxygenase provide insight into Nature's solution to the "trouble with oxygen". Coupled with studies of other O2-activating enzymes, two key features emerge. The first is the predominance of a rate-limiting transfer of the first electron transfer to O2, with subsequent electron and proton transfers occurring in rapid steps. The second feature is the identification of non-metal binding sites and channels for O2. These permit a controlled reactivity of oxygen to generate the desired regio- and stereochemical products, while minimizing deleterious side reactions.