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- W27343837 endingPage "277" @default.
- W27343837 startingPage "233" @default.
- W27343837 abstract "Dioxygen is a unique reagent for biological systems being at once thermodynamically reactive and kinetically stable. Life in a sea of oxygen is possible because oxygenase and oxidase enzymes have evolved that allow the inherent reactivity of dioxygen to be realized in a controlled manner that maintains specificity. Monooxygenases are a class of such enzymes that catalyze the activation of dioxygen through reductive cleavage of the OoO bond with the incorporation of one oxygen atom into the product and the release of the second as water. Numerous mechanistic strategies are used within the monooxygenase family, but a cofactor of some type is generally required to facilitate the binding and reduction of dioxygen. Typically, hemes, metal ions, flavins, pterins, and similar redox active species are bound by the enzyme and perform this function. The cofactor selected depends to some extent on the type of" @default.
- W27343837 created "2016-06-24" @default.
- W27343837 creator A5019917073 @default.
- W27343837 creator A5028504081 @default.
- W27343837 date "2000-01-01" @default.
- W27343837 modified "2023-10-16" @default.
- W27343837 title "Electron Transfer and Radical Forming Reactions of Methane Monooxygenase" @default.
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