Metal-Catalyzed Oxygenation Mechanisms

Oxygen is abundant and reactive, yet converting it into a useful chemical form without causing uncontrolled oxidative damage requires exquisite molecular machinery. Metalloenzymes accomplish this by binding dioxygen at metal centers—often iron, copper, or manganese—and steering it through a series of electron and proton transfers toward highly selective oxidation of specific bonds, a feat that synthetic chemists have spent decades trying to replicate and understand. Central puzzles include how short-lived, high-valent intermediates such as iron-oxo species are generated and stabilized just long enough to do useful chemistry, and how enzymes like cytochrome P450 and methane monooxygenase manage to hydroxylate inert carbon-hydrogen bonds under mild physiological conditions. Current work focuses on capturing these fleeting intermediates spectroscopically, disentangling the timing of proton and electron transfers, and translating those mechanistic insights into non-heme iron catalysts that could perform similar transformations in industrial or pharmaceutical synthesis.

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Keywords

Dioxygen ActivationMetalloenzymeOxygenation ReactionsProton-Coupled Electron TransferNon-Heme Iron CatalystsCytochrome P450 Enzymes