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Significance Many enzymes harness the energy of molecular oxygen to catalyze diverse transformations. However, reaction with oxygen is kinetically challenging and must be precisely controlled to prevent cellular damage. The formylglycine-generating enzyme activates its targets by utilizing a mononuclear copper center to facilitate oxidation of a substrate cysteine. We reveal the structure of its atypical copper active site and discover that substrate binding directly to copper precedes and initiates reactivity toward oxygen. We furthermore identify a transient intermediate that may provide evidence for the involvement of an elusive catalytic species. This work uncovers a distinct strategy among copper enzymes that exploits a dynamic binding site to tightly couple the activation of oxygen with selective substrate oxidation.

Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O 2 activation

Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O ₂ activation