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The PHD- and FIH-catalyzed reactions and outline of the proposed consensus mechanism for 2OG-dependent oxygenases. A, prolyl hydroxylation performed by PHD2; B, asparaginyl hydroxylation as performed by FIH; C, O2 binding subsequent to formation of the enzyme·substrate complex leads to 2OG decarboxylation with the formation of an Fe(IV)-oxo intermediate, which then performs oxidative modification of the “prime” substrate (e.g. HIF-α).
