Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants : Structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins
The R2 protein of ribonucleotide reductase catalyzes the dioxygen- dependent one-electron oxidation of Tyr122 at a diiron-carboxylate site. Methane monooxygenase and related hydroxylases catalyze hydrocarbon hydroxylation at diiron sites structurally related to the one in R2. In protein R2, the likely reaction site for dioxygen is close to Phe208. The crystal structure of an iron ligand mutant R2,