Crystal Structure of Tyrosine Hydroxylase with Bound Cofactor Analogue and Iron at 2.3 Å Resolution:  Self-Hydroxylation of Phe300 and the Pterin-Binding Site

TyrOH is a non-heme iron enzyme which uses molecular oxygen to hydroxylate tyrosine to form l-dihydroxyphenylalanine (l-DOPA), and tetrahydrobiopterin to form 4a-hydroxybiopterin, in the rate-limiting step of the catecholamine biosynthetic pathway. The 2.3 Å crystal structure of the catalytic and te...

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