Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum.

ABSTRACT: Phenylalanine hydroxylase (PheH) is a pterin-dependent, mononuclear nonheme iron(II) oxygenase that uses the oxidative power of O₂ to hydroxylate phenylalanine to form tyrosine. PheH is a member of a superfamily of O₂-activating enzymes that utilizes a common metal binding motif: the 2-His-1-carboxylate facial triad. Like most members of this superfamily, binding of substrates to PheH results in a reorganization of its active site to allow O₂ activation. Exploring the energetics of each step before O₂ activation can provide mechanistic insight into the initial steps that support the highly specific O₂ activation pathway carried out by this metalloenzyme. Here the thermal stability of PheH and its substrate complexes were investigated u

SUBMITTER: Li M 

PROVIDER: S-EPMC10184773 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature