C-H Bond Cleavage Is Rate-Limiting for Oxidative C-P Bond Cleavage by the Mixed Valence Diiron-Dependent Oxygenase PhnZ.

ABSTRACT: PhnZ utilizes a mixed valence diiron(II/III) cofactor and O₂ to oxidatively cleave the carbon-phosphorus bond of (R)-2-amino-1-hydroxyethylphosphonic acid to form glycine and orthophosphate. The active site residues Y24 and E27 are proposed to mediate induced-fit recognition of the substrate and access of O₂ to one of the active site Fe ions. H62 is proposed to deprotonate the C1-hydroxyl of the substrate during catalysis. Kinetic isotope effects (KIEs), pH-rate dependence, and site-directed mutagenesis were used to probe the rate-determining transition state and the roles of these three active site residues. Primary deuterium KIE values of 5.5 ± 0.3 for ^D(V) and 2.2 ± 0.4 for ^D(V/K) were measured with (R)-2-amino[1-

SUBMITTER: Gama SR 

PROVIDER: S-EPMC7176486 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature