Mechanism of and exquisite selectivity for O-O bond formation by the heme-dependent chlorite dismutase.

ABSTRACT: Chlorite dismutase (Cld) is a heme b-dependent, O-O bond forming enzyme that transforms toxic chlorite (ClO(2)(-)) into innocuous chloride and molecular oxygen. The mechanism and specificity of the reaction with chlorite and alternate oxidants were investigated. Chlorite is the sole source of dioxygen as determined by oxygen-18 labeling studies. Based on ion chromatography and mass spectrometry results, Cld is highly specific for the dismutation of chlorite to chloride and dioxygen with no other side products. Cld does not use chlorite as an oxidant for oxygen atom transfer and halogenation reactions (using cosubstrates guaiacol, thioanisole, and monochlorodimedone, respectively). When peracetic acid or H(2)O(2) was used as an alternative oxidant, oxidation and oxygen atom transfer but not

SUBMITTER: Lee AQ 

PROVIDER: S-EPMC2572943 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature