cis-[Ru(2,9-Me(2)phen)(2)(OH(2))(2)](2+) reacts readily with chlorite at room temperature at pH 4.9 and 6.8. The ruthenium(II) complex can catalyze the disproportionation of chlorite to chlorate and chloride, the oxidation of chlorite to chlorine dioxide, as well as the oxidation of alcohols by chlorite.

Chloroperoxidase and horseradish peroxidase use NaClOz as both the oxidant and the halogen donor for the peroxidative chlorination of monochlorodimedone. Previous studies have shown that both horseradish peroxidase and chloroperoxidase can catalyze iodination reactions with hydrogen peroxide as the oxidant; however, only chloroperoxidase catalyzes chlorination reactions under these conditions. ...

Horseradish peroxidase and chlorite, NaC102, are able to catalyze chlorination of monochlorodimedone to form dichlorodimedone. Catalytic amounts of horseradish peroxidase act to disproportionate chlorite forming chlorine dioxide and chloride ion. The chlorine dioxide thus formed is responsible for the chlorination of monochlorodimedone. It was previously thought (Chiang, R., Rand-Meir, T., Maki...

A compilation of Fe-bearing chlorite analyses is used: (1) to investigate the Alfree di-trioctahedral (AFDT) substitution 2Fe +□ = 3(Mg,Fe) in chlorite; and (2) to estimate the composition of a ferri-sudoite end-member (Si3Al)[(Fe ,Mg)2Fe 3+ 2 □Al]O10(OH)8 within the chlorite solid-solution domain. According to our observations, up to two Fe cations might be allocated in the M2-M3 chlorite site...

Chlorite dismutases are prokaryotic heme b oxidoreductases that convert chlorite to chloride and dioxygen. It has been postulated that during turnover hypochlorite is formed transiently, which might be responsible for the observed irreversible inactivation of these iron proteins. The only charged distal residue in the heme cavity is a conserved and mobile arginine, but its role in catalysis and...

Acidified sodium chlorite cleaves isodityrosine and solubilizes covalently bound hydroxyproline-rich material from cell walls. This has been taken as evidence that isodityrosine acts as a cross-link holding the hydroxyproline-rich glycoprotein extensin in the cell wall. However, acidified chlorite was found to cleave peptide bonds in salt-soluble extensin and in bovine serum albumin (BSA). This...

The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Although structure and steady-state kinetics of Clds have been elucidated, many questions remain (e.g., the mechanism of chlorite cleavage and the pH dependence of the reaction). Here, we present high-resolution X-ray crystal structures of a dimeric Cld at pH 6.5 and 8.5, its fluoride and is...

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...

Semi-pelitic rocks ranging in grade from the prehnite–pumpellyite to the greenschist facies from southeastern Otago, New Zealand, have been investigated in order to evaluate the reactions leading to formation and breakdown of stilpnomelane. Detrital grains of mica and chlorite along with fine-grained authigenic illite and chlorite occur in lower-grade rocks with compactional fabric parallel to ...