ArticleBiochemistry2014
Transiently produced hypochlorite is responsible for the irreversible inhibition of chlorite dismutase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Biochemical and structural characterization of chlorite dismutase enzyme from Pseudomonas aeruginosa.The FEBS journal · 2025Article
- Deciphering the role of the distal pocket in Staphylococcus aureus coproheme decarboxylase.Journal of inorganic biochemistry · 2025Article
- Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine.Biochemistry · 2023Article
- Chlorine redox chemistry is widespread in microbiology.The ISME journal · 2023Article
- A genetically encoded system for oxygen generation in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mechanisms of chlorate toxicity and resistance in Pseudomonas aeruginosa.Molecular microbiology · 2022Article
- Roles of High-valent Hemes and pH Dependence in Halite Decomposition Catalyzed by Chlorite Dismutase fromACS catalysis · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis.Biochemistry · 2021Article
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020Article
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- Heterologous expression of the gene for chlorite dismutase from Ideonella dechloratans is induced by an FNR-type transcription factor.MicrobiologyOpen · 2020Article
- Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage.The Journal of biological chemistry · 2018Article
- Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.Biochemistry · 2018Article
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Chemical reviews · 2018Review
- Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.Biochemistry · 2018Article
- Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.ACS catalysis · 2017Article
- Active Sites of OBiochemistry · 2017Article
- Characterizing Isozymes of Chlorite Dismutase for Water Treatment.Frontiers in microbiology · 2017Article
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Chlorite dismutases (Clds) are heme b-containing prokaryotic oxidoreductases that catalyze the reduction of chlorite to chloride with the concomitant release of molecular oxygen. Over time, they are irreversibly inactivated. To elucidate the mechanism of inactivation and investigate the role of the postulated intermediate hypochlorite, the pentameric chlorite dismutase of "Candidatus Nitrospira defluvii" (NdCld) and two variants (having the conserved distal arginine 173 exchanged with alanine and lysine) were recombinantly produced in Escherichia coli. Exchange of the distal arginine boosts the extent of irreversible inactivation. In the presence of the hypochlorite traps methionine, monochlorodimedone, and 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]benzoic acid, the extent of chlorite degradation and release of molecular oxygen is significantly increased, whereas heme bleaching and oxidative modifications of the protein are suppressed. Among other modifications, hypochlorite-mediated formation of chlorinated tyrosines is demonstrated by mass spectrometry. The data obtained were analyzed with respect to the proposed reaction mechanism for chlorite degradation and its dependence on pH. We discuss the role of distal Arg173 by keeping hypochlorite in the reaction sphere for O-O bond formation.
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