ArticleACS catalysis2017
Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.
Article in ACS catalysis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 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
- Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin.Bioscience reports · 2025Article
- Widespread occurrence of dissolved oxygen anomalies, aerobic microbes, and oxygen-producing metabolic pathways in apparently anoxic environments.FEMS microbiology ecology · 2024Review
- Ray-tracing analytical absorption correction for X-ray crystallography based on tomographic reconstructions.Journal of applied crystallography · 2024Article
- Utilizing the oxygen-atom trapping effect of CoProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Iron species activating chlorite: Neglected selective oxidation for water treatment.Environmental science and ecotechnology · 2023Article
- Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine.Biochemistry · 2023Article
- Roles of High-valent Hemes and pH Dependence in Halite Decomposition Catalyzed by Chlorite Dismutase fromACS catalysis · 2022Article
- Unique Biradical Intermediate in the Mechanism of the Heme Enzyme Chlorite Dismutase.ACS catalysis · 2021Article
- 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
- Semi-empirical model to estimate ideal conditions for the growth of large protein crystals.Acta crystallographica. Section D, Structural biology · 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
- An enzymatic method for precise oxygen affinity measurements over nanomolar-to-millimolar concentration regime.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Probing the role of the conserved residue Glu166 in a class A β-lactamase using neutron and X-ray protein crystallography.Acta crystallographica. Section D, Structural biology · 2020Article
- Improving the accuracy and resolution of neutron crystallographic data by three-dimensional profile fitting of Bragg peaks in reciprocal space.Acta crystallographica. Section D, Structural biology · 2018Article
- Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.Biochemistry · 2018Article
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Authors and funding
13 authors at 5 institutions in 4 countries.
Funding
Abstract
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 isothiocyanate complexes and the neutron structure at pH 9.0 together with the pH dependence of the Fe(III)/Fe(II) couple, and the UV-vis and resonance Raman spectral features. We demonstrate that the distal Arg127 cannot act as proton acceptor and is fully ionized even at pH 9.0 ruling out its proposed role in dictating the pH dependence of chlorite degradation. Stopped-flow studies show that (i) Compound I and hypochlorite do not recombine and (ii) Compound II is the immediately formed redox intermediate that dominates during turnover. Homolytic cleavage of chlorite is proposed.
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Registered trials
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