ArticleBiochemistry2012
Redox thermodynamics of high-spin and low-spin forms of chlorite dismutases with diverse subunit and oligomeric structures.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Biochemical and structural characterization of chlorite dismutase enzyme from Pseudomonas aeruginosa.The FEBS journal · 2025Article
- 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
- In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase-The Interplay of Key Amino Acids, pH, Buffer and Glycerol.International journal of molecular sciences · 2021Article
- 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
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.Biochemistry · 2018Article
- Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.The FEBS journal · 2016Article
- Article
- From chlorite dismutase towards HemQ - the role of the proximal H-bonding network in haeme binding.Bioscience reports · 2016Article
- Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425.Molecular microbiology · 2015Article
- Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015Article
- A dimeric chlorite dismutase exhibits O2-generating activity and acts as a chlorite antioxidant in Klebsiella pneumoniae MGH 78578.Biochemistry · 2015Article
- Production of dioxygen in the dark: dismutases of oxyanions.Metal ions in life sciences · 2015Review
- Investigation of ion binding in chlorite dismutases by means of molecular dynamics simulations.Biochemistry · 2014Article
- Transiently produced hypochlorite is responsible for the irreversible inhibition of chlorite dismutase.Biochemistry · 2014Article
- Chlorite dismutases - a heme enzyme family for use in bioremediation and generation of molecular oxygen.Biotechnology journal · 2014Review
- Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry, and reactivity.Biochemistry · 2014Article
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
Chlorite dismutases (Clds) are heme b-containing oxidoreductases that convert chlorite to chloride and dioxygen. In this work, the thermodynamics of the one-electron reduction of the ferric high-spin forms and of the six-coordinate low-spin cyanide adducts of the enzymes from Nitrobacter winogradskyi (NwCld) and Candidatus "Nitrospira defluvii" (NdCld) were determined through spectroelectrochemical experiments. These proteins belong to two phylogenetically separated lineages that differ in subunit (21.5 and 26 kDa, respectively) and oligomeric (dimeric and pentameric, respectively) structure but exhibit similar chlorite degradation activity. The E°' values for free and cyanide-bound proteins were determined to be -119 and -397 mV for NwCld and -113 and -404 mV for NdCld, respectively (pH 7.0, 25 °C). Variable-temperature spectroelectrochemical experiments revealed that the oxidized state of both proteins is enthalpically stabilized. Molecular dynamics simulations suggest that changes in the protein structure are negligible, whereas solvent reorganization is mainly responsible for the increase in entropy during the redox reaction. Obtained data are discussed with respect to the known structures of the two Clds and the proposed reaction mechanism.
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