ArticleBiochemistry2014
Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry, and reactivity.
Article in Biochemistry, 2014. 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, 34 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
- Electrochemical and Spectroscopic Characterization of Co-Neuroglobin: A Bioelectrocatalyst for HInorganic chemistry · 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
- Unique Biradical Intermediate in the Mechanism of the Heme Enzyme Chlorite Dismutase.ACS catalysis · 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
- 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
- Distinguishing Active Site Characteristics of Chlorite Dismutases with Their Cyanide Complexes.Biochemistry · 2018Article
- Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments.Archives of biochemistry and biophysics · 2018Article
- Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.ACS catalysis · 2017Article
- Active Sites of OBiochemistry · 2017Article
- Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.The FEBS journal · 2016Article
- 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
- HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.Archives of biochemistry and biophysics · 2015Review
- Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.Archives of biochemistry and biophysics · 2015Review
- Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.Archives of biochemistry and biophysics · 2015Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
Abstract
Chlorite dismutases (Clds) are heme b containing oxidoreductases that convert chlorite to chloride and molecular oxygen. In order to elucidate the role of conserved heme cavity residues in the catalysis of this reaction comprehensive mutational and biochemical analyses of Cld from "Candidatus Nitrospira defluvii" (NdCld) were performed. Particularly, point mutations of the cavity-forming residues R173, K141, W145, W146, and E210 were performed. The effect of manipulation in 12 single and double mutants was probed by UV-vis spectroscopy, spectroelectrochemistry, pre-steady-state and steady-state kinetics, and X-ray crystallography. Resulting biochemical data are discussed with respect to the known crystal structure of wild-type NdCld and the variants R173A and R173K as well as the structures of R173E, W145V, W145F, and the R173Q/W146Y solved in this work. The findings allow a critical analysis of the role of these heme cavity residues in the reaction mechanism of chlorite degradation that is proposed to involve hypohalous acid as transient intermediate and formation of an O═O bond. The distal R173 is shown to be important (but not fully essential) for the reaction with chlorite, and, upon addition of cyanide, it acts as a proton acceptor in the formation of the resulting low-spin complex. The proximal H-bonding network including K141-E210-H160 keeps the enzyme in its ferric (E°' = -113 mV) and mainly five-coordinated high-spin state and is very susceptible to perturbation.
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