ArticleArchives of biochemistry and biophysics2015
Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.
Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes.The FEBS journal · 2026Article
- Insights into the flexibility of the domain-linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations.Protein science : a publication of the Protein Society · 2025Article
- Molecular interactions between gelatin-derived carbon quantum dots and Apo-myoglobin: Implications for carbon nanomaterial frameworks.International journal of biological macromolecules · 2024Article
- The alternative coproporphyrinogen III oxidase (CgoN) catalyzes the oxygen-independent conversion of coproporphyrinogen III into coproporphyrin III.Frontiers in microbiology · 2024Article
- Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site.Journal of the American Chemical Society · 2023Article
- Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme.Biomolecules · 2023Article
- Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW.Biochemistry · 2023Article
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- Inhibitory Effect of Select Nitrocompounds and Chlorate againstPathogens (Basel, Switzerland) · 2022Article
- Mitochondrial COA7 is a heme-binding protein with disulfide reductase activity, which acts in the early stages of complex IV assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae.Biophysical journal · 2021Article
- Lipocalin Blc is a potential heme-binding protein.FEBS letters · 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
- Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.The FEBS journal · 2020Article
- A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation.ACS catalysis · 2020Article
- Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to HemeACS catalysis · 2019Article
- The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis.Journal of inorganic biochemistry · 2019Article
- Review
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Chlorite dismutase-like proteins are structurally closely related to functional chlorite dismutases which are heme b-dependent oxidoreductases capable of reducing chlorite to chloride with simultaneous production of dioxygen. Chlorite dismutase-like proteins are incapable of performing this reaction and their biological role is still under discussion. Recently, members of this large protein family were shown to be involved in heme biosynthesis in Gram-positive bacteria, and thus the protein was renamed HemQ in these organisms. In the present work the structural and heme binding properties of the chlorite dismutase-like protein from the Gram-positive pathogen Listeria monocytogenes (LmCld) were analyzed in order to evaluate its potential role as a regulatory heme sensing protein. The homopentameric crystal structure (2.0Å) shows high similarity to chlorite-degrading chlorite dismutases with an important difference in the structure of the putative substrate and heme entrance channel. In solution LmCld is a stable hexamer able to bind the low-spin ligand cyanide. Heme binding is reversible with KD-values determined to be 7.2μM (circular dichroism spectroscopy) and 16.8μM (isothermal titration calorimetry) at pH 7.0. Both acidic and alkaline conditions promote heme release. Presented biochemical and structural data reveal that the chlorite dismutase-like protein from L. monocytogenes could act as a potential regulatory heme sensing and storage protein within heme biosynthesis.
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