ArticlePloS one2011
Structural studies of β-carbonic anhydrase from the green alga Coccomyxa: inhibitor complexes with anions and acetazolamide.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 56 citations in OpenAlex.
- Systematic modeling of porphyrin-based photosensitizers for inhibiting Mycobacterium tuberculosis β-Carbonic Anhydrases.Scientific reports · 2026Article
- Elucidating copper ion interactions with carbonic anhydrase: insights from fluorescence quenching and thermodynamic analysis.Photosynthetica · 2026Article
- Structural characterization and inhibition of carbonic anhydrase fromJournal of structural biology: X · 2025Article
- Azobenzenesulfonamide Carbonic Anhydrase Inhibitors as New Weapons to FightPharmaceuticals (Basel, Switzerland) · 2024Article
- Inhibition of α-, β- and γ-carbonic anhydrases from the pathogenic bacteriumJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Multimerization variants as potential drivers of neofunctionalization.Science advances · 2021Article
- Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- In Silico-Guided Identification of New Potent Inhibitors of Carbonic Anhydrases Expressed inACS medicinal chemistry letters · 2020Article
- Crystal Structure of β-Carbonic Anhydrase CafA from the Fungal PathogenMolecules and cells · 2020Article
- Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Comparison of the Anion Inhibition Profiles of the α-CA Isoforms (SpiCA1, SpiCA2 and SpiCA3) from the Scleractinian Coral Stylophora pistillata.International journal of molecular sciences · 2018Article
- Legionella pneumophila Carbonic Anhydrases: Underexplored Antibacterial Drug Targets.Pathogens (Basel, Switzerland) · 2016Review
- Carbon Dioxide "Trapped" in a β-Carbonic Anhydrase.Biochemistry · 2015Article
- Saturating light and not increased carbon dioxide under ocean acidification drives photosynthesis and growth in Ulva rigida (Chlorophyta).Ecology and evolution · 2015Article
- Bioinformatic analysis of beta carbonic anhydrase sequences from protozoans and metazoans.Parasites & vectors · 2014Article
- Preliminary X-ray crystallographic analysis of β-carbonic anhydrase psCA3 from Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The β-class carbonic anhydrases (β-CAs) are widely distributed among lower eukaryotes, prokaryotes, archaea, and plants. Like all CAs, the β-enzymes catalyze an important physiological reaction, namely the interconversion between carbon dioxide and bicarbonate. In plants the enzyme plays an important role in carbon fixation and metabolism. To further explore the structure-function relationship of β-CA, we have determined the crystal structures of the photoautotroph unicellular green alga Coccomyxa β-CA in complex with five different inhibitors: acetazolamide, thiocyanate, azide, iodide, and phosphate ions. The tetrameric Coccomyxa β-CA structure is similar to other β-CAs but it has a 15 amino acid extension in the C-terminal end, which stabilizes the tetramer by strengthening the interface. Four of the five inhibitors bind in a manner similar to what is found in complexes with α-type CAs. Iodide ions, however, make contact to the zinc ion via a zinc-bound water molecule or hydroxide ion--a type of binding mode not previously observed in any CA. Binding of inhibitors to Coccomyxa β-CA is mediated by side-chain movements of the conserved residue Tyr-88, extending the width of the active site cavity with 1.5-1.8 Å. Structural analysis and comparisons with other α- and β-class members suggest a catalytic mechanism in which the movements of Tyr-88 are important for the CO(2)-HCO(3)(-) interconversion, whereas a structurally conserved water molecule that bridges residues Tyr-88 and Gln-38, seems important for proton transfer, linking water molecules from the zinc-bound water to His-92 and buffer molecules.
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