ArticleProceedings of the National Academy of Sciences of the United States of America2015
Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 46 citations in OpenAlex.
- Critical evaluation of two neutron structures of Mn superoxide dismutase with quantum refinement.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Effect of Water Networks On Ligand Binding: Computational Predictions vs Experiments.Journal of chemical information and modeling · 2024Article
- Energetics and dynamics of the proton shuttle of carbonic anhydrase II.Cellular and molecular life sciences : CMLS · 2023Article
- Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase.Nature communications · 2021Article
- Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018Article
- Carbonic Anhydrases: Role in pH Control and Cancer.Metabolites · 2018Review
- Insights into the binding mode of sulphamates and sulphamides to hCA II: crystallographic studies and binding free energy calculations.Journal of enzyme inhibition and medicinal chemistry · 2017Article
- Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.Molecules (Basel, Switzerland) · 2017Review
- Review
- Article
- Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential.IUCrJ · 2015Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Human carbonic anhydrase II (HCA II) uses a Zn-bound OH(-)/H2O mechanism to catalyze the reversible hydration of CO2. This catalysis also involves a separate proton transfer step, mediated by an ordered solvent network coordinated by hydrophilic residues. One of these residues, Tyr7, was previously shown to be deprotonated in the neutron crystal structure at pH 10. This observation indicated that Tyr7 has a perturbed pKa compared with free tyrosine. To further probe the pKa of this residue, NMR spectroscopic measurements of [(13)C]Tyr-labeled holo HCA II (with active-site Zn present) were preformed to titrate all Tyr residues between pH 5.4-11.0. In addition, neutron studies of apo HCA II (with Zn removed from the active site) at pH 7.5 and holo HCA II at pH 6 were conducted. This detailed interrogation of tyrosines in HCA II by NMR and neutron crystallography revealed a significantly lowered pKa of Tyr7 and how pH and Tyr proximity to Zn affect hydrogen-bonding interactions.
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