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Neutron Structure of Human Carbonic Anhydrase II: A Hydrogen-Bonded Water Network “Switch” Is Observed between pH 7.8 and 10.0

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/anie.201101753openalex-snapshot
Identification of the Elusive Hydronium Ion Exchanging Roles with a Proton in an Enzyme at Lower pH Values
inferredcites →https://doi.org/10.1016/j.molcatb.2009.04.018openalex-snapshot
Biocatalytic capture of CO2 with carbonic anhydrase and its transformation to solid carbonate
inferredcites →https://doi.org/10.1021/ar00145a005openalex-snapshot
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
inferredcites →https://doi.org/10.1021/ar7000588openalex-snapshot
Solvent-Mediated Proton Transfer in Catalysis by Carbonic Anhydrase
inferredcites →https://doi.org/10.1021/ar9501232openalex-snapshot
Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design
inferredcites →https://doi.org/10.1021/bi00102a005openalex-snapshot
Conformational mobility of His-64 in the Thr-200 .fwdarw. Ser mutant of human carbonic anhydrase II
inferredcites →https://doi.org/10.1021/bi00445a054openalex-snapshot
Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
inferredcites →https://doi.org/10.1021/bi00563a008openalex-snapshot
Carbon dioxide hydration activity of carbonic anhydrase in mixtures of water and deuterium oxide
inferredcites →https://doi.org/10.1021/bi0480279openalex-snapshot
Structural and Kinetic Characterization of Active-Site Histidine as a Proton Shuttle in Catalysis by Human Carbonic Anhydrase II,
inferredcites →https://doi.org/10.1021/bi602620kopenalex-snapshot
Speeding Up Proton Transfer in a Fast Enzyme: Kinetic and Crystallographic Studies on the Effect of Hydrophobic Amino Acid Substitutions in the Active Site of Human Carbonic Anhydrase II
inferredcites →https://doi.org/10.1021/bi8005434openalex-snapshot
Hydrogen Location in Stages of an Enzyme-Catalyzed Reaction: Time-of-Flight Neutron Structure of d -Xylose Isomerase with Bound d -Xylulose
inferredcites →https://doi.org/10.1021/bi901995nopenalex-snapshot
Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer
inferredcites →https://doi.org/10.1021/ja00025a005openalex-snapshot
Unexpected pH-dependent conformation of His-64, the proton shuttle of carbonic anhydrase II
inferredcites →https://doi.org/10.1021/ja8091938openalex-snapshot
Elucidation of the Proton Transport Mechanism in Human Carbonic Anhydrase II
inferredcites →https://doi.org/10.1021/jp021931vopenalex-snapshot
Is a “Proton Wire” Concerted or Stepwise? A Model Study of Proton Transfer in Carbonic Anhydrase
inferredcites →https://doi.org/10.1038/nchem.1122openalex-snapshot
The many faces of a proton
inferredcites →https://doi.org/10.1074/jbc.m805353200openalex-snapshot
Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II
inferredcites →https://doi.org/10.1107/s0108768109030419openalex-snapshot
Eu3Si15 − x Al1 + x O x N23 − x (x ≃ 5/3) as a commensurate composite crystal

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Neutron Scattering Techniques and Applications in Structural Biology
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Complementary Information from Neutron Crystallography Studies
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The Active Site of a Prototypical “Rigid” Drug Target is Marked by Extensive Conformational Dynamics
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The Active Site of a Prototypical “Rigid” Drug Target is Marked by Extensive Conformational Dynamics
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Coordination Dynamics of Zinc Triggers the Rate Determining Proton Transfer in Human Carbonic Anhydrase II
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Effect of Glycosylation on the Reorganization at the Active Site of Human Carbonic Anhydrase IX
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Structures of Human Carbonic Anhydrases and Their Complexes with Inhibitors
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Correlations Between Inhibitor Binding Thermodynamics and Co-crystal Structures with Carbonic Anhydrases
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Kinetic Analysis of Carbonic Anhydrase–Sulfonamide Inhibitor Interactions
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Carbonic Anhydrases in Industrial Applications
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Catalytic Mechanism of α-Class Carbonic Anhydrases: CO2 Hydration and Proton Transfer
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Carbonic anhydrase under the computational lens: a review of advances, challenges, and future directions
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Protonation and conformational states of a catalytically important histidine sidechain at constant pH
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Biological Structures
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In silico approaches to biomacromolecules through conformational dynamics and catalysis
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Engineered Mammalian Carbonic Anhydrases for CO2 Capture
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Enzyme-catalyzed Solvents for CO2 Separation
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Large crystal growth for neutron protein crystallography
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Neutron crystallographic studies of carbonic anhydrase
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Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1016/j.abb.2015.11.033openalex-snapshot
Neutron protein crystallography: A complementary tool for locating hydrogens in proteins
inferred← citeshttps://doi.org/10.1016/j.bpj.2020.08.020openalex-snapshot
Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors
inferred← citeshttps://doi.org/10.1016/j.jcat.2024.115384openalex-snapshot
Bifunctional Metal-Acid Sites on Nickel Boride Catalysts:Phenol Hydrodeoxygenation and Water-Promoted C=C Hydrogenation
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Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative
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The use of neutron scattering to determine the functional structure of glycoside hydrolase
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"To Be or Not to Be" Protonated: Atomic Details of Human Carbonic Anhydrase-Clinical Drug Complexes by Neutron Crystallography and Simulation
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Solvent effects on catalytic reactions and related phenomena at liquid-solid interfaces
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Advances in biomimetic carbonic anhydrase strategies for CO2 capture
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Thermodynamic, kinetic, and structural parameterization of human carbonic anhydrase interactions toward enhanced inhibitor design
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Microbatch Mixing: “Shaken not Stirred”, a Method for Macromolecular Microcrystal Production for Serial Crystallography
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Spectrally Resolved Estimation of Water Entropy in the Active Site of Human Carbonic Anhydrase II
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Enhanced Sampling and Conformation-Dependent pKa of Histidine Side Chains: A Case Study in Human Carbonic Anhydrase II
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Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II
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Water-Mediated Heterogeneously Catalyzed Reactions
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Three Water Molecules Mediate Ring Opening of d -Glucose in Aqueous Solutions
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Neutron Diffraction of Acetazolamide-Bound Human Carbonic Anhydrase II Reveals Atomic Details of Drug Binding
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Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy
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Seeing the chemistry in biology with neutron crystallography
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Towards solvent regulated self-activation of N-terminal disulfide bond oxidoreductase-D
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Neutron macromolecular crystallography
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Opportunities and challenges in neutron crystallography
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Looking for Hydrogen Atoms: Neutron Crystallography Provides Novel Insights Into Protein Structure and Function
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Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography
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Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer
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Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase
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Structural insight into activity enhancement and inhibition of H64A carbonic anhydrase II by imidazoles
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Neutron structure of human carbonic anhydrase II in complex with methazolamide: mapping the solvent and hydrogen-bonding patterns of an effective clinical drug
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Neutron crystallography aids in drug design
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Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography
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Active-site solvent replenishment observed during human carbonic anhydrase II catalysis.
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Structure and mechanism of copper–carbonic anhydrase II: a nitrite reductase
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Preliminary time-of-flight neutron diffraction studies ofEscherichia coliABC transport receptor phosphate-binding protein at the Protein Crystallography Station
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Structural comparison of protiated, H/D-exchanged and deuterated human carbonic anhydrase IX
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XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
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Limiting the effects of radiation damage in MicroED through dose selection during data processing
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Crystallography and Its Impact on Carbonic Anhydrase Research
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Joint neutron and x-ray crystal structure of human carbonic anhydrase IX mimic (saccharin-sugar conjugate complex)
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Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules
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Neutron diffraction for deciphering protein‐carbohydrate interactions involved in bacterial infection
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