ArticleBiochemistry2013
Water networks in fast proton transfer during catalysis by human carbonic anhydrase II.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 57 citations in OpenAlex.
- Structural basis for multi-subunit DNA-dependent RNA polymerase catalytic activity.Molecular cell · 2026Article
- Carbonic anhydrase under the computational lens: a review of advances, challenges, and future directions.Journal of molecular modeling · 2026Review
- GRACE: Generative Redesign in Artificial Computational Enzymology.ACS synthetic biology · 2024Article
- Carbonic Anhydrase Robustness for Use in Nanoscale COACS omega · 2023Article
- Proton transfer reactions: From photochemistry to biochemistry and bioenergetics.BBA advances · 2023Article
- The Solvation-Induced Onsager Reaction Field Rather than the Double-Layer Field Controls COJACS Au · 2022Article
- Inhibition of Carbonic Anhydrase Using SLC-149: Support for a Noncatalytic Function of CAIX in Breast Cancer.Journal of medicinal chemistry · 2021Article
- Conformational Change of H64 and Substrate Transportation: Insight Into a Full Picture of Enzymatic Hydration of COFrontiers in chemistry · 2021Article
- Article
- Extreme Catalytic Power of Ketosteroid Isomerase Related to the Reversal of Proton Dislocations in Hydrogen-Bond Network.The journal of physical chemistry. B · 2020Article
- 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
- Insights Into the Origin of Life: Did It Begin from HCN and HACS central science · 2019Article
- The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior.International journal of molecular sciences · 2018Article
- Exploring the Potential Roles of Band 3 and Aquaporin-1 in Blood COFrontiers in physiology · 2018Review
- Structure activity study of carbonic anhydrase IX: Selective inhibition with ureido-substituted benzenesulfonamides.European journal of medicinal chemistry · 2017Article
- A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Thermostable Carbonic Anhydrases in Biotechnological Applications.International journal of molecular sciences · 2015Review
- Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors.BioMed research international · 2015Review
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II.Archives of biochemistry and biophysics · 2013Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Variants of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with water molecules in the active-site cavity have provided insights into the proton transfer rates in this protein environment. X-ray crystallography and (18)O exchange measured by membrane inlet mass spectrometry have been used to investigate structural and catalytic properties of variants of HCA II containing replacements of Tyr7 with Phe (Y7F) and Asn67 with Gln (N67Q). The rate constants for transfer of a proton from His64 to the zinc-bound hydroxide during catalysis were 4 and 9 μs(-1) for Y7F and Y7F/N67Q, respectively, compared with a value of 0.8 μs(-1) for wild-type HCA II. These higher values observed for Y7F and Y7F/N67Q HCA II could not be explained by differences in the values of the pK(a) of the proton donor (His64) and acceptor (zinc-bound hydroxide) or by the orientation of the side chain of the proton shuttle residue His64. They appeared to be associated with a reduced level of branching in the networks of hydrogen-bonded water molecules between proton shuttle residue His64 and the zinc-bound solvent molecule as observed in crystal structures at 1.5-1.6 Å resolution. Moreover, Y7F/N67Q HCA II is unique among the variants studied in having a direct, hydrogen-bonded chain of water molecules between the zinc-bound solvent and N(ε) of His64. This study provides the clearest example to date of the relevance of ordered water structure to rate constants for proton transfer in catalysis by carbonic anhydrase.
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