ReviewJournal of the Royal Society, Interface2014
Proton transfer reactions and hydrogen-bond networks in protein environments.
Review in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed.
- Article
- Conformational Dynamics of Plasmepsin X during Inhibitor Binding.The journal of physical chemistry. B · 2026Article
- Mitigating alkaline instability induced by tyrosine-tyrosine repulsion in an FcγRIIIa-binding protein through phenylalanine substitution.Journal of biochemistry · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.Biochemistry · 2026Article
- Quantum Biology Using Ultrafast Integrative and Molecular Engineering Tools: A Perspective.Computational and structural biotechnology journal · 2026Review
- Parametrizing reaction probabilities for proton transfers in protic ionic liquids.Frontiers in chemistry · 2026Article
- Current perspectives on proton and electron transfer pathways in photosystem II water oxidation.Plant & cell physiology · 2025Review
- Structure of the D1-Val185Asn mutated photosystem II complex with slow O-O bond formation reveals changes in the Cl1 water channel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.bioRxiv : the preprint server for biology · 2025Article
- Revisiting the Proposed Protonated Water Cluster at the Exit Site of the Proton Transfer Pathway in Bacteriorhodopsin.The journal of physical chemistry. B · 2025Article
- Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Acid-Base Chemistry of Short Hydrogen Bonds: A Tale of Schrödinger's Cat in Glutamine-Derived Crystals.The journal of physical chemistry letters · 2025Article
- Photosystem II: Probing Protons and Breaking Barriers.Biochemistry · 2025Review
- Key Interaction Changes Determine the Activation Process of Human Parathyroid Hormone Type 1 Receptor.Journal of the American Chemical Society · 2025Article
- FTIR study of light-induced proton transfer and CaBiophysical journal · 2024Article
- Article
- Molecular Modeling and In Vitro Functional Analysis of the RGS12 PDZ Domain Variant Associated with High-Penetrance Familial Bipolar Disorder.International journal of molecular sciences · 2024Article
- Cooperativity and halonium transfer in the ternary NCI···CHJournal of molecular modeling · 2024Article
- Energetics of the H-Bond Network inBiochemistry · 2024Article
- Exploring the Deprotonation Process during Incorporation of a Ligand Water Molecule at the Dangling Mn Site in Photosystem II.The journal of physical chemistry. B · 2024Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In protein environments, proton transfer reactions occur along polar or charged residues and isolated water molecules. These species consist of H-bond networks that serve as proton transfer pathways; therefore, thorough understanding of H-bond energetics is essential when investigating proton transfer reactions in protein environments. When the pKa values (or proton affinity) of the H-bond donor and acceptor moieties are equal, significantly short, symmetric H-bonds can be formed between the two, and proton transfer reactions can occur in an efficient manner. However, such short, symmetric H-bonds are not necessarily stable when they are situated near the protein bulk surface, because the condition of matching pKa values is opposite to that required for the formation of strong salt bridges, which play a key role in protein-protein interactions. To satisfy the pKa matching condition and allow for proton transfer reactions, proteins often adjust the pKa via electron transfer reactions or H-bond pattern changes. In particular, when a symmetric H-bond is formed near the protein bulk surface as a result of one of these phenomena, its instability often results in breakage, leading to large changes in protein conformation.
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