ArticleNature chemistry2016
Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins.
Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Photoinduced proton transfer in differently structured water: an EPR approach to solving a classic problem.Scientific reports · 2026Article
- Water Networks in Photosystem II Using Crystalline Molecular Dynamics Simulations and Room-Temperature XFEL Serial Crystallography.Journal of the American Chemical Society · 2023Article
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- Electronic Structure Changes of an Aromatic Amine Photoacid along the Förster Cycle.Angewandte Chemie (International ed. in English) · 2022Article
- Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed byJournal of the American Chemical Society · 2021Article
- Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore.Journal of the American Chemical Society · 2020Article
- Deciphering the selectivity of inhibitor MKC9989 towards residue K907 in IRE1α; a multiscaleRSC advances · 2020Article
- Ultrafast Proton Transport between a Hydroxy Acid and a Nitrogen Base along Solvent Bridges Governed by the Hydroxide/Methoxide Transfer Mechanism.Journal of the American Chemical Society · 2019Article
- Water assisted biomimetic synergistic process and its application in water-jet rewritable paper.Nature communications · 2018Article
- Excited State Structural Evolution of a GFP Single-Site Mutant Tracked by Tunable Femtosecond-Stimulated Raman Spectroscopy.Molecules (Basel, Switzerland) · 2018Article
- Multiscale modelization in a small virus: Mechanism of proton channeling and its role in triggering capsid disassembly.PLoS computational biology · 2018Article
- Origins of Enzyme Catalysis: Experimental Findings for C-H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs.Journal of the American Chemical Society · 2017Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Directional proton transport along 'wires' that feed biochemical reactions in proteins is poorly understood. Amino-acid residues with high pKa are seldom considered as active transport elements in such wires because of their large classical barrier for proton dissociation. Here, we use the light-triggered proton wire of the green fluorescent protein to study its ground-electronic-state proton-transport kinetics, revealing a large temperature-dependent kinetic isotope effect. We show that 'deep' proton tunnelling between hydrogen-bonded oxygen atoms with a typical donor-acceptor distance of 2.7-2.8 Å fully accounts for the rates at all temperatures, including the unexpectedly large value (2.5 × 10(9) s(-1)) found at room temperature. The rate-limiting step in green fluorescent protein is assigned to tunnelling of the ionization-resistant serine hydroxyl proton. This suggests how high-pKa residues within a proton wire can act as a 'tunnel diode' to kinetically trap protons and control the direction of proton flow.
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