ArticleProceedings of the National Academy of Sciences of the United States of America2009
Hydrogen bond dynamics in the active site of photoactive yellow protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Discovery of Quercetin as a Potential Entry Inhibitor of Nipah Virus: A Path Toward Antiviral Therapy.International journal of molecular sciences · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.Biochemistry · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.bioRxiv : the preprint server for biology · 2025Article
- Potent Inhibition of Chikungunya Virus Entry by a Pyrazole-Benzene Derivative: A Computational Study Targeting the E1-E2 Glycoprotein Complex.International journal of molecular sciences · 2025Article
- Proton transfer reactions: From photochemistry to biochemistry and bioenergetics.BBA advances · 2023Article
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Bioluminescence and Photoreception in Unicellular Organisms: Light-Signalling in a Bio-Communication Perspective.International journal of molecular sciences · 2021Review
- Article
- On the Case of the Misplaced Hydrogens.Chembiochem : a European journal of chemical biology · 2021Review
- New intranasal cross-linked mosapride xyloglucan pluronics micelles (MOS-XPMs) for reflux esophagitis disease:Journal of advanced research · 2020Article
- Computational prediction of active sites and ligands in different AHL quorum quenching lactonases and acylases.Journal of biosciences · 2020Article
- Visualization of H atoms in the X-ray crystal structure of photoactive yellow protein: Does it contain low-barrier hydrogen bonds?Protein science : a publication of the Protein Society · 2019Article
- Perturbation of Short Hydrogen Bonds in Photoactive Yellow Protein via Noncanonical Amino Acid Incorporation.The journal of physical chemistry. B · 2019Article
- Active-Site pKa Determination for Photoactive Yellow Protein Rationalizes Slow Ground-State Recovery.Biophysical journal · 2017Article
- Vibrational analysis on the revised potential energy curve of the low-barrier hydrogen bond in photoactive yellow protein.Computational and structural biotechnology journal · 2016Article
- (15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-Bis(dimethylamino)naphthalene.The journal of physical chemistry. B · 2015Article
- Proton transfer reactions and hydrogen-bond networks in protein environments.Journal of the Royal Society, Interface · 2014Review
- Strong ionic hydrogen bonding causes a spectral isotope effect in photoactive yellow protein.Biophysical journal · 2013Article
- Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- (1)H, (13)C, and (15)N resonance assignment of photoactive yellow protein.Biomolecular NMR assignments · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Hydrogen bonds play major roles in biological structure and function. Nonetheless, hydrogen-bonded protons are not typically observed by X-ray crystallography, and most structural studies provide limited insight into the conformational plasticity of individual hydrogen bonds or the dynamical coupling present within hydrogen bond networks. We report the NMR detection of the hydrogen-bonded protons donated by Tyr-42 and Glu-46 to the chromophore oxygen in the active site of the bacterial photoreceptor, photoactive yellow protein (PYP). We have used the NMR resonances for these hydrogen bonds to probe their conformational properties and ability to rearrange in response to nearby electronic perturbation. The detection of geometric isotope effects transmitted between the Tyr-42 and Glu-46 hydrogen bonds provides strong evidence for robust coupling of their equilibrium conformations. Incorporation of a modified chromophore containing an electron-withdrawing cyano group to delocalize negative charge from the chromophore oxygen, analogous to the electronic rearrangement detected upon photon absorption, results in a lengthening of the Tyr-42 and Glu-46 hydrogen bonds and an attenuated hydrogen bond coupling. The results herein elucidate fundamental properties of hydrogen bonds within the complex environment of a protein interior. Furthermore, the robust conformational coupling and plasticity of hydrogen bonds observed in the PYP active site may facilitate the larger-scale dynamical coupling and signal transduction inherent to the biological function that PYP has evolved to carry out and may provide a model for other coupled dynamic systems.
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