ArticleThe journal of physical chemistry. B2013
Internal water and microsecond dynamics in myoglobin.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Residue-Specific Structural and Dynamical Coupling of Protein and Hydration Water Revealed by Molecular Dynamics Simulations.Biomolecules · 2025Article
- Effect of Exchange Dynamics on the NMR Relaxation of Water in Porous Silica.The journal of physical chemistry letters · 2024Article
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- Terahertz spectroscopy as a method for investigation of hydration shells of biomolecules.Biophysical reviews · 2023Review
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Water as an Intrinsic Structural Element in Cellulose Fibril Aggregates.The journal of physical chemistry letters · 2022Article
- In situ molecular imaging of adsorbed protein films in water indicating hydrophobicity and hydrophilicity.Scientific reports · 2020Article
- Water in protein hydration and ligand recognition.Journal of molecular recognition : JMR · 2019Review
- Slow Dynamics of Tryptophan-Water Networks in Proteins.Journal of the American Chemical Society · 2018Article
- Water Dynamics in the Hydration Shells of Biomolecules.Chemical reviews · 2017Review
- Perspective: Structure and ultrafast dynamics of biomolecular hydration shells.Structural dynamics (Melville, N.Y.) · 2017Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- Solvation and cavity occupation in biomolecules.Biochimica et biophysica acta · 2015Article
- Reptation-induced coalescence of tunnels and cavities in Escherichia Coli XylE transporter conformers accounts for facilitated diffusion.The Journal of membrane biology · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myoglobin (Mb) binds diatomic ligands, like O2, CO, and NO, in a cavity that is only transiently accessible. Crystallography and molecular simulations show that the ligands can migrate through an extensive network of transiently connected cavities but disagree on the locations and occupancy of internal hydration sites. Here, we use water (2)H and (17)O magnetic relaxation dispersion (MRD) to characterize the internal water molecules in Mb under physiological conditions. We find that equine carbonmonoxy Mb contains 4.5 ± 1.0 ordered internal water molecules with a mean survival time of 5.6 ± 0.5 μs at 25 °C. The likely locations of these water molecules are the four polar hydration sites, including one of the xenon-binding cavities, that are fully occupied in all high-resolution crystal structures of equine Mb. The finding that water escapes from these sites, located 17-31 Å apart in the protein, on the same μs time scale suggests a global exchange mechanism. We propose that this mechanism involves transient penetration of the protein by H-bonded water chains. Such a mechanism could play a functional role by eliminating trapped ligands. In addition, the MRD results indicate that 2 or 3 of the 11 histidine residues of equine Mb undergo intramolecular hydrogen exchange on a μs time scale.
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