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Internal water and microsecond dynamics in myoglobin.

Shuji Kaieda1, Bertil Halle

  • 1Department of Biophysical Chemistry, Lund University , P.O. Box 124, SE-22100 Lund, Sweden.

The Journal of Physical Chemistry. B
|November 8, 2013
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Summary
This summary is machine-generated.

Internal water molecules in myoglobin (Mb) are characterized using magnetic relaxation dispersion. We found ordered water molecules with a mean survival time of 5.6 μs, suggesting a global exchange mechanism potentially aiding ligand release.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Myoglobin (Mb) binds diatomic ligands within a transiently accessible cavity.
  • Ligand migration pathways and internal hydration sites in Mb are debated.
  • Understanding internal water dynamics is crucial for Mb's function.

Purpose of the Study:

  • To characterize internal water molecules in myoglobin under physiological conditions.
  • To investigate the dynamics and locations of internal water in equine carbonmonoxy Mb.
  • To elucidate the mechanism of water exchange and its potential role in ligand release.

Main Methods:

  • Water (2)H and (17)O magnetic relaxation dispersion (MRD) spectroscopy.
  • Characterization of internal water molecules in equine carbonmonoxy Mb.
  • Analysis of water survival times and exchange mechanisms.

Main Results:

  • Equine carbonmonoxy Mb contains 4.5 ± 1.0 ordered internal water molecules.
  • Mean survival time of internal water molecules is 5.6 ± 0.5 μs at 25 °C.
  • Evidence for a global water exchange mechanism involving H-bonded water chains and intramolecular hydrogen exchange in histidine residues.

Conclusions:

  • Internal water molecules in Mb exchange on a microsecond timescale, suggesting a global mechanism.
  • This water exchange mechanism may facilitate the elimination of trapped diatomic ligands.
  • Myoglobin's internal water dynamics are linked to its ligand-binding and release functions.