Internal water and microsecond dynamics in myoglobin.
(2013) In The Journal of Physical Chemistry Part B 117(47). p.14676-14687- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4179738
- author
- Kaieda, Shuji LU and Halle, Bertil LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Part B
- volume
- 117
- issue
- 47
- pages
- 14676 - 14687
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000330160100010
- pmid:24195787
- scopus:84891352533
- pmid:24195787
- ISSN
- 1520-5207
- DOI
- 10.1021/jp409234g
- language
- English
- LU publication?
- yes
- id
- d5e85ab2-359d-4259-a271-5fc0b606982d (old id 4179738)
- date added to LUP
- 2016-04-01 10:37:14
- date last changed
- 2022-02-25 03:28:47
@article{d5e85ab2-359d-4259-a271-5fc0b606982d,
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.}},
author = {{Kaieda, Shuji and Halle, Bertil}},
issn = {{1520-5207}},
language = {{eng}},
number = {{47}},
pages = {{14676--14687}},
publisher = {{The American Chemical Society (ACS)}},
series = {{The Journal of Physical Chemistry Part B}},
title = {{Internal water and microsecond dynamics in myoglobin.}},
url = {{http://dx.doi.org/10.1021/jp409234g}},
doi = {{10.1021/jp409234g}},
volume = {{117}},
year = {{2013}},
}