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PMID: 9370470 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Myoglobin and hemoglobin rotational diffusion in the cell.

Biophysical journal ·Vol. 73 ·No. 5 ·1997-11-00 ·Pages 2764-70

Wang D, Kreutzer U, Chung Y, Jue T

Abstract

The detection of the 1H NMR signal of myoglobin (Mb) in tissue opens an opportunity to examine its cellular diffusion property, which is central to its purported role in facilitating oxygen transport. In perfused myocardium the field-dependent transverse relaxation analysis of the deoxy Mb proximal histidyl NdeltaH indicates that the Mb rotational correlation time in the cell is only approximately 1.4 times longer than it is in solution. Such a mobility is consistent with the theory that Mb facilitates oxygen diffusion from the sarcoplasm to the mitochondria. The microviscosities of the erythrocyte and myocyte environment are different. The hemoglobin (Hb) rotational correlation time is 2.2 longer in the cell than in solution. Because both the overlapping Hb and Mb signals are visible in vivo, a relaxation-based NMR strategy has been developed to discriminate between them.

MeSH Terms
Animals Diffusion Erythrocytes/chemistry,metabolism Hemoglobins/analysis,chemistry,metabolism Histidine/chemistry,metabolism Horses Humans Myocardium/chemistry,metabolism Myoglobin/analysis,chemistry,metabolism Nuclear Magnetic Resonance, Biomolecular Oxygen/metabolism Viscosity
Chemicals
Hemoglobins Myoglobin Histidine deoxyhemoglobin Oxygen
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wang D
Biological Chemistry Department, University of California Davis, 95616-8635, USA.
Kreutzer U
Chung Y
Jue T
References (31)
31 references, click to expand
  1. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites.
    J Mol Biol. 1965 Sep;13(2):482-95 PMID: 5867031
  2. Myoglobin content and oxygen diffusion: model analysis of horse and steer muscle.
    Am J Physiol. 1996 Dec;271(6 Pt 1):C2027-36 PMID: 8997205
  3. Segmental flexibility in an antibody molecule.
    J Mol Biol. 1970 Aug;51(3):573-90 PMID: 5492607
  4. The self-diffusion coefficients of myoglobin and hemoglobin in concentrated solutions.
    J Biol Chem. 1972 Feb 10;247(3):895-901 PMID: 5061974
  5. Nuclear magnetic resonance of rotational mobility of mouse hemoglobin labeled with (2-13C)histidine.
    Science. 1975 Apr 18;188(4185):266-8 PMID: 1118727
  6. Magnetic field and temperature induced line broadening in the hyperfine-shifted proton resonances of myoglobin and hemoglobin.
    J Am Chem Soc. 1977 Feb 16;99(4):1245-50 PMID: 833399
  7. Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale.
    J Mol Biol. 1977 Mar 5;110(3):537-68 PMID: 845959
  8. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale.
    J Mol Biol. 1977 Mar 5;110(3):569-84 PMID: 845960
  9. Assignment of proximal histidine proton NMR peaks in myoglobin and hemoglobin.
    Biochem Biophys Res Commun. 1977 Jul 11;77(1):104-10 PMID: 883967
  10. Proton nuclear magnetic resonance and biochemical studies of oxygenation of human adult hemoglobin in deuterium oxide.
    Biochemistry. 1979 Nov 13;18(23):5238-47 PMID: 497180
  11. Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee.
    Biochem Biophys Res Commun. 1980 Oct 16;96(3):1172-7 PMID: 7437062
  12. Proton nuclear magnetic resonance studies of hemoglobins M Boston (alpha 58E7 His leads to Tyr) and M Milwaukee (beta 67E11 Val leads to Glu): spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the alpha and beta chains of normal human adult hemoglobin.
    Biochemistry. 1980 Nov 11;19(23):5196-202 PMID: 6255985
  13. Structure and refinement of oxymyoglobin at 1.6 A resolution.
    J Mol Biol. 1980 Oct 5;142(4):531-54 PMID: 7463482
  14. Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.
    Biophys J. 1981 May;34(2):217-26 PMID: 7236849
  15. Proton nuclear magnetic resonance investigation of hemoglobins.
    Methods Enzymol. 1981;76:275-312 PMID: 7329262
  16. Tracer diffusion coefficients of oxyhemoglobin A and oxyhemoglobin S in blood cells as determined by pulsed field gradient NMR.
    Biophys Chem. 1982 Nov;16(3):241-5 PMID: 7171716
  17. Myoglobin diffusion in bovine heart muscle.
    Science. 1983 Apr 1;220(4592):71-3 PMID: 6828881
  18. NMR study of the exchange rates of allosterically responsive labile protons in the heme pockets of hemoglobin A.
    Biophys J. 1984 Jul;46(1):117-20 PMID: 6331541
  19. Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin.
    Biochim Biophys Acta. 1985 Nov 29;832(2):175-85 PMID: 4063376
  20. Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
    J Mol Biol. 1987 Mar 20;194(2):313-27 PMID: 3612809
  21. Transport of oxygen in muscle.
    Annu Rev Physiol. 1989;51:857-78 PMID: 2653210
  22. 1H-nuclear magnetic resonance deoxymyoglobin signal as indicator of intracellular oxygenation in myocardium.
    Am J Physiol. 1991 Dec;261(6 Pt 2):H2091-7 PMID: 1750555
  23. Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation.
    Proc Natl Acad Sci U S A. 1992 May 15;89(10):4731-3 PMID: 1584810
  24. H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signals.
    Biochim Biophys Acta. 1993 Jan 15;1161(1):33-7 PMID: 8422419
  25. NMR visibility studies of N-delta proton of proximal histidine in deoxyhemoglobin in lysed and intact red cells.
    Magn Reson Med. 1993 Dec;30(6):759-63 PMID: 8139460
  26. Diffusivity of myoglobin in intact skeletal muscle cells.
    Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3829-33 PMID: 8170996
  27. Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
    Biochemistry. 1994 Sep 13;33(36):10934-43 PMID: 8086410
  28. 1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.
    Biophys J. 1995 Feb;68(2):681-93 PMID: 7696519
  29. Critical intracellular O2 in myocardium as determined by 1H nuclear magnetic resonance signal of myoglobin.
    Am J Physiol. 1995 Apr;268(4 Pt 2):H1675-81 PMID: 7733370
  30. Diffusion of myoglobin in skeletal muscle cells--dependence on fibre type, contraction and temperature.
    Pflugers Arch. 1995 Aug;430(4):519-25 PMID: 7491278
  31. Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle.
    Physiol Rev. 1970 Oct;50(4):559-636 PMID: 4922928
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1997-11-00
Pages
2764-70
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1181178
Subset
IM
Grants
NIGMS NIH HHS · GM44916 · United States
NHLBI NIH HHS · HL09274 · United States
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