Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1988 Mar 15;250(3):853–858. doi: 10.1042/bj2500853

1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin.

H S Aojula 1, M T Wilson 1, G R Moore 1, D J Williamson 1
PMCID: PMC1148933  PMID: 3390144

Abstract

1H-n.m.r. and c.d. studies on sperm-whale myoglobin show that the c.d. signal in the Soret region is inversely and linearly related to the proportion of minor isomer present. An alternative method, 'pH jump', is described for inducing orientational disorder in sperm-whale myoglobin without recourse to reconstitution. 1H-n.m.r. studies on human haemoglobin A indicate little heterogeneity in freshly isolated haemoglobin A, but the effect is enhanced in freeze-dried Sigma haemoglobin A.

Full text

PDF
853

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ahmad M. B., Kincaid J. R. Haem disorder in modified myoglobins. Effect of reconstitution procedures. Biochem J. 1983 Oct 1;215(1):117–122. doi: 10.1042/bj2150117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aojula H. S., Wilson M. T., Drake A. Characterization of haem disorder by circular dichroism. Biochem J. 1986 Jul 15;237(2):613–616. doi: 10.1042/bj2370613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Aojula H. S., Wilson M. T., Morrison I. G. Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins. Biochem J. 1987 Apr 1;243(1):205–210. doi: 10.1042/bj2430205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ascoli F., Fanelli M. R., Antonini E. Preparation and properties of apohemoglobin and reconstituted hemoglobins. Methods Enzymol. 1981;76:72–87. doi: 10.1016/0076-6879(81)76115-9. [DOI] [PubMed] [Google Scholar]
  5. Docherty J. C., Brown S. B. Haem disorder in reconstituted human haemoglobin. Biochem J. 1982 Dec 1;207(3):583–587. doi: 10.1042/bj2070583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Formanek H., Engel J. Optical rotatory dispersion of a respiratory hemeprotein of Chironomus thummi. Biochim Biophys Acta. 1968 Jun 26;160(2):151–158. doi: 10.1016/0005-2795(68)90081-0. [DOI] [PubMed] [Google Scholar]
  7. Gersonde K., Sick H., Overkamp M., Smith K. M., Parish D. W. Bohr effect in monomeric insect haemoglobins controlled by O2 off-rate and modulated by haem-rotational disorder. Eur J Biochem. 1986 Jun 2;157(2):393–404. doi: 10.1111/j.1432-1033.1986.tb09681.x. [DOI] [PubMed] [Google Scholar]
  8. Jue T., La Mar G. N. Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy. Biochem Biophys Res Commun. 1984 Mar 15;119(2):640–645. doi: 10.1016/s0006-291x(84)80297-1. [DOI] [PubMed] [Google Scholar]
  9. La Mar G. N., Budd D. L., Viscio D. B., Smith K. M., Langry K. C. Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5755–5759. doi: 10.1073/pnas.75.12.5755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. La Mar G. N., Davis N. L., Parish D. W., Smith K. M. Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein. J Mol Biol. 1983 Aug 25;168(4):887–896. doi: 10.1016/s0022-2836(83)80080-1. [DOI] [PubMed] [Google Scholar]
  11. La Mar G. N., Smith K. M., Gersonde K., Sick H., Overkamp M. Proton nuclear nagnetic resonance characterization of heme disorder in monomeric insect hemoglobins. J Biol Chem. 1980 Jan 10;255(1):66–70. [PubMed] [Google Scholar]
  12. La Mar G. N., Yamamoto Y., Jue T., Smith K. M., Pandey R. K. 1H NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin. Biochemistry. 1985 Jul 16;24(15):3826–3831. doi: 10.1021/bi00336a002. [DOI] [PubMed] [Google Scholar]
  13. Lecomte J. T., Johnson R. D., La Mar G. N. Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effects. Biochim Biophys Acta. 1985 Jun 10;829(2):268–274. doi: 10.1016/0167-4838(85)90197-9. [DOI] [PubMed] [Google Scholar]
  14. Levy M. J., La Mar G. N., Jue T., Smith K. M., Pandey R. K., Smith W. S., Livingston D. J., Brown W. D. Proton NMR study of yellowfin tuna myoglobin in whole muscle and solution. Evidence for functional metastable protein forms involving heme orientational disorder. J Biol Chem. 1985 Nov 5;260(25):13694–13698. [PubMed] [Google Scholar]
  15. Light W. R., Rohlfs R. J., Palmer G., Olson J. S. Functional effects of heme orientational disorder in sperm whale myoglobin. J Biol Chem. 1987 Jan 5;262(1):46–52. [PubMed] [Google Scholar]
  16. TEALE F. W. Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta. 1959 Oct;35:543–543. doi: 10.1016/0006-3002(59)90407-x. [DOI] [PubMed] [Google Scholar]
  17. Yamamoto Y., La Mar G. N. 1H NMR study of dynamics and thermodynamics of heme rotational disorder in native and reconstituted hemoglobin A. Biochemistry. 1986 Sep 9;25(18):5288–5297. doi: 10.1021/bi00366a045. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES