Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Jan;87(1):1–5. doi: 10.1073/pnas.87.1.1

Temperature-derivative spectroscopy: a tool for protein dynamics.

J Berendzen 1, D Braunstein 1
PMCID: PMC53187  PMID: 2296572

Abstract

A relaxation method that measures the derivative of a population with respect to temperature is introduced and used to study the recombination of CO to sperm whale myoglobin after a photolyzing flash. Measurement of the geminate process in the infrared CO-stretch bands shows distributed activation enthalpies with different distributions for each band, transitions between two bands that correspond to photolyzed ligands, and kinetic hole burning. The data are well described by gaussian enthalpy distributions; the results match and complement those of isothermal methods. The temperature-derivative technique is further used to explore the recombination of CO from outside the heme pocket.

Full text

PDF
1

Selected References

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

  1. Agmon N. Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin. Biochemistry. 1988 May 3;27(9):3507–3511. doi: 10.1021/bi00409a057. [DOI] [PubMed] [Google Scholar]
  2. Alben J. O., Beece D., Bowne S. F., Doster W., Eisenstein L., Frauenfelder H., Good D., McDonald J. D., Marden M. C., Moh P. P. Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3744–3748. doi: 10.1073/pnas.79.12.3744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Alben J. O., Moh P. P., Fiamingo F. G., Altschuld R. A. Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex. Proc Natl Acad Sci U S A. 1981 Jan;78(1):234–237. doi: 10.1073/pnas.78.1.234. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Alcala J. R., Gratton E., Prendergast F. G. Fluorescence lifetime distributions in proteins. Biophys J. 1987 Apr;51(4):597–604. doi: 10.1016/S0006-3495(87)83384-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ansari A., Berendzen J., Braunstein D., Cowen B. R., Frauenfelder H., Hong M. K., Iben I. E., Johnson J. B., Ormos P., Sauke T. B. Rebinding and relaxation in the myoglobin pocket. Biophys Chem. 1987 May 9;26(2-3):337–355. doi: 10.1016/0301-4622(87)80034-0. [DOI] [PubMed] [Google Scholar]
  6. Austin R. H., Beeson K. W., Eisenstein L., Frauenfelder H., Gunsalus I. C. Dynamics of ligand binding to myoglobin. Biochemistry. 1975 Dec 2;14(24):5355–5373. doi: 10.1021/bi00695a021. [DOI] [PubMed] [Google Scholar]
  7. Campbell B. F., Chance M. R., Friedman J. M. Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin. Science. 1987 Oct 16;238(4825):373–376. doi: 10.1126/science.3659921. [DOI] [PubMed] [Google Scholar]
  8. Careri G., Fasella P., Gratton E. Enzyme dynamics: the statistical physics approach. Annu Rev Biophys Bioeng. 1979;8:69–97. doi: 10.1146/annurev.bb.08.060179.000441. [DOI] [PubMed] [Google Scholar]
  9. Celaschi S., Mascarenhas S. Thermal-stimulated pressure and current studies of bound water in lysozyme. Biophys J. 1977 Nov;20(2):273–277. doi: 10.1016/S0006-3495(77)85548-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dlott D. D., Frauenfelder H., Langer P., Roder H., DiIorio E. E. Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg]. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6239–6243. doi: 10.1073/pnas.80.20.6239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Doster W., Bowne S. F., Frauenfelder H., Reinisch L., Shyamsunder E. Recombination of carbon monoxide to ferrous horseradish peroxidase types A and C. J Mol Biol. 1987 Mar 20;194(2):299–312. doi: 10.1016/0022-2836(87)90377-9. [DOI] [PubMed] [Google Scholar]
  12. Frauenfelder H., Parak F., Young R. D. Conformational substates in proteins. Annu Rev Biophys Biophys Chem. 1988;17:451–479. doi: 10.1146/annurev.bb.17.060188.002315. [DOI] [PubMed] [Google Scholar]
  13. Iben IE, Braunstein D, Doster W, Frauenfelder H, Hong MK, Johnson JB, Luck S, Ormos P, Schulte A, Steinbach PJ. Glassy behavior of a protein. Phys Rev Lett. 1989 Apr 17;62(16):1916–1919. doi: 10.1103/PhysRevLett.62.1916. [DOI] [PubMed] [Google Scholar]
  14. Ormos P., Braunstein D., Frauenfelder H., Hong M. K., Lin S. L., Sauke T. B., Young R. D. Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8492–8496. doi: 10.1073/pnas.85.22.8492. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Stein D. L. A model of protein conformational substates. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3670–3672. doi: 10.1073/pnas.82.11.3670. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES