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
. 1984 Feb;81(4):1263–1267. doi: 10.1073/pnas.81.4.1263

Temperature dependence of the resonance Raman spectra of plastocyanin and azurin between cryogenic and ambient conditions.

W H Woodruff, K A Norton, B I Swanson, H A Fry
PMCID: PMC344809  PMID: 6422471

Abstract

Resonance Raman spectra of spinach plastocyanin and Pseudomonas aeruginosa azurin were studied as a function of temperature between 10 K and 300 K. The spectra are markedly improved both in signal/noise ratio and in resolution at low temperatures. The assignments of the resonance Raman-active vibrations are reinterpreted in view of the number and intensities of peaks observed in the low-temperature spectra. Features appear in the low-temperature spectra of azurin that may be due to copper-bound methionine. The plastocyanin spectra undergo a transition between 220 K and the melting point of water that results in dramatically narrowed peaks at lower temperature and a shift in the carbon-sulfur stretching frequency of the copper-bound cysteine, suggesting a structural change in the active site and an accompanying effect on vibrational dephasing. Considering that the structures and nonvibrational spectroscopies of these two proteins are similar, the substantial differences in the resonance Raman spectra are striking and significant.

Full text

PDF
1263

Selected References

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

  1. Adman E. T., Canters G. W., Hill H. A., Kitchen N. A. The effect of pH and temperature on the structure of the active site of azurin from Pseudomonas aeruginosa. FEBS Lett. 1982 Jul 5;143(2):287–292. doi: 10.1016/0014-5793(82)80118-x. [DOI] [PubMed] [Google Scholar]
  2. Adman E. T., Stenkamp R. E., Sieker L. C., Jensen L. H. A crystallographic model for azurin a 3 A resolution. J Mol Biol. 1978 Jul 25;123(1):35–47. doi: 10.1016/0022-2836(78)90375-3. [DOI] [PubMed] [Google Scholar]
  3. Ferris N. S., Woodruff W. H., Tennent D. L., McMillin D. R. Native azurin and its Ni(II) derivative: a resonance Raman study. Biochem Biophys Res Commun. 1979 May 14;88(1):288–296. doi: 10.1016/0006-291x(79)91728-5. [DOI] [PubMed] [Google Scholar]
  4. Fischer A. J., Marres E. H., Thijssen H. O. A tumour in the cerebellopontine angle region: an unusual case. Clin Neurol Neurosurg. 1978;80(3):189–194. doi: 10.1016/s0303-8467(78)80040-7. [DOI] [PubMed] [Google Scholar]
  5. Hill H. A., Smith B. E. Characteristics of azurin from Pseudomonas aeruginosa via 270-MHz 1H nuclear magnetic resonance spectroscopy. J Inorg Biochem. 1979 Oct;11(2):79–93. doi: 10.1016/s0162-0134(00)80174-9. [DOI] [PubMed] [Google Scholar]
  6. Kincaid J., Stein P., Spiro T. G. Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure. Proc Natl Acad Sci U S A. 1979 Feb;76(2):549–552. doi: 10.1073/pnas.76.2.549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Larrabee J. A., Spiro T. G., Ferris N. S., Woodruff W. H., Maltese W. A., Kerr M. S. Resonance raman study of mollusc and arthropod hemocyanins using ultraviolet excitation: copper environment and subunit inhomogeneity. J Am Chem Soc. 1977 Mar 16;99(6):1979–1980. doi: 10.1021/ja00448a053. [DOI] [PubMed] [Google Scholar]
  8. Malkin R., Malmström B. G. The state and function of copper in biological systems. Adv Enzymol Relat Areas Mol Biol. 1970;33:177–244. doi: 10.1002/9780470122785.ch4. [DOI] [PubMed] [Google Scholar]
  9. Markley J. L., Ulrich E. L., Berg S. P., Krogmann D. W. Nuclear magnetic resonance studies of the copper binding sites of blue copper proteins: oxidized, reduced, and apoplastocyanin. Biochemistry. 1975 Oct 7;14(20):4428–4433. doi: 10.1021/bi00691a014. [DOI] [PubMed] [Google Scholar]
  10. Miskowski V., Tang S. P., Spiro T. G., Shapiro E., Moss T. H. The copper coordination group in "blue" copper proteins: evidence from resonance Raman spectra. Biochemistry. 1975 Mar 25;14(6):1244–1250. doi: 10.1021/bi00677a024. [DOI] [PubMed] [Google Scholar]
  11. Norris G. E., Anderson B. F., Baker E. N. Structure of azurin from Alcaligenes denitrificans at 2.5 A resolution. J Mol Biol. 1983 Apr 15;165(3):501–521. doi: 10.1016/s0022-2836(83)80216-2. [DOI] [PubMed] [Google Scholar]
  12. Peeling J., Haslett B. G., Evans I. M., Clark D. T., Boulter D. Some observations on the ESCA spectra of plastocyanins. J Am Chem Soc. 1977 Feb 16;99(4):1025–1028. doi: 10.1021/ja00446a008. [DOI] [PubMed] [Google Scholar]
  13. Rosen P., Pecht I. Conformational equilibria accompanying the electron transfer between cytochrome c (P551) and azurin from Pseudomonas aeruginosa. Biochemistry. 1976 Feb 24;15(4):775–786. doi: 10.1021/bi00649a008. [DOI] [PubMed] [Google Scholar]
  14. Shaklai N., Sharma V. S., Ranney H. M. Interaction of sickle cell hemoglobin with erythrocyte membranes. Proc Natl Acad Sci U S A. 1981 Jan;78(1):65–68. doi: 10.1073/pnas.78.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Siiman O., Young N. M., Carey P. R. Resonance Raman studies of "blue" copper proteins. J Am Chem Soc. 1974 Aug 21;96(17):5583–5585. doi: 10.1021/ja00824a053. [DOI] [PubMed] [Google Scholar]
  16. Siiman O., Young N. M., Carey P. R. Resonance raman spectra of "blue" copper proteins and the nature of their copper sites. J Am Chem Soc. 1976 Feb 4;98(3):744–748. doi: 10.1021/ja00419a017. [DOI] [PubMed] [Google Scholar]
  17. Solomon E. I., Clendening P. J., Gray H. B., Grunthaner F. J. Letter: Direct observation of sulfur coordination in bean plastocyanin by X-ray photoelectron spectroscopy. J Am Chem Soc. 1975 Jun 25;97(13):3878–3879. doi: 10.1021/ja00846a087. [DOI] [PubMed] [Google Scholar]
  18. Solomon E. I., Hare J. W., Gray H. B. Spectroscopic studies and a structural model for blue copper centers in proteins. Proc Natl Acad Sci U S A. 1976 May;73(5):1389–1393. doi: 10.1073/pnas.73.5.1389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Teraoka J., Kitagawa T. Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line. J Biol Chem. 1981 Apr 25;256(8):3969–3977. [PubMed] [Google Scholar]
  20. Thamann T. J., Frank P., Willis L. J., Loehr T. M. Normal coordinate analysis of the copper center of azurin and the assignment of its resonance Raman spectrum. Proc Natl Acad Sci U S A. 1982 Oct;79(20):6396–6400. doi: 10.1073/pnas.79.20.6396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tullius T. D., Frank P., Hodgson K. O. Characterization of the blue copper site in oxidized azurin by extended x-ray absorption fine structure: Determination of a short Cu-S distance. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4069–4073. doi: 10.1073/pnas.75.9.4069. [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