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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
. 1978 Nov;75(11):5255–5259. doi: 10.1073/pnas.75.11.5255

Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation.

B I Greene, R M Hochstrasser, R B Weisman, W A Eaton
PMCID: PMC392939  PMID: 281677

Abstract

The photolysis of HbO2 and HbCO has been investigated with picosecond laser techniques. Transient absorption spectra were measured in the Soret and visible regions after excitation with 353- or 530-nm pulses. The photoproducts appeared within 8 psec and exhibited considerably broadened deoxyhemoglobin-like spectra, which persisted to 680 psec. The altered spectra are attributed to the production of deoxyheme conformational and spin states that might result from the intense excitation.

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Selected References

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  1. Alberding N., Chan S. S., Eisenstein L., Frauenfelder H., Good D., Gunsalus I. C., Nordlund T. M., Perutz M. F., Reynolds A. H., Sorensen L. B. Binding of carbon monoxide to isolated hemoglobin chains. Biochemistry. 1978 Jan 10;17(1):43–51. doi: 10.1021/bi00594a007. [DOI] [PubMed] [Google Scholar]
  2. Alpert B., Banerjee R., Lindqvist L. Rapid structural changes in human hemoglobin studied by laser photolysis. Biochem Biophys Res Commun. 1972 Jan 31;46(2):913–918. doi: 10.1016/s0006-291x(72)80228-6. [DOI] [PubMed] [Google Scholar]
  3. Alpert B., Banerjee R., Lindqvist L. The kinetics of conformational changes in hemoglobin, studied by laser photolysis. Proc Natl Acad Sci U S A. 1974 Feb;71(2):558–562. doi: 10.1073/pnas.71.2.558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Antonini E., Anderson N. M., Brunori M. Properties of the product of partial photodissociation of carbon monoxide hemoglobin. J Biol Chem. 1972 Jan 10;247(1):319–321. [PubMed] [Google Scholar]
  5. 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]
  6. Edelstein S. J. Cooperative interactions of hemoglobin. Annu Rev Biochem. 1975;44:209–232. doi: 10.1146/annurev.bi.44.070175.001233. [DOI] [PubMed] [Google Scholar]
  7. Ferrone F. A., Hopfield J. J. Rate of quaternary structure change in hemoglobin measured by modulated excitation. Proc Natl Acad Sci U S A. 1976 Dec;73(12):4497–4501. doi: 10.1073/pnas.73.12.4497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. GIBSON Q. H. The photochemical formation of a quickly reacting form of haemoglobin. Biochem J. 1959 Feb;71(2):293–303. doi: 10.1042/bj0710293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gelin B. R., Karplus M. Mechanism of tertiary structural change in hemoglobin. Proc Natl Acad Sci U S A. 1977 Mar;74(3):801–805. doi: 10.1073/pnas.74.3.801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gibson Q. H., Antonini E. Observations on rapidly reacting hemoglobin. J Biol Chem. 1967 Oct 25;242(20):4678–4681. [PubMed] [Google Scholar]
  11. Hoffman B. M., Gibson Q. H. On the photosensitivity of liganded hemoproteins and their metal-substituted analogues. Proc Natl Acad Sci U S A. 1978 Jan;75(1):21–25. doi: 10.1073/pnas.75.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Iizuka T., Yamamoto H., Kotani M., Yonetani T. Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin. Biochim Biophys Acta. 1974 Nov 5;371(1):126–139. doi: 10.1016/0005-2795(74)90161-5. [DOI] [PubMed] [Google Scholar]
  13. McCray J. A. Oxygen recombination kinetics following laser photolysis of oxyhemoglobin. Biochem Biophys Res Commun. 1972 Apr 14;47(1):187–193. doi: 10.1016/s0006-291x(72)80027-5. [DOI] [PubMed] [Google Scholar]
  14. Noble R. W., Brunori M., Wyman J., Antonini E. Studies on the quantum yields of the photodissociation of carbon monoxide from hemoglobin and myoglobin. Biochemistry. 1967 Apr;6(4):1216–1222. doi: 10.1021/bi00856a035. [DOI] [PubMed] [Google Scholar]
  15. Noe L. J., Eisert W. G., Rentzepis P. M. Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin. Proc Natl Acad Sci U S A. 1978 Feb;75(2):573–577. doi: 10.1073/pnas.75.2.573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature. 1970 Nov 21;228(5273):726–739. doi: 10.1038/228726a0. [DOI] [PubMed] [Google Scholar]
  17. Saffran W. A., Gibson Q. H. Photodissociation of ligands from heme and heme proteins. Effect of temperature and organic phosphate. J Biol Chem. 1977 Nov 25;252(22):7955–7958. [PubMed] [Google Scholar]
  18. Sawicki C. A., Gibson Q. H. Properties of the T state of human oxyhemoglobin studies by laser photolysis. J Biol Chem. 1977 Nov 10;252(21):7538–7547. [PubMed] [Google Scholar]
  19. Sawicki C. A., Gibson Q. H. Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. J Biol Chem. 1976 Mar 25;251(6):1533–1542. [PubMed] [Google Scholar]
  20. Shank C. V., Ippen E. P., Bersohn R. Time-resolved spectroscopy of hemoglobin and its complexes with subpicosecond optical pulses. Science. 1976 Jul 2;193(4247):50–51. doi: 10.1126/science.935853. [DOI] [PubMed] [Google Scholar]
  21. Shulman R. G., Hopfield J. J., Ogawa S. Allosteric interpretation of haemoglobin properties. Q Rev Biophys. 1975 Jul;8(3):325–420. doi: 10.1017/s0033583500001840. [DOI] [PubMed] [Google Scholar]
  22. Szabo A., Karplus M. A mathematical model for structure-function relations in hemoglobin. J Mol Biol. 1972 Dec 14;72(1):163–197. doi: 10.1016/0022-2836(72)90077-0. [DOI] [PubMed] [Google Scholar]

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