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Science 17 December 1982:
Vol. 218. no. 4578, pp. 1244 - 1246
DOI: 10.1126/science.7146910
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Articles

Science, Vol 218, Issue 4578, 1244-1246
Copyright © 1982 by American Association for the Advancement of Science

articles

Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage

JM Friedman, DL Rousseau, MR Ondrias, and RA Stepnoski

Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T- state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates.
V Jayaraman, K. Rodgers, I Mukerji, and T. Spiro (1995)
Science 269, 1843-1848
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Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin.
B. Campbell, M. Chance, and J. Friedman (1987)
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Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity.
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Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination.
J. Friedman, T. Scott, G. Fisanick, Simon SR, E. Findsen, M. Ondrias, and V. Macdonald (1985)
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Structure, dynamics, and reactivity in hemoglobin.
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Metastable species of hemoglobin: room temperature transients and cryogenically trapped intermediates.
M. Ondrias, J. Friedman, and D. Rousseau (1983)
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