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Science 16 September 1994:
Vol. 265. no. 5179, pp. 1697 - 1699
DOI: 10.1126/science.8085153
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Articles

Science, Vol 265, Issue 5179, 1697-1699
Copyright © 1994 by American Association for the Advancement of Science

articles

Nanosecond dynamics of the R-->T transition in hemoglobin: ultraviolet Raman studies

KR Rodgers and TG Spiro

Department of Chemistry, North Dakota State University, Fargo 58105.

Pulse-probe transient Raman spectroscopy, with probe excitation at 230 nanometers, reveals changes in signals arising from tyrosine and tryptophan residues of the hemoglobin molecule as it moves from the relaxed (R) to the tense (T) state after photodeligation. Signals associated with intersubunit contacts in the T state develop in about 10 microseconds but are preceded by quite different signals, which reach maximum amplitude in about 50 nanoseconds. These signals involve the interior tryptophan residues that bridge the A and E helices by means of H bonds between the indole rings and serine or threonine side chains. Alterations of the H bond strengths, as a result of interhelix motions, can account for the signals. A model is proposed here in which loss of the ligand from the heme binding pocket is concerted with inward motion of the adjacent E helix; this motion, along with a complementary motion of the proximal F helix, transmits the energy associated with heme deligation to the subunit interfaces, leading to the T state rearrangement.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Conformational Changes in Hemoglobin S (beta E6V) Imposed by Mutation of the beta Glu7-beta Lys132 Salt Bridge and Detected by UV Resonance Raman Spectroscopy.
L. J. Juszczak, C. Fablet, V. Baudin-Creuza, S. Lesecq-Le Gall, R. E. Hirsch, R. L. Nagel, J. M. Friedman, and J. Pagnier (2003)
J. Biol. Chem. 278, 7257-7263
   Abstract »    Full Text »    PDF »
The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.
A. Riccio, L. Vitagliano, G. di Prisco, A. Zagari, and L. Mazzarella (2002)
PNAS 99, 9801-9806
   Abstract »    Full Text »    PDF »
UV Resonance Raman Spectra of Ligand Binding Intermediates of Sol-Gel Encapsulated Hemoglobin.
L. J. Juszczak and J. M. Friedman (1999)
J. Biol. Chem. 274, 30357-30360
   Abstract »    Full Text »    PDF »
Solution-active Structural Alterations in Liganded Hemoglobins C (beta 6 Glu right-arrow Lys) and S (beta 6 Glu right-arrow Val).
R. E. Hirsch, L. J. Juszczak, N. A. Fataliev, J. M. Friedman, and R. L. Nagel (1999)
J. Biol. Chem. 274, 13777-13782
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A Steric Mechanism for Inhibition of CO Binding to Heme Proteins.
G. S. Kachalova, A. N. Popov, and H. D. Bartunik (1999)
Science 284, 473-476
   Abstract »    Full Text »
Conformational Changes in Oxyhemoglobin C (Glu[IMAGE] [IMAGE] Lys) Detected by Spectroscopic Probing.
R. E. Hirsch, M. J. Lin, G. V. A. Vidugirus, S. Huang, J. M. Friedman, and R. L. Nagel (1996)
J. Biol. Chem. 271, 372-375
   Abstract »    Full Text »    PDF »
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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