Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 29 September 1995:
Vol. 269. no. 5232, pp. 1843 - 1848
DOI: 10.1126/science.7569921
Prev | Table of Contents | Next

Articles

Science, Vol 269, Issue 5232, 1843-1848
Copyright © 1995 by American Association for the Advancement of Science

articles

Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates

V Jayaraman, KR Rodgers, I Mukerji, and TG Spiro

Department of Chemistry, Princeton University, NJ 08544, USA.

The end states, R and T, of the allosteric transition in hemoglobin (Hb) are structurally well characterized, but there is little information on intermediate structures along the allosteric pathway. These intermediates were examined by means of time-resolved resonance Raman spectroscopy in the nanosecond-to-microsecond interval after HbCO photolysis. Complementary spectra of the heme group and of the tyrosine and tryptophan residues were recorded during laser excitation at 436 and 230 nanometers. These spectra reveal a sequence of interleaved tertiary and quaternary motions during the photocycle, motions involving the proximal and distal helices, and the alpha 1 beta 2 subunit interface. This sequence leads to a modified form of the T state, in which the alpha 1 beta 2 interface is deformed as a result of two carbon monoxide molecules binding to the same dimer within the tetramer.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.
A. Sato, Y. Gao, T. Kitagawa, and Y. Mizutani (2007)
PNAS 104, 9627-9632
   Abstract »    Full Text »    PDF »
Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy.
S. G. Kruglik, A. Jasaitis, K. Hola, T. Yamashita, U. Liebl, J.-L. Martin, and M. H. Vos (2007)
PNAS 104, 7408-7413
   Abstract »    Full Text »    PDF »
Allosteric action in real time: Time-resolved crystallographic studies of a cooperative dimeric hemoglobin.
J. E. Knapp, R. Pahl, V. Srajer, and W. E. Royer Jr. (2006)
PNAS 103, 7649-7654
   Abstract »    Full Text »    PDF »
Direct observation of photolysis-induced tertiary structural changes in hemoglobin.
S.-i. Adachi, S.-Y. Park, J. R. H. Tame, Y. Shiro, and N. Shibayama (2003)
PNAS 100, 7039-7044
   Abstract »    Full Text »    PDF »
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 »
Spectroscopically and Kinetically Distinct Conformational Populations of Sol-Gel-encapsulated Carbonmonoxy Myoglobin. A COMPARISON WITH HEMOGLOBIN.
U. Samuni, D. Dantsker, I. Khan, A. J. Friedman, E. Peterson, and J. M. Friedman (2002)
J. Biol. Chem. 277, 25783-25790
   Abstract »    Full Text »    PDF »
Intersubunit circular permutation of human hemoglobin.
K. E. Sanders, J. Lo, and S. G. Sligar (2002)
Blood 100, 299-305
   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
   Abstract »    Full Text »    PDF »
Coupling of the Oxygen-linked Interaction Energy for Inositol Hexakisphosphate and Bezafibrate Binding to Human HbA0.
M. Coletta, M. Angeletti, P. Ascenzi, A. Bertollini, S. Della Longa, G. De Sanctis, A. M. Priori, R. Santucci, and G. Amiconi (1999)
J. Biol. Chem. 274, 6865-6874
   Abstract »    Full Text »    PDF »
Hb Montefiore (alpha 126(H9)Asp right-arrow Tyr). HIGH OXYGEN AFFINITY AND LOSS OF COOPERATIVITY SECONDARY TO C-TERMINAL DISRUPTION.
H. Wajcman, J. Kister, F. Galacteros, A. Spielvogel, M. J. Lin, G. J.A. Vidugiris, R. E. Hirsch, J. M. Friedman, and R. L. Nagel (1996)
J. Biol. Chem. 271, 22990-22998
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)