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Science 14 June 1985:
Vol. 228. no. 4705, pp. 1273 - 1280
DOI: 10.1126/science.4001941
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Articles

Science, Vol 228, Issue 4705, 1273-1280
Copyright © 1985 by American Association for the Advancement of Science

articles

Structure, dynamics, and reactivity in hemoglobin

JM Friedman

The static structure of hemoglobin and its functional properties are very well characterized. It is still not known how energy is stored and used within the structure of the protein to promote function and functional diversity. An essential part of this question is understanding the mechanism through which the overall protein structure (quaternary structure) couples to the local environment about the oxygen binding sites. Time-resolved resonance Raman spectroscopy has been used to probe the vibrational degrees of the freedom of the binding site as a function of protein structure. Comparison of the spectra from both equilibrium and transient forms of deoxy hemoglobin from a variety of mammalian, reptilian, and fish hemoglobins reveals that for each quaternary structure there exist two tertiary states stabilized by the presence or absence of an iron-bound ligand. Pulse-probe Raman experiments show that for photodissociated, ligated hemoglobins the local tertiary structure relaxes at a solution-dependent rate extending from tens of nanoseconds to microseconds. In this local environment, the linkage between the iron and the proximal histidine proves to be the single observed structural feature that responds in a systematic and substantial manner to structural changes in the protein. The additional finding of a correlation between the frequency of the iron-proximal histidine stretching motion (nu Fe-His) and various parameters of ligand reactivity, including geminate recombination, implicates the associated localized structural element in the mechanism of protein control of ligand binding. On the basis of these and related finds, a model is presented to account for both coarse and fine control of ligand binding by the protein structure.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Kinetic Modulation in Carbonmonoxy Derivatives of Truncated Hemoglobins: THE ROLE OF DISTAL HEME POCKET RESIDUES AND EXTENDED APOLAR TUNNEL.
U. Samuni, D. Dantsker, A. Ray, J. B. Wittenberg, B. A. Wittenberg, S. Dewilde, L. Moens, Y. Ouellet, M. Guertin, and J. M. Friedman (2003)
J. Biol. Chem. 278, 27241-27250
   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 »
Altered Ligand Rebinding Kinetics Due to Distal-side Effects in Hemoglobin Chico (Lysbeta 66(E10) right-arrow Thr).
C. Bonaventura, J. Bonaventura, D. T.-b. Shih, E. T. Iben, and J. Friedman (1999)
J. Biol. Chem. 274, 8686-8693
   Abstract »    Full Text »    PDF »
Probing the Hemoglobin Central Cavity by Direct Quantification of Effector Binding Using Fluorescence Lifetime Methods.
D. S. Gottfried, L. J. Juszczak, N. A. Fataliev, A. S. Acharya, R. E. Hirsch, and J. M. Friedman (1997)
J. Biol. Chem. 272, 1571-1578
   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 »
The energy landscapes and motions of proteins.
H Frauenfelder, S. Sligar, and P. Wolynes (1991)
Science 254, 1598-1603
   Abstract »    PDF »
Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin.
B. Campbell, M. Chance, and J. Friedman (1987)
Science 238, 373-376
   Abstract »    PDF »


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