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 12 July 1985:
Vol. 229. no. 4709, pp. 187 - 190
DOI: 10.1126/science.4012316
Prev | Table of Contents | Next

Articles

Science, Vol 229, Issue 4709, 187-190
Copyright © 1985 by American Association for the Advancement of Science

articles

Localized control of ligand binding in hemoglobin: effect of tertiary structure on picosecond geminate recombination

JM Friedman, TW Scott, GJ Fisanick, Simon SR, EW Findsen, MR Ondrias, and VW Macdonald

The picosecond geminate rebinding of molecular oxygen was monitored in a variety of different human, reptilian, and fish hemoglobins. The fast (100 to 200 picoseconds) component of the rebinding is highly sensitive to protein structure. Both proximal and distal perturbations of the heme affect this rebinding process. The rebinding yield for the fast process correlates with the frequency of the stretching motion of the iron-proximal histidine mode (VFe-His) observed in the transient Raman spectra of photodissociated ligated hemoglobins. The high-affinity R-state species exhibit the highest values for VFe-His and the highest yields for fast rebinding, whereas low affinity R-state species and T-state species exhibit lower values of VFe-His and correspondingly reduced yields for this geminate process. These findings link protein control of ligand binding with events at the heme.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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 »
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 »
Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales.
L Genberg, L Richard, G McLendon, and R. Miller (1991)
Science 251, 1051-1054
   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 »


To Advertise     Find Products

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