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Science 4 June 1976:
Vol. 192. no. 4243, pp. 1002 - 1004
DOI: 10.1126/science.1273579
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Articles

Science, Vol 192, Issue 4243, 1002-1004
Copyright © 1976 by American Association for the Advancement of Science

articles

Tunneling in ligand binding to heme proteins

N Alberding, RH Austin, KW Beeson, SS Chan, L Eisenstein, H Frauenfelder, and TM Nordlund

Rebinding of carbon monoxide to the beta chain of hemoglobin after photodissociation by a laser flash is intramolecular below about 200 K. Above 25 K, rebinding occurs via classical over-the-barrier motion; below, quantum-mechanical tunneling dominates. Both are described by an energy spectrum peaked at Epeak=4.0 kilojoules per mole. The barrier width d(E), determined from the energy dependence of the tunneling rate, depends on barrier height, d(E) approximately 0.05 nanometer X (E/Epeak) 1.5.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Thr-E11 Regulates O2 Affinity in Cerebratulus lacteus Mini-hemoglobin.
A. Pesce, M. Nardini, P. Ascenzi, E. Geuens, S. Dewilde, L. Moens, M. Bolognesi, A. F. Riggs, A. Hale, P. Deng, et al. (2004)
J. Biol. Chem. 279, 33662-33672
   Abstract »    Full Text »    PDF »
Ligand binding and protein dynamics in neuroglobin.
J. M. Kriegl, A. J. Bhattacharyya, K. Nienhaus, P. Deng, O. Minkow, and G. U. Nienhaus (2002)
PNAS 99, 7992-7997
   Abstract »    Full Text »    PDF »


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