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Science 7 August 1981:
Vol. 213. no. 4508, pp. 657 - 659
DOI: 10.1126/science.7256263
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Articles

Science, Vol 213, Issue 4508, 657-659
Copyright © 1981 by American Association for the Advancement of Science

articles

Structural changes at the heme induced by freezing hemoglobin

MR Ondrias, DL Rousseau, and Simon SR

A dramatic change occurs in the vibrational properties of the iron-histidine bond, trans to the oxygen binding site, on freezing deoxyhemoglobin. The large, quaternary structure-dependent differences in the shape and frequency of the iron-histidine mode observed in resonance Raman scattering measurements above freezing ae significantly diminished by the freezing event and the scattering intensity increases substantially. On further reduction in temperature to 10 K this broad line becomes narrow and shifts to a higher frequency. These data implicate dynamical processes and protein interaction with water as contributors to the quaternary structure dependence of the iron-histidine bond and thus reflect on the role of that bond in the energetics of cooperative ligand binding.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Metastable species of hemoglobin: room temperature transients and cryogenically trapped intermediates.
M. Ondrias, J. Friedman, and D. Rousseau (1983)
Science 220, 615-617
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