Publication Date:
1981-08-07
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Rousseau, D L -- Simon, S R -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):657-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256263" target="_blank"〉PubMed〈/a〉
Keywords:
Allosteric Regulation
;
*Freezing
;
*Heme
;
*Hemoglobin A
;
Histidine
;
Humans
;
Motion
;
Protein Conformation
;
Spectrum Analysis, Raman
;
Water
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
