Elongation of the Fe–His Bond in the α Subunit Induced by Binding of the Allosteric Effector Bezafibrate to Hemoglobins
Author:
Affiliation:
1. Department of Chemistry, University of Tsukuba, Tsukuba, Ibaraki 305-8571, Japan
2. Department of Obstetrics and Gynecology, Institute of Clinical Medicine, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp205010m
Reference51 articles.
1. On the nature of allosteric transitions: A plausible model
2. X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
3. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin
4. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
5. Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron
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1. Heterogeneity between Two α Subunits of α2β2 Human Hemoglobin and O2 Binding Properties: Raman, 1H Nuclear Magnetic Resonance, and Terahertz Spectra;Biochemistry;2017-11-07
2. Advances in NMR Methods To Map Allosteric Sites: From Models to Translation;Chemical Reviews;2016-04-25
3. An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer;PLOS ONE;2015-08-05
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