Journal ArticleDOI
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin.
About:
This article is published in Biochemistry.The article was published on 1974-05-07. It has received 275 citations till now. The article focuses on the topics: Methemoglobin & Globin.read more
Citations
More filters
Book ChapterDOI
[4] Circular dichroism
TL;DR: Circular dichroism is a spectroscopic method which depends on the fact that certain molecules interact differently with right and left circularly polarized light and can provide information about the secondary structure of proteins and nucleic acids and about the binding of ligands to these types of macromolecule.
Journal ArticleDOI
Structure of human oxyhaemoglobin at 2.1 A resolution.
TL;DR: The overall quaternary structure of oxyhaemoglobin is identical, within experimental error, to that of carbon monoxide haemoglobin, and thus confirms the applicability of the allosteric mechanisms proposed by Perutz and Baldwin & Chothia to the process of oxygen binding.
Journal ArticleDOI
Molecular code for cooperativity in hemoglobin
TL;DR: This work has revealed that the allosteric mechanism is controlled by a previously unrecognized symmetry feature: quaternary switching from form T to form R occurs whenever heme-site binding creates a tetramer with at least one ligated subunit on each dimeric half-molecule.
Journal ArticleDOI
The interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane.
Joseph A. Walder,R. Chatterjee,Theodore L. Steck,Philip S. Low,G. F. Musso,E. T. Kaiser,P. H. Rogers,Arthur Arnone +7 more
TL;DR: The interaction of hemoglobin with the synthetic peptide AcM-E-E, corresponding to the first 11 residues of band 3, and with the entire 43,000-Da cytoplasmic domain of the protein is reported, indicating that the peptide binds preferentially to deoxyhemoglobin.
Journal ArticleDOI
Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
TL;DR: Thioltransferase (glutaredoxin) appears to be specific for glutathione-containing mixed disulfides, and in separate experiments, TTase from rat liver displayed analogous selectivity.
References
More filters
Journal ArticleDOI
The kinetics of ligand binding and of the association-dissociation reactions of human hemoglobin. Properties of deoxyhemoglobin dimers.
TL;DR: In this paper, the tetramer-dimer dissociation constant of both HbCO and deoxy-Hb increases dramatically above pH 10.0 and the value of K4,2 for Hb CO is significantly greater than the value for deoxyHb in the pH range of 7 to 11.0.
Journal ArticleDOI
The interaction of inositol hexaphosphate with methaemoglobin
TL;DR: Results support the idea that inositol hexaphosphate causes methaemoglobin to take up the deoxyhaemobic quaternary structure at pH6.5, and also cause a decrease in the alkaline oxidation Bohr effect at these same pH values.
Journal ArticleDOI
Determination of the reactive sulfhydryl groups in heme proteins with 4,4′-dipyridinedisulfide
Journal ArticleDOI
Cofactor Binding and Oxygen Equilibria in Haemoglobin
TL;DR: The observations that deoxyhaemoglobin has a single strong binding site for the cofactor, which in consequence stabilizes it in relation to the oxygenated state can be explained qualitatively by observations that the binding site is associated with the β chains.
Journal ArticleDOI
Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation.
TL;DR: Electron density maps show the α haems to undergo autoxidation more readily than theβ haems, just as the β haems were reduced more easily than theα haems in BME-haemoglobin.