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
PH dependence of the shape of the hemoglobin-oxygen equilibrium curve.
TL;DR: The maximum slope of the Hill plot significantly decreases with increasing pH, and the magnitude of the shift of the equilibrium curve due to pH change depends upon the oxygen saturation, markedly decreasing when the latter is above 80%.
Journal ArticleDOI
Studies on the oxidation-reduction potentials of heme proteins. v. the oxidation bohr effect in normal human hemoglobin and human hemoglobin digested with carboxypeptidase a.
Journal ArticleDOI
Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism.
TL;DR: Comparison of UV circular-dichroism spectra of human and horse hemoglobins and corresponding proteins modified with a reagent known to eliminate the conformational rearrangement normally associated with cooperativity indicates that one region is sensitive chiefly to the state of the hemes; changes in another region may be correlated with the conformations linked to cooperative interactions.
Journal ArticleDOI
Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
TL;DR: Several N-substituted maleimides have been reacted with horse oxy- and deoxyhemoglobin and the physical and functional properties of the resulting derivatives have been determined.
Journal ArticleDOI
Structure and functional properties of chemically modified horse hemoglobin: III. Functional consequences of structural alterations and their implications for the molecular basis of co-operativity☆
TL;DR: A stereochemical model is proposed for the reaction between the various N-substituted maleimides and the -SH group of Cys F9(93)β in oxy- and deoxyhemoglobin, suggesting that the existence of a hydrogen bond between its phenolic hydroxyl and the main-chain carbonyl of Val FG5(98)β is essential for the expression of co-operativity.