Journal ArticleDOI
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin.
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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
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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
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Journal ArticleDOI
On the nature of allosteric transitions: implications of non-exclusive ligand binding.
TL;DR: The non-exclusive binding of one or more of the ligands, such as the substrate, inhibitor or activator of a regulatory enzyme, is expected to introduce limits on the extent to which the equilibrium between the conformational states of an allosteric protein may be shifted in their presence.
Journal ArticleDOI
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
Journal ArticleDOI
Hemoglobin Kansas, a Human Hemoglobin with a Neutral Amino Acid Substitution and an Abnormal Oxygen Equilibrium
Joseph Bonaventura,Austen Riggs +1 more
TL;DR: The structure of an abnormal human hemoglobin with a low affinity for oxygen and little heme-heme interaction has been determined and threonine replaces asparagine in position 102 of the β chain, which is the fourth residue of the G helix.
Journal ArticleDOI
Influence of globin structure on the state of the heme. III. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction
Max F. Perutz,Elizabeth J. Heidner,Jane E. Ladner,John G. Beetlestone,Chien Ho,Edward F. Slade +5 more
Journal ArticleDOI
Extensions of the Allosteric Model for Haemoglobin
TL;DR: Numerical analysis yields a unique value for the allosteric constant showing that only the two state model can account for the behaviour of the protein.