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
Citations
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Journal ArticleDOI
Structure of cyanide methemoglobin.
TL;DR: This and other studies suggest that the structural changes responsible for co-operativity in hemoglobin may be initiated not merely by an alteration in the covalent porphyrin-proximal histidine linkage, but by changes in the noncovalent interactions of the globin with the ligand and porphyrsin as well.
Journal ArticleDOI
A structural model for the kinetic behavior of hemoglobin.
TL;DR: The tertiary structures of all liganded hemoglobins in the R state differ in detail, and structural interpretation of this kinetic behavior indicates that the relative contributions of nonbonded ligand-globin interactions and nonbonding heme interactions to transition state free energies differ for linear and bent ligands.
Journal ArticleDOI
Sulfhemoglobinemia. Clinical and molecular aspects.
TL;DR: A propos d'une observation: femme de 33 ans prenant depuis 8 ans des doses elevees de produits multiples (amphetamine, barbiturique, propoxyphene, phenacetine, cafeine, Alkaseltzer), Diagnostic provisoire de methanoglobinemie.
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Conformation and spin state in methemoglobin.
TL;DR: The properties of human methemoglobin have been investigated under a wide variety of conditions to determine its conformation and to test for evidence of the T state conformation which has been proposed by Perutz to exist in the presence of high spin ligands and inositol hexaphosphate (IHP).
References
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Journal ArticleDOI
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin.
TL;DR: DPG has a two-fold effect on human deoxyhaemoglobin: it both stabilizes and slightly distorts the S form, and may therefore affect the solubility.
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Stereochemistry of cooperative effects in hemoglobin.
M. F. Perutz,L. F. TenEyck +1 more
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Rates and Mechanisms of Substitution in Inorganic Complexes in Solution.
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Nature of Haem–Haem Interaction
TL;DR: Dr Perutz describes how spin changes that accompany reaction with ligands alter the oxygen affinity of the haems.
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The interaction of 2,3-diphosphoglycerate with various human hemoglobins
TL;DR: Results suggest that the N-terminal amino groups of the non-α-chains are involved in the binding of 2,3-DPG to hemoglobin.