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Journal ArticleDOI

Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin.

Max F. Perutz, +3 more
- 07 May 1974 - 
- Vol. 13, Iss: 10, pp 2174-2186
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.

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Citations
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Journal ArticleDOI

Ultraviolet circular dichroism of nitrosyl hemoglobin

TL;DR: This work has shown that for hemoglobins which crystalize in a structure isomorphous with oxyhemoglobin this neg- ative CD peak is not produced even in the absence of heme ligand, and indicates the R to T transition in hemoglobin independent of the degree of ligation.
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Circular dichroism spectroscopy of tertiary and quaternary conformations of human hemoglobin entrapped in wet silica gels

TL;DR: The results support the view that ligation and allosteric effectors can modulate the structural and functional properties of hemoglobin by regulating the equilibrium between the same tertiary species within both quaternary states.
Journal ArticleDOI

Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin.

TL;DR: Oxygen binding results, obtained from a combination of direct and indirect methods, demonstrate the same combinatorial aspect to cooperativity that is predicted by the symmetry rule.
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Ferrihaemoglobin formation by amyl nitrite and sodium nitrite in different species in vivo and in vitro.

TL;DR: Inhalation of AN by human volunteers in a gas mask and from ampoules crushed close to the nose did not induce haemoglobin oxidation to a practically significant extent, but it was associated with headache, tiredness, dizziness, and a fall in blood pressure.
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Temperature induced difference spectra of oxy and deoxy hemoglobin in the near IR, visible and Soret regions.

TL;DR: Human Oxy- and Deoxy-Hb spectra and difference spectra are quantitatively analyzed for the first time in terms of individual Gaussian or skewed-Gaussian components, by precise computer analysis.
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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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.
Journal ArticleDOI

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.
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