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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
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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.

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Citations
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Journal ArticleDOI

Kinetic and thermodynamic parameters of the iron spin-state transition in human aquomethemoglobin.

TL;DR: It is demonstrated that a scheme that includes a fast spin transition of the iron atoms, preceding formate binding, adequately accounts for formatebinding to aquomethemoglobin in the T and R quaternary states.
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Solution studies on heme proteins circular dichroism and optical rotation of Glycera dibranchiata hemoglobins

TL;DR: The removal of the heme moiety from the monomer hemoglobin did result in a major decrease in its helix content similar to the loss of heme from myoglobin.
Journal ArticleDOI

The structure of hemoglobin Creteil (beta 89 Ser replaced by Asn) is similar to that of abnormal human hemoglobins having sequence changes at Tyr 145 beta.

TL;DR: Direct comparison of the difference electron density map of deoxyhemoglobin Creteil with that of de oxygenhemoglobin Nancy suggests that these two abnormal hemoglobins may have the same mechanism of dysfunction despite the very different nature of their respective sequence changes.
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Spectral evidence for two forms of acid ferrihemoglobin.

TL;DR: A quantitative analysis of the spectral changes suggests that the effect of glycerol on ferrihemoglobin can in large part be ascribed to its effect on the activity of the solvent water.
Journal ArticleDOI

Transition of hemoglobin between two tertiary conformations : The transition constant differs significantly for the major and minor hemoglobins of the Japanese quail (Cortunix cortunix japonica)

TL;DR: It is demonstrated that 5,5'-dithiobis(2-nitrobenzoate) - DTNB - reacts with only CysF9[93]beta and CysB5[23]beta among the multiple sulfhydryl groups of the major and minor hemoglobins of the Japanese quail (Cortunix cortunix japonica).
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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