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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

The kinetics of carbon monoxide binding to partially reduced methemoglobin

TL;DR: Experiments with horse heart metmyoglobin show that the pulse radiolysis technique used to study the kinetics of the CO binding to partially reduced methemoglobin gives results which are in good agreement with those obtained by other methods.
Journal ArticleDOI

Contribution of alpha140Tyr and beta37Trp to the near-UV CD spectra on quaternary structure transition of human hemoglobin A.

TL;DR: The results indicate that the other aromatic amino acid residues, alpha42Tyr and beta145Tyr, at the alpha1beta2 interface, are also responsible for the change of the CD band upon the R-->T transition of Hb A.
Journal ArticleDOI

Circular dichroism as a probe of the allosteric R⇄T transformation in hemoglobins and modified hemoglobins

TL;DR: The circular dichroism in the 280 nm region is shown to be a useful diagnostic tool for chemical agents that affect the R⇄T allosteric transformation.
Journal ArticleDOI

Effect of organic phosphates on the sulfhydryl reactivities of oxyhemoglobins A and S.

TL;DR: The beta 93 sulfhydryl groups of oxyhemoglobins A and S display a difference in reactivity with 5,5'-dithiobis-2-nitrobenzoic acid and this difference arises from differences in tertiary structure in the vicinity of the beta 93 site, indicating that the structure at the organic phosphate binding site is different in the two oxyhemogobins.
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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