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
Differences in iron-fluoride bonding between the isolated subunits of human methemoglobin fluoride and sperm whale metmyoglobin fluoride as measured by resonance Raman spectroscopy.
TL;DR: The data are interpreted to indicate that the effect of the R leads to T conversion in HbIIIF is to perturb heme macrocycle conformation without altering the heme out-of-plane iron distance or the Fe-F bond length.
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Circular dichroism and spin-label studies of carp hemoglobin
TL;DR: In this paper, a circular dichroism (c.d.) spectra was obtained for deoxy, oxy, carboxy, nitrosyl, aquomet and azidomet derivatives of carp hemoglobin.
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Organic phosphate-binding groups electrostatically linked to the reactivity of the Cys F9 [93]β sulfhydryl group of haemoglobin
TL;DR: The complex pH-dependence profile of stripped haemoglobin quantitatively is analysed quantitatively by assuming that there is an electrostatic interaction between the sulfhydryl and the cationic groups.
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The cooperative interaction of aniline with methemoglobin.
John J. Mieyal,Linda S. Freeman +1 more
TL;DR: The observed spectral changes relfected conversion of high-spin aquomethemoglobin to the low-spin aniline complex and indicated that anilines bound cooperatively, which is unusual, since most ligand-methemoglobin interactions show n = 1.2.
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Critical redox and allosteric aspects of nitric oxide interactions with hemoglobin.
TL;DR: Recent reports concerning the redox and allosteric aspects of NO/Hb interactions that have advanced the authors' understanding of the physiological significance of NO binding to heme groups and of reactions promoting formation of S-nitrosated Hb (SNO-Hb).
References
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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.