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
Temperature-jump method for determining the equilibrium constant of the iron spin states in human methaemoglobin A
TL;DR: Results obtained show that chemical modification with cystamine increases the binding affinity of methaemoglobin, and perturbs the spin equilibrium, which validates the temperature-jump method for Kspin determination.
Journal ArticleDOI
Ligand-induced conformational changes in spin labelmodified human hemoglobins and chains and their carboxypeptidase A-digested derivatives
Mirna McDonald,Mirna McDonald,Anna L. Tan-Wilson,Anna L. Tan-Wilson,Daniel J. Kosman,Daniel J. Kosman,Alice DeYoung,Alice DeYoung,Robert W. Noble,Robert W. Noble +9 more
TL;DR: Findings support the premise that the COOH-terminal end of the beta or gamma chain contributes, although possibly to different extents, to the spectral differences exhibited by both the spin-labeled hemoglobins and chains.
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Unusual temperature dependence of electron transfer rates in the hemoglobin reductase system
TL;DR: In this paper, the rate of electron transfer between the proteins metHb (III) (human) and cytochrome b 5su(II) (rat) was studied as a function of temperature.
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Inhibition of NADH-methemoglobin reductase by organic phosphates.
Karla J. Matteson,F. Taketa +1 more
TL;DR: It is suggested that the interaction of the organic phosphate with the enzyme as well as with the substrate is significant in determining the overall rate of methemoglobin reduction.
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Change in surface properties of hemoglobin induced by heme reaction with O2 and CO
TL;DR: In this paper , the surface properties of hemoglobin bound to O2 (HbO2) or CO(HbCO) were investigated by ethanol precipitation, particle size analysis, and ζ potential measurements.
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.