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. 1969 Aug;63(4):1403–1409. doi: 10.1073/pnas.63.4.1403

NUCLEAR MAGNETIC RESONANCE STUDIES OF HEMOGLOBINS, III. EVIDENCE FOR THE NONEQUIVALENCE OF α- AND β-CHAINS IN AZIDE DERIVATIVES OF METHEMOGLOBINS*

Donald G Davis 1, Samuel Charache 1,†, Chien Ho 1
PMCID: PMC223479  PMID: 5260944

Abstract

Nuclear magnetic resonance spectroscopy (100-MHz proton) was used to study the low-spin (S = 1/2) azide derivatives of human adult (α2β2), human fetal (α2γ2), Zürich (α2β263 His → Arg), and horse (α2′β2′) methemoglobins, as well as whale metmyoglobin in 0.1 M deuterated phosphate at pD 7 and at 31°C. The experimental results indicate that the azide-bound heme groups of the α- and β-chains in human adult methemoglobin and of the α- and γ-chains in fetal methemoglobin are not equivalent. The affinity of the β- or γ-chain for azide ion appears larger than that of the α-chain. The nuclar magnetic resonance spectrum of hemoglobin Zürich shows that the environment of the azide-heme complex in the abnormal β-chain is altered by the substitution of arginine for histidine in the β-63 position, while the α-heme environment remains unaffected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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