Davis D G, Charache S, Ho C
Proc Natl Acad Sci U S A. 1969 Aug;63(4):1403-9. doi: 10.1073/pnas.63.4.1403.
Nuclear magnetic resonance spectroscopy (100-MHz proton) was used to study the low-spin (S = 1/2) azide derivatives of human adult (alpha(2)beta(2)), human fetal (alpha(2)gamma(2)), Zürich (alpha(2)beta(2) (63 His --> Arg)), and horse (alpha(2)'beta(2)') methemoglobins, as well as whale metmyoglobin in 0.1 M deuterated phosphate at pD 7 and at 31 degrees C. The experimental results indicate that the azide-bound heme groups of the alpha- and beta-chains in human adult methemoglobin and of the alpha- and gamma-chains in fetal methemoglobin are not equivalent. The affinity of the beta- or gamma-chain for azide ion appears larger than that of the alpha-chain. The nuclar magnetic resonance spectrum of hemoglobin Zürich shows that the environment of the azide-heme complex in the abnormal beta-chain is altered by the substitution of arginine for histidine in the beta-63 position, while the alpha-heme environment remains unaffected.
利用核磁共振光谱法（100兆赫质子）研究了成人（α₂β₂）、胎儿（α₂γ₂）、苏黎世变体（α₂β₂（63位组氨酸→精氨酸））和马（α₂'β₂'）高铁血红蛋白的低自旋（S = 1/2）叠氮衍生物，以及在pD 7和31℃的0.1 M氘代磷酸盐中的鲸肌红蛋白。实验结果表明，成人高铁血红蛋白α链和β链以及胎儿高铁血红蛋白α链和γ链中与叠氮结合的血红素基团并不等同。β链或γ链对叠氮离子的亲和力似乎大于α链。苏黎世血红蛋白的核磁共振光谱表明，β-63位组氨酸被精氨酸取代改变了异常β链中叠氮-血红素复合物的环境，而α-血红素环境未受影响。
