Ohms J P, Hagenmaier H, Hayes M B, Cohen J S
Biochemistry. 1979 Apr 17;18(8):1599-602. doi: 10.1021/bi00575a034.
Proton NMR titration curves of the histidine Cepsilon-H resonances of the deoxy and oxy forms of human, horse, and sperm whale myoglobins (Mb) were determined and compared with the results for the met and azide forms. One extra titrating resonance (H-8) was observed for each deoxy-Mb compared with the corresponding met-Mb, and a further extra resonance (H-9) was observed for the oxy-Mb form. These resonances correspond to the two additional resonances previously described for azide-Mb [Hayes, M., Hagenmaier, H., & Cohen, J. S. (1975) J. Biol. Chem. 250, 7461--7472]. This new evidence prompts us to reassign these resonances to the near-heme histidine residues.
测定了人、马和抹香鲸肌红蛋白（Mb）的脱氧形式和氧合形式中组氨酸Cε-H共振的质子核磁共振滴定曲线，并与高铁形式和叠氮形式的结果进行了比较。与相应的高铁肌红蛋白相比，每种脱氧肌红蛋白都观察到一个额外的滴定共振峰（H-8），而氧合肌红蛋白形式还观察到另一个额外的共振峰（H-9）。这些共振峰对应于先前在叠氮肌红蛋白中描述的另外两个共振峰[海斯，M.，哈根迈尔，H.，&科恩，J.S.（1975年）《生物化学杂志》250，7461 - 7472]。这一新证据促使我们将这些共振峰重新归属于近血红素组氨酸残基。
