Near-heme histidine residues of deoxy- and oxymyoglobins.
Near-heme histidine residues of deoxy- and oxymyoglobins.
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脱氧肌红蛋白和氧合肌红蛋白的近血红素组氨酸残基。
DOI：
10.1021/bi00575a034
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发表时间：
1979
期刊：
影响因子：
2.9
通讯作者：
J. Cohen
中科院分区：
文献类型：
--
作者：
J. Ohms;H. Hagenmaier;M. Hayes;J. Cohen
测定了人、马和抹香鲸肌红蛋白 (Mb) 脱氧和氧形式的组氨酸 Cepsilon-H 共振的质子 NMR 滴定曲线，并与甲硫氨酸和叠氮化物形式的结果进行了比较。与相应的met-Mb相比，每种脱氧-Mb观察到一个额外的滴定共振(H-8)，并且对于氧-Mb形式观察到进一步的额外共振(H-9)。这些共振对应于先前描述的叠氮化物-Mb 的两个附加共振 [Hayes, M., Hagenmaier, H., & Cohen, J. S. (1975) J. Biol.化学。 250, 7461--7472]。这一新证据促使我们将这些共振重新分配给接近血红素的组氨酸残基。
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.