光解碳monoxy-myoglobin 的晶体结构
I Schlichting1, J Berendzen, G N Phillips
1Department of Biophysics, Max Planck Institute for Medical Research, Heidelberg, Germany.
Nature
|October 27, 1994
概括
使用光的碳-一氧化-肌球蛋白 (MbCO) 的光解离产生一种不稳定的中间体. 射线晶体学揭示了CO的含量.
科学领域:
- 生物物理学的生物物理.
- 结构生物学 结构生物学
- 蛋白质动力学 蛋白质动力学
背景情况:
- 肌球蛋白 (Mb) 是一种关键的氧结合蛋白.
- 碳一氧化肌球蛋白 (MbCO) 是研究蛋白质反应的模型系统.
- MbCO的光解离释放CO,形成一个短暂的中间体.
研究的目的:
- 为了确定不稳定的MbCO中间体的结构.
- 为了阐明伴随着CO光解离在线红蛋白中的结构变化.
主要方法:
- 在液温度下的X射线晶体学.
- 高分辨率的结构确定 (1.5 Å).
主要成果:
- 光解离的CO位于海姆醇环C上方.
- 结构变化包括血"",铁位移,近接胺键压缩,F螺旋变异和远距离胺重新定位.
结论:
- 该研究提供了MbCO中间体的高分辨率快照.
- 在连接体光解离后显示出显著的蛋白质结构重组.
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