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盖廷从氧化合成酶中释放的NO.

Charlotte A Whited1, Jeffrey J Warren, Katherine D Lavoie

  • 1Beckman Institute and Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.

Journal of the American Chemical Society
|December 14, 2011
PubMed
概括

我们研究了来自Geobacillus stearothermophilus氧化合成酶 (gsNOS) 的氧化 (NO) 释放. 突变特定位置显示,位置223和134都充当了门,控制了NO的逃逸.

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科学领域:

  • 生物化学 生物化学
  • 酶学 是一种酶学.
  • 分子生物学分子生物学

背景情况:

  • 氧化合成酶 (NOS) 是生物系统中的关键酶.
  • 以前的研究表明,在哺乳动物NOS中释放氧化 (NO) 的关门机制.
  • 细菌NOS的结构和功能,如Geobacillus stearothermophilus NOS (gsNOS),对于NO释放动态的理解较少.

研究的目的:

  • 为了研究从野生类型的gsNOS中逃出的NO的动力学.
  • 为了确定特定的氨基酸残留物 (位置223和134) 在调节gsNOS的NO释放中的作用.
  • 将gsNOS的NO释放率与已知的哺乳动物NOS酶进行比较.

主要方法:

  • 停止流动UV-VIS光谱法用于监测反应.
  • 在野生型gsNOS和特定突变 (H134S,I223V,H134S/I223V) 上进行了动力实验.
  • 通过将减少的酶/N-基-l-氨酸复合物与空气缓冲剂混合来启动反应.

主要成果:

  • 野生类型的gsNOS在特征的NOS酶中表现出最慢的NO释放率.
  • 在位置223和134的突变显著增加了NO的逃逸率.
  • 双重突变 (H134S/I223V) 的NO释放率与最快的哺乳动物NOS酶相美.
  • 在位置223和134的绝缘阻碍被确定为阻碍NO释放的关键因素.

结论:

  • 在gsNOS中,位置223和134都充当控制NO排放的关键门.
  • 调节这些门残留物可以大大改变NO释放动力学.
  • 了解这些关门机制,可以深入了解不同物种的NOS酶功能和调节.